Publications

Publications

Selected publications

Selected publications

REVIEWS

James EI, Murphree TA, Vorauer C, Engen JR, and Guttman M. (2022). Advances in Hydrogen/Deuterium exchange mass spectrometry and the pursuit of challenging biological systems. Chem. Rev. 122(8), 7562-7623.  DOI: 10.1021/acs.chemrev.1c00279. Pubmed: 34493042.

Engen JR, Botzanowski T, Peterle D, Georgescauld F, and Wales TE. (2021). Developments in Hydrogen/Deuterium Exchange Mass Spectrometry. Anal. Chem. 93(1), 567-582. DOI: 10.1021/acs.analchem.0c04281. Pubmed: 33112590.

Engen JR, and Komives EA. (2020). Complementarity of Hydrogen/Deuterium Exchange Mass Spectrometry and Cryo-Electron Microscopy. Trends Biochem. Sci. 45, 906-918. DOI: 10.1016/j.tibs.2020.05.005. Pubmed: 32487353.

Georgescauld F, Wales TE, and Engen JR. (2019). Hydrogen deuterium exchange mass spectrometry applied to chaperones and chaperone-assisted protein folding. Expert Rev. Proteomics 16, 613-625. DOI: 10.1080/14789450.2019.1633920. Pubmed: 31215268.

Harrison RA, and Engen JR. (2016). Conformational insight into multi-protein signaling assemblies by hydrogen-deuterium exchange mass spectrometry. Curr. Opin. Struct. Biol. 41, 187-193. DOI: 10.1016/j.sbi.2016.08.003. Pubmed: 27552080.

Engen JR, and Wales TE. (2015). Analytical Aspects of Hydrogen Exchange Mass Spectrometry. Annu. Rev. Anal. Chem. (Palo Alto Calif.) 8, 127-148. DOI: 10.1146/annurev-anchem-062011-143113. Pubmed: 26048552.

HDX MS METHODS

Peterle D, Depice D, Wales TE, and Engen JR. (2023).  Increase the flow rate and improve hydrogen deuterium exchange mass spectrometry.  J. Chromatogr. A 1689, 463742. DOI: 10.1016/j.chroma.2022.463742. Pubmed: 36586285.

Peterle D, Wales TE, and Engen JR. (2022). Simple and fast maximally deuterated control (maxD) preparation for hydrogen-deuterium exchange mass spectrometry. Anal. Chem. 94(28), 10142-10150. DOI: 10.1021/acs.analchem.2c01446. Pubmed: 35796687.

Kochert BA, Iacob RE, Wales TE, Makriyannis A, and Engen JR. (2018). Hydrogen-Deuterium Exchange Mass Spectrometry to Study Protein Complexes. Methods Mol. Biol. 1764, 153-171. DOI: 10.1007/978-1-4939-7759-8_10. Pubmed: 29605914.

Wales TE, Fadgen KE, Eggertson MJ, and Engen JR. (2017). Subzero Celsius separations in three-zone temperature controlled hydrogen deuterium exchange mass spectrometry. J. Chromatogr. A 1523, 275-282. DOI: 10.1016/j.chroma.2017.05.067. Pubmed: 28596009.

TYROSINE KINASES

Joseph RE, Amatya N, Fulton DB, Engen JR, Wales TE, and Andreotti A. (2020). Differential impact of BTK active site inhibitors on the conformational state of full-length BTK. eLife 9, e60470. DOI: 10.7554/eLife.60470. Pubmed: 33226337.

Amatya N, Wales TE, Kwon A, Yeung W, Joseph RE, Fulton DB, Kannan N, Engen JR, and Andreotti AH. (2019). Lipid-targeting pleckstrin homology domain turns its autoinhibitory face toward the TEC kinases. Proc. Natl. Acad. Sci. U. S. A. 116, 21539-21544. DOI: 10.1073/pnas.1907566116. Pubmed: 31591208.

Shen K, Moroco JA, Patel RK, Shi H, Engen JR, Dorman HR, and Smithgall TE. (2018). The Src family kinase Fgr is a transforming oncoprotein that functions independently of SH3-SH2 domain regulation. Sci. Signal 11(553), eaat5916. DOI: 10.1126/scisignal.aat5916. Pubmed: 30352950.

Badger J, Grover P, Shi H, Panjarian SB, Engen JR, Smithgall TE, and Makowski L. (2016). c-Abl Tyrosine Kinase Adopts Multiple Active Conformational States in Solution. Biochemistry 55, 3251-3260. DOI: 10.1021/acs.biochem.6b00202. Pubmed: 27166638.

PROTEIN FOLDING

Ji Z, Li H, Peterle D, Paulo JA, Ficarro SB, Wales TE, Marto JA, Gygi SP, Engen JR, and Rapoport TA. (2022). Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase. Mol. Cell 82(3), 570-584.E8. DOI: 10.1016/j.molcel.2021.11.033. Pubmed: 34951965.

Shi Y, Chen X, Elsasser S, Stocks BB, Tian G, Lee BH, Shi Y, Zhang N, de Poot SA, Tuebing F, Sun S, Vannoy J, Tarasov SG, Engen JR, Finley D, and Walters KJ. (2016). Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome. Science 351(6275), aad9421. DOI: 10.1126/science.aad9421. Pubmed: 26912900.

Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, and Hartl FU. (2014). GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding. Cell 157, 922-934. DOI: 10.1016/j.cell.2014.03.038. Pubmed: 24813614.

APOPTOSIS

Bloch NB, Wales TE, Prew MS, Levy HR, Engen JR, and Walensky LD. (2021). The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core. Nat. Commun. 12(1), 4932. DOI: 10.1038/s41467-021-25200-7. Pubmed: 34389733.

Hauseman ZJ, Harvey EP, Newman CE, Wales TE, Bucci JC, Mintseris J, Schweppe DK, David L, Fan L, Cohen DT, Herce HD, Mourtada R, Ben-Nun Y, Bloch NB, Hansen SB, Wu H, Gygi SP, Engen JR, and Walensky LD. (2020). Homogeneous Oligomers of Pro-apoptotic BAX Reveal Structural Determinants of Mitochondrial Membrane Permeabilization. Mol. Cell 79, 68-83 e67. DOI: 10.1016/j.molcel.2020.05.029. Pubmed: 32533918.

Lee S, Wales TE, Escudero S, Cohen DT, Luccarelli J, Gallagher CG, Cohen NA, Huhn AJ, Bird GH, Engen JR, and Walensky LD. (2016). Allosteric inhibition of antiapoptotic MCL-1. Nat. Struct. Mol. Biol. 23, 600-607. DOI: 10.1038/nsmb.3223. Pubmed: 27159560.

PLASMA & MEMBRANE PROTEINS

Peterle D, Klimtchuk ES, Wales TE, Georgescauld F, Connors LH, Engen JR & Gursky O. (2021). A conservative point mutation in a dynamic antigen-binding loop of human immunoglobulin λ6 light chain promotes pathologic amyloid formation. J. Mol. Biol. 433(24), 167310. DOI: 10.1016/j.jmb.2021.167310. Pubmed: 34678302.

Frame NM, Kumanan M, Wales TE, Bandara A, Fandrich M, Straub JE, Engen JR, and Gursky O. (2020). Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A. J. Mol. Biol. 432, 1978-1995. DOI: 10.1016/j.jmb.2020.01.029. Pubmed: 32035904.

Wilson CJ, Das M, Jayaraman S, Gursky O, and Engen JR. (2018). Effects of Disease-Causing Mutations on the Conformation of Human Apolipoprotein A-I in Model Lipoproteins. Biochemistry 57, 4583-4596. DOI: 10.1021/acs.biochem.8b00538. Pubmed: 30004693.

All publications

All publications

Find publications in:

Klimtchuk ES, Peterle D, Bullitt EA, Connors LH, Engen JR, and Gursky O. (2023). Role of complementarity-determining regions 1 and 3 in pathologic amyloid formation by human immunoglobulin κ1 light chains. Under review, bioRxiv: 2023.02.01.526662.

Wales TE, Pajak A, Roeselova A, Shivakumaraswamy S, Howell S, Hartl FU, Engen JR, and Balchin D. (2023). Resolving chaperone-assisted protein folding on the ribosome at the peptide level. Under review, bioRxiv: 2022.09.23.509153.

Peterle D, Depice D, Wales TE, and Engen JR. (2023).  Increase the flow rate and improve hydrogen deuterium exchange mass spectrometry.  J. Chromatogr. A 1689, 463742. DOI: 10.1016/j.chroma.2022.463742. Pubmed: 36586285.

Du S, Alvarado JJ, Wales TE, Moroco JA, Engen JR, and Smithgall TE. (2022). ATP-site inhibitors induce unique conformations of the acute myeloid leukemia-associated Src-family kinase, Fgr.  Structure 30(11), 1508-1517. DOI: 10.1016/j.str.2022.08.008. Pubmed: 36115344.

Su Y, Iacob RE, Li J, Engen JR, and Springer TA. (2022). Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change.  J. Biol. Chem. 298(9), 102323. DOI: 10.1016/j.jbc.2022.102323. Pubmed: 35931112.

Peterle D, Wales TE, and Engen JR. (2022). Simple and fast maximally deuterated control (maxD) preparation for hydrogen-deuterium exchange mass spectrometry. Anal. Chem. 94(28), 10142-10150. DOI: 10.1021/acs.analchem.2c01446. Pubmed: 35796687.

Prew MS, Camara CM, Botzanowski T, Moroco JA, Bloch NB, Levy HR, Seo H-S, Dhe-Paganon S, Bird GH, Herce HD, Gygi MA, Escudero S, Wales TE, Engen JR, and Walensky LD. (2022).  Structural basis for defective membrane targeting of mutant enzyme in human VLCAD deficiency. Nat. Commun. 13, 3669.  DOI: 10.1038/s41467-022-31466-2. Pubmed: 35760926.

Bonazza K, Iacob RE, Hudson NE, Li J, Lu C, Engen JR, and Springer TA. (2022). Von Willebrand factor A1 domain stability and affinity for GPIbα are differentially regulated by its O-glycosylated N- and C-linker. eLife 11, e75760. DOI: 10.7554/eLife.75760. Pubmed: 35532124.

James EI, Murphree TA, Vorauer C, Engen JR, and Guttman M. (2022).  Advances in Hydrogen/Deuterium exchange mass spectrometry and the pursuit of challenging biological systems. Chem. Rev. 122(8), 7562-7623.  10.1021/acs.chemrev.1c00279. Pubmed: 34493042.

Hung KY, Klumpe S, Eisele MR, Elsasser S, Tian G, Sun S, Moroco JA, Cheng TC, Joshi T, Seibel T, Van Dalen D, Feng X-H, Lu Y, Ovaa H, Engen JR, Lee B-H, Rudack T, Sakata E, and Finley D. (2022). Allosteric control of Ubp6 and the proteasome via a bidirectional switch.  Nat. Commun. 13, 838. DOI: 10.1038/s41467-022-28186-y. Pubmed: 35149681.

Le VQ, Iacob RE, Zhao B, Su Y, Tian Y, Toohey C, Engen JR, and Springer TA. (2022). Protection of the prodomain α1-helix correlates with latency in the transforming growth factor-β family.  J. Mol. Biol. 434(5), 167439. DOI: 10.1016/j.jmb.2021.167439. Pubmed: 34990654.

Joseph RE, Lowe J, Fulton DB, Engen JR, Wales TE, and Andreotti AH. (2022). The conformational state of BTK substrate PLCγ contributes to Ibrutinib resistance.  J. Mol. Biol. 434(5), 167422. DOI: 10.1016/j.jmb.2021.167422. Pubmed: 34954235.

Ji Z, Li H, Peterle D, Paulo JA, Ficarro SB, Wales TE, Marto JA, Gygi SP, Engen JR, and Rapoport TA. (2022). Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase.  Mol. Cell 82(3), 570-584.E8. DOI: 10.1016/j.molcel.2021.11.033. Pubmed: 34951965.

Peterle D, Klimtchuk ES, Wales TE, Georgescauld F, Connors LH, Engen JR, and Gursky O. (2021). A conservative point mutation in a dynamic antigen-binding loop of human immunoglobulin λ6 light chain promotes pathologic amyloid formation. J. Mol. Biol. 433(24), 167310. DOI: 10.1016/j.jmb.2021.167310. Pubmed: 34678302.

Bloch NB, Wales TE, Prew MS, Levy HR, Engen JR, and Walensky LD. (2021).  The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core.  Nat. Commun. 12(1), 4932. DOI: 10.1038/s41467-021-25200-7.  Pubmed: 34389733.

Newman JA, Gavard AE, Lieb S, Ravichandran MC, Hauer K, Werni P, Geist L, Bottcher J, Engen JR, Rumpel K, Samwer M, Petronczki M, and Gileadi O. (2021). Structure of the helicase core of Werner helicase, a key target in microsatellite instability cancers. Life Sci. Alliance 4(1), e202000795. DOI: 10.26508/lsa.202000795. Pubmed: 33199508.

Engen JR, Botzanowski T, Peterle D, Georgescauld F, and Wales TE. (2021). Developments in Hydrogen/Deuterium Exchange Mass Spectrometry. Anal. Chem. 93(1), 567-582. DOI: 10.1021/acs.analchem.0c04281. Pubmed: 33112590.

Joseph RE, Amatya N, Fulton DB, Engen JR, Wales TE, and Andreotti A. (2020). Differential impact of BTK active site inhibitors on the conformational state of full-length BTK. eLife 9, e60470. DOI: 10.7554/eLife.60470. Pubmed: 33226337.

Staudt RP, Alvarado JJ, Emert-Sedlak LA, Shi H, Shu ST, Wales TE, Engen JR, and Smithgall TE. (2020). Structure, function, and inhibitor targeting of HIV-1 Nef-effector kinase complexes. J. Biol. Chem. 295, 15158-15171. DOI: 10.1074/jbc.REV120.012317. Pubmed: 32862141.

Cathcart AM, Bird GH, Wales TE, Herce HD, Harvey EP, Hauseman ZJ, Newman CE, Adhikary U, Prew MS, Oo T, Lee S, Engen JR, and Walensky LD. (2020). Targeting a helix-in-groove interaction between E1 and E2 blocks ubiquitin transfer. Nat. Chem. Biol. 16, 1218-1226. DOI: 10.1038/s41589-020-0625-7. Pubmed: 32807965.

Vetter CJ, Thorn DC, Wheeler SG, Mundorff CC, Halverson KA, Wales TE, Shinde UP, Engen JR, David LL, Carver JA, and Lampi KJ. (2020). Cumulative deamidations of the major lens protein gammaS-crystallin increase its aggregation during unfolding and oxidation. Protein Sci. 29, 1945-1963. DOI: 10.1002/pro.3915. Pubmed: 32697405.

Korshavn KJ, Wales TE, Bird GH, Engen JR, and Walensky LD. (2020). A redox switch regulates the structure and function of anti-apoptotic BFL-1. Nat. Struct. Mol. Biol. 27, 781-789. DOI: 10.1038/s41594-020-0458-9. Pubmed: 32661419.

Hauseman ZJ, Harvey EP, Newman CE, Wales TE, Bucci JC, Mintseris J, Schweppe DK, David L, Fan L, Cohen DT, Herce HD, Mourtada R, Ben-Nun Y, Bloch NB, Hansen SB, Wu H, Gygi SP, Engen JR, and Walensky LD. (2020). Homogeneous Oligomers of Pro-apoptotic BAX Reveal Structural Determinants of Mitochondrial Membrane Permeabilization. Mol. Cell 79, 68-83 e67. DOI: 10.1016/j.molcel.2020.05.029. Pubmed: 32533918.

Engen JR, and Komives EA. (2020). Complementarity of Hydrogen/Deuterium Exchange Mass Spectrometry and Cryo-Electron Microscopy. Trends Biochem. Sci. 45, 906-918. DOI: 10.1016/j.tibs.2020.05.005. Pubmed: 32487353.

Harvey EP, Hauseman ZJ, Cohen DT, Rettenmaier TJ, Lee S, Huhn AJ, Wales TE, Seo HS, Luccarelli J, Newman CE, Guerra RM, Bird GH, Dhe-Paganon S, Engen JR, Wells JA, and Walensky LD. (2020). Identification of a Covalent Molecular Inhibitor of Anti-apoptotic BFL-1 by Disulfide Tethering. Cell Chem. Biol. 27, 647-656 e646. DOI: 10.1016/j.chembiol.2020.04.004. Pubmed: 32413285.

Ben-Nun Y, Seo HS, Harvey EP, Hauseman ZJ, Wales TE, Newman CE, Cathcart AM, Engen JR, Dhe-Paganon S, and Walensky LD. (2020). Identification of a Structural Determinant for Selective Targeting of HDMX. Structure 28, 847-857 e845. DOI: 10.1016/j.str.2020.04.011. Pubmed: 32359398.

Bird GH, Fu A, Escudero S, Godes M, Opoku-Nsiah K, Wales TE, Cameron MD, Engen JR, Danial NN, and Walensky LD. (2020). Hydrocarbon-Stitched Peptide Agonists of Glucagon-Like Peptide-1 Receptor. ACS Chem. Biol. 15, 1340-1348. DOI: 10.1021/acschembio.0c00308. Pubmed: 32348108.

Schauer NJ, Liu X, Magin RS, Doherty LM, Chan WC, Ficarro SB, Hu W, Roberts RM, Iacob RE, Stolte B, Giacomelli AO, Perera S, McKay K, Boswell SA, Weisberg EL, Ray A, Chauhan D, Dhe-Paganon S, Anderson KC, Griffin JD, Li J, Hahn WC, Sorger PK, Engen JR, Stegmaier K, Marto JA, and Buhrlage SJ. (2020). Selective USP7 inhibition elicits cancer cell killing through a p53-dependent mechanism. Sci. Rep. 10, 5324. DOI: 10.1038/s41598-020-62076-x. Pubmed: 32210275.

Cohen DT, Wales TE, McHenry MW, Engen JR, and Walensky LD. (2020). Site-Dependent Cysteine Lipidation Potentiates the Activation of Proapoptotic BAX. Cell Rep. 30, 3229-3239. DOI: 10.1016/j.celrep.2020.02.057. Pubmed: 32160532.

Fleischhacker AS, Gunawan AL, Kochert BA, Liu L, Wales TE, Borowy MC, Engen JR, and Ragsdale SW. (2020). The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation. J. Biol. Chem. 295, 5177-5191. DOI: 10.1074/jbc.RA120.012803. Pubmed: 32152224.

Kardon JR, Moroco JA, Engen JR, and Baker TA. (2020). Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding. eLife 9, e54387. DOI: 10.7554/eLife.54387. Pubmed: 32091391.

Makarov AA, Iacob RE, Pirrone GF, Rodriguez-Granillo A, Joyce L, Mangion I, Moore JC, Sherer EC, and Engen JR. (2020). Combination of HDX-MS and in silico modeling to study enzymatic reactivity and stereo-selectivity at different solvent conditions. J. Pharm. Biomed. Anal. 182, 113141. DOI: 10.1016/j.jpba.2020.113141. Pubmed: 32036298.

Frame NM, Kumanan M, Wales TE, Bandara A, Fandrich M, Straub JE, Engen JR, and Gursky O. (2020). Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A. J. Mol. Biol. 432, 1978-1995. DOI: 10.1016/j.jmb.2020.01.029. Pubmed: 32035904.

Manthei KA, Patra D, Wilson CJ, Fawaz MV, Piersimoni L, Shenkar JC, Yuan W, Andrews PC, Engen JR, Schwendeman A, Ohi MD, and Tesmer JJG. (2020). Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles. Commun. Biol. 3, 28. DOI: 10.1038/s42003-019-0749-z. Pubmed: 31942029.

Eggertson MJ, Fadgen K, Engen JR, and Wales TE. (2020). Considerations in the Analysis of Hydrogen Exchange Mass Spectrometry Data. Methods Mol. Biol. 2051, 407-435. DOI: 10.1007/978-1-4939-9744-2_18. Pubmed: 31552640.

Wang J, Su Y, Iacob RE, Engen JR, and Springer TA. (2019). General structural features that regulate integrin affinity revealed by atypical alphaVbeta8. Nat. Commun. 10, 5481. DOI: 10.1038/s41467-019-13248-5. Pubmed: 31792290.

Amatya N, Wales TE, Kwon A, Yeung W, Joseph RE, Fulton DB, Kannan N, Engen JR, and Andreotti AH. (2019). Lipid-targeting pleckstrin homology domain turns its autoinhibitory face toward the TEC kinases. Proc. Natl. Acad. Sci. U. S. A. 116, 21539-21544. DOI: 10.1073/pnas.1907566116. Pubmed: 31591208.

Mourtada R, Herce HD, Yin DJ, Moroco JA, Wales TE, Engen JR, and Walensky LD. (2019). Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice. Nat. Biotechnol. 37, 1186-1197. DOI: 10.1038/s41587-019-0222-z. Pubmed: 31427820.

Bera AK, Lu J, Wales TE, Gondi S, Gurbani D, Nelson A, Engen JR, and Westover KD. (2019). Structural basis of the atypical activation mechanism of KRAS(V14I). J. Biol. Chem. 294, 13964-13972. DOI: 10.1074/jbc.RA119.009131. Pubmed: 31341022.

Masson GR, Burke JE, Ahn NG, Anand GS, Borchers C, Brier S, Bou-Assaf GM, Engen JR, Englander SW, Faber J, Garlish R, Griffin PR, Gross ML, Guttman M, Hamuro Y, Heck AJR, Houde D, Iacob RE, Jorgensen TJD, Kaltashov IA, Klinman JP, Konermann L, Man P, Mayne L, Pascal BD, Reichmann D, Skehel M, Snijder J, Strutzenberg TS, Underbakke ES, Wagner C, Wales TE, Walters BT, Weis DD, Wilson DJ, Wintrode PL, Zhang Z, Zheng J, Schriemer DC, and Rand KD. (2019). Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nat. Methods 16, 595-602. DOI: 10.1038/s41592-019-0459-y. Pubmed: 31249422.

Twomey EC, Ji Z, Wales TE, Bodnar NO, Ficarro SB, Marto JA, Engen JR, and Rapoport TA. (2019). Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding. Science 365(6452), eaax1033. DOI: 10.1126/science.aax1033. Pubmed: 31249135.

Georgescauld F, Wales TE, and Engen JR. (2019). Hydrogen deuterium exchange mass spectrometry applied to chaperones and chaperone-assisted protein folding. Expert Rev. Proteomics 16, 613-625. DOI: 10.1080/14789450.2019.1633920. Pubmed: 31215268.

Poulin EJ, Bera AK, Lu J, Lin YJ, Strasser SD, Paulo JA, Huang TQ, Morales C, Yan W, Cook J, Nowak JA, Brubaker DK, Joughin BA, Johnson CW, DeStefanis RA, Ghazi PC, Gondi S, Wales TE, Iacob RE, Bogdanova L, Gierut JJ, Li Y, Engen JR, Perez-Mancera PA, Braun BS, Gygi SP, Lauffenburger DA, Westover KD, and Haigis KM. (2019). Tissue-Specific Oncogenic Activity of KRAS(A146T). Cancer Discov. 9, 738-755. DOI: 10.1158/2159-8290.CD-18-1220. Pubmed: 30952657.

Kochert BA, Fleischhacker AS, Wales TE, Becker DF, Engen JR, and Ragsdale SW. (2019). Dynamic and structural differences between heme oxygenase-1 and -2 are due to differences in their C-terminal regions. J. Biol. Chem. 294, 8259-8272. DOI: 10.1074/jbc.RA119.008592. Pubmed: 30944174.

Dautant A, Henri J, Wales TE, Meyer P, Engen JR, and Georgescauld F. (2019). Remodeling of the Binding Site of Nucleoside Diphosphate Kinase Revealed by X-ray Structure and H/D Exchange. Biochemistry 58, 1440-1449. DOI: 10.1021/acs.biochem.8b01308. Pubmed: 30785730.

Shen K, Moroco JA, Patel RK, Shi H, Engen JR, Dorman HR, and Smithgall TE. (2018). The Src family kinase Fgr is a transforming oncoprotein that functions independently of SH3-SH2 domain regulation. Sci. Signal 11(553), eaat5916. DOI: 10.1126/scisignal.aat5916. Pubmed: 30352950.

Feng J, Dong X, Pinello J, Zhang J, Lu C, Iacob RE, Engen JR, Snell WJ, and Springer TA. (2018). Fusion surface structure, function, and dynamics of gamete fusogen HAP2. eLife 7, e39772. DOI: 10.7554/eLife.39772. Pubmed: 30281023.

Wilson CJ, Das M, Jayaraman S, Gursky O, and Engen JR. (2018). Effects of Disease-Causing Mutations on the Conformation of Human Apolipoprotein A-I in Model Lipoproteins. Biochemistry 57, 4583-4596. DOI: 10.1021/acs.biochem.8b00538. Pubmed: 30004693.

Bodnar NO, Kim KH, Ji Z, Wales TE, Svetlov V, Nudler E, Engen JR, Walz T, and Rapoport TA. (2018). Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat. Struct. Mol. Biol. 25, 616-622. DOI: 10.1038/s41594-018-0085-x. Pubmed: 29967539.

de Wispelaere M, Lian W, Potisopon S, Li PC, Jang J, Ficarro SB, Clark MJ, Zhu X, Kaplan JB, Pitts JD, Wales TE, Wang J, Engen JR, Marto JA, Gray NS, and Yang PL. (2018). Inhibition of Flaviviruses by Targeting a Conserved Pocket on the Viral Envelope Protein. Cell Chem. Biol. 25, 1006-1016 e1008. DOI: 10.1016/j.chembiol.2018.05.011. Pubmed: 29937406.

Kochert BA, Iacob RE, Wales TE, Makriyannis A, and Engen JR. (2018). Hydrogen-Deuterium Exchange Mass Spectrometry to Study Protein Complexes. Methods Mol. Biol. 1764, 153-171. DOI: 10.1007/978-1-4939-7759-8_10. Pubmed: 29605914.

Escudero S, Zaganjor E, Lee S, Mill CP, Morgan AM, Crawford EB, Chen J, Wales TE, Mourtada R, Luccarelli J, Bird GH, Steidl U, Engen JR, Haigis MC, Opferman JT, and Walensky LD. (2018). Dynamic Regulation of Long-Chain Fatty Acid Oxidation by a Noncanonical Interaction between the MCL-1 BH3 Helix and VLCAD. Mol. Cell 69, 729-743 e727. DOI: 10.1016/j.molcel.2018.02.005. Pubmed: 29499131.

Le VQ, Iacob RE, Tian Y, McConaughy W, Jackson J, Su Y, Zhao B, Engen JR, Pirruccello-Straub M, and Springer TA. (2018). Tolloid cleavage activates latent GDF8 by priming the pro-complex for dissociation. EMBO J. 37, 384-397. DOI: 10.15252/embj.201797931. Pubmed: 29343545.

Moroco JA, Alvarado JJ, Staudt RP, Shi H, Wales TE, Smithgall TE, and Engen JR. (2018). Remodeling of HIV-1 Nef Structure by Src-Family Kinase Binding. J. Mol. Biol. 430, 310-321. DOI: 10.1016/j.jmb.2017.12.008. Pubmed: 29258818.

Lamberto I, Liu X, Seo HS, Schauer NJ, Iacob RE, Hu W, Das D, Mikhailova T, Weisberg EL, Engen JR, Anderson KC, Chauhan D, Dhe-Paganon S, and Buhrlage SJ. (2017). Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7. Cell Chem. Biol. 24, 1490-1500 e1411. DOI: 10.1016/j.chembiol.2017.09.003. Pubmed: 29056421.

Kerres N, Steurer S, Schlager S, Bader G, Berger H, Caligiuri M, Dank C, Engen JR, Ettmayer P, Fischerauer B, Flotzinger G, Gerlach D, Gerstberger T, Gmaschitz T, Greb P, Han B, Heyes E, Iacob RE, Kessler D, Kolle H, Lamarre L, Lancia DR, Lucas S, Mayer M, Mayr K, Mischerikow N, Muck K, Peinsipp C, Petermann O, Reiser U, Rudolph D, Rumpel K, Salomon C, Scharn D, Schnitzer R, Schrenk A, Schweifer N, Thompson D, Traxler E, Varecka R, Voss T, Weiss-Puxbaum A, Winkler S, Zheng X, Zoephel A, Kraut N, McConnell D, Pearson M, and Koegl M. (2017). Chemically Induced Degradation of the Oncogenic Transcription Factor BCL6. Cell Rep. 20, 2860-2875. DOI: 10.1016/j.celrep.2017.08.081. Pubmed: 28930682.

Joseph RE, Wales TE, Fulton DB, Engen JR, and Andreotti AH. (2017). Achieving a Graded Immune Response: BTK Adopts a Range of Active/Inactive Conformations Dictated by Multiple Interdomain Contacts. Structure 25, 1481-1494 e1484. DOI: 10.1016/j.str.2017.07.014. Pubmed: 28867612.

Bhat JY, Milicic G, Thieulin-Pardo G, Bracher A, Maxwell A, Ciniawsky S, Mueller-Cajar O, Engen JR, Hartl FU, Wendler P, and Hayer-Hartl M. (2017). Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase. Mol. Cell 67, 744-756 e746. DOI: 10.1016/j.molcel.2017.07.004. Pubmed: 28803776.

Lu J, Harrison RA, Li L, Zeng M, Gondi S, Scott D, Gray NS, Engen JR, and Westover KD. (2017). KRAS G12C Drug Development: Discrimination between Switch II Pocket Configurations Using Hydrogen/Deuterium-Exchange Mass Spectrometry. Structure 25, 1442-1448 e1443. DOI: 10.1016/j.str.2017.07.003. Pubmed: 28781083.

Chen TF, Sazinsky SL, Houde D, DiLillo DJ, Bird J, Li KK, Cheng GT, Qiu H, Engen JR, Ravetch JV, and Wittrup KD. (2017). Engineering Aglycosylated IgG Variants with Wild-Type or Improved Binding Affinity to Human Fc Gamma RIIA and Fc Gamma RIIIAs. J. Mol. Biol. 429, 2528-2541. DOI: 10.1016/j.jmb.2017.07.001. Pubmed: 28694069.

Pritz JR, Wachter F, Lee S, Luccarelli J, Wales TE, Cohen DT, Coote P, Heffron GJ, Engen JR, Massefski W, and Walensky LD. (2017). Allosteric sensitization of proapoptotic BAX. Nat. Chem. Biol. 13, 961-967. DOI: 10.1038/nchembio.2433. Pubmed: 28692068.

Chaikuad A, Filippakopoulos P, Marcsisin SR, Picaud S, Schroder M, Sekine S, Ichijo H, Engen JR, Takeda K, and Knapp S. (2017). Structures of PGAM5 Provide Insight into Active Site Plasticity and Multimeric Assembly. Structure 25, 1089-1099 e1083. DOI: 10.1016/j.str.2017.05.020. Pubmed: 28648608.

Wales TE, Fadgen KE, Eggertson MJ, and Engen JR. (2017). Subzero Celsius separations in three-zone temperature controlled hydrogen deuterium exchange mass spectrometry. J. Chromatogr. A 1523, 275-282. DOI: 10.1016/j.chroma.2017.05.067. Pubmed: 28596009.

Iacob RE, Engen JR, Krull IS (2017). Applicability of Hydrogen-Deuterium exchange in comparing conformations of innovator to biosimilar biopharmaceutical products. LC-GC 35(6), 382-390.

Dong X, Zhao B, Iacob RE, Zhu J, Koksal AC, Lu C, Engen JR, and Springer TA. (2017). Force interacts with macromolecular structure in activation of TGF-beta. Nature 542, 55-59. DOI: 10.1038/nature21035. Pubmed: 28117447.

Das M, Wilson CJ, Mei X, Wales T, Engen JR, and Gursky O. (2017). Structural stability and local dynamics in disease-causing mutants of human apolipoprotein a-I: what makes the protein amyloidogenic? Amyloid 24, 11-12. DOI: 10.1080/13506129.2016.1269737. Pubmed: 28042708.

Huang RY, Iacob RE, Krystek SR, Jin M, Wei H, Tao L, Das TK, Tymiak AA, Engen JR, and Chen G. (2017). Characterization of Aggregation Propensity of a Human Fc-Fusion Protein Therapeutic by Hydrogen/Deuterium Exchange Mass Spectrometry. J. Am. Soc. Mass Spectrom. 28, 795-802. DOI: 10.1007/s13361-016-1452-7. Pubmed: 27527097.

Harrison RA, Lu J, Carrasco M, Hunter J, Manandhar A, Gondi S, Westover KD, and Engen JR. (2016). Structural Dynamics in Ras and Related Proteins upon Nucleotide Switching. J. Mol. Biol. 428, 4723-4735. DOI: 10.1016/j.jmb.2016.10.017. Pubmed: 27751724.

Harrison RA, and Engen JR. (2016). Conformational insight into multi-protein signaling assemblies by hydrogen-deuterium exchange mass spectrometry. Curr. Opin. Struct. Biol. 41, 187-193. DOI: 10.1016/j.sbi.2016.08.003. Pubmed: 27552080.

Badger J, Grover P, Shi H, Panjarian SB, Engen JR, Smithgall TE, and Makowski L. (2016). c-Abl Tyrosine Kinase Adopts Multiple Active Conformational States in Solution. Biochemistry 55, 3251-3260. DOI: 10.1021/acs.biochem.6b00202. Pubmed: 27166638.

Lee S, Wales TE, Escudero S, Cohen DT, Luccarelli J, Gallagher CG, Cohen NA, Huhn AJ, Bird GH, Engen JR, and Walensky LD. (2016). Allosteric inhibition of antiapoptotic MCL-1. Nat. Struct. Mol. Biol. 23, 600-607. DOI: 10.1038/nsmb.3223. Pubmed: 27159560.

Wales TE, Poe JA, Emert-Sedlak L, Morgan CR, Smithgall TE, and Engen JR. (2016). Hydrogen Exchange Mass Spectrometry of Related Proteins with Divergent Sequences: A Comparative Study of HIV-1 Nef Allelic Variants. J. Am. Soc. Mass Spectrom. 27, 1048-1061. DOI: 10.1007/s13361-016-1365-5. Pubmed: 27032648.

Chopra N, Wales TE, Joseph RE, Boyken SE, Engen JR, Jernigan RL, and Andreotti AH. (2016). Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases. PLoS Comput. Biol. 12, e1004826. DOI: 10.1371/journal.pcbi.1004826. Pubmed: 27010561.

Shi Y, Chen X, Elsasser S, Stocks BB, Tian G, Lee BH, Shi Y, Zhang N, de Poot SA, Tuebing F, Sun S, Vannoy J, Tarasov SG, Engen JR, Finley D, and Walters KJ. (2016). Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome. Science 351(6275), aad9421. DOI: 10.1126/science.aad9421. Pubmed: 26912900.

Guttman M, Wales TE, Whittington D, Engen JR, Brown JM, and Lee KK. (2016). Tuning a High Transmission Ion Guide to Prevent Gas-Phase Proton Exchange During H/D Exchange MS Analysis. J. Am. Soc. Mass Spectrom. 27, 662-668. DOI: 10.1007/s13361-015-1330-8. Pubmed: 26810432.

Roberts JM, Tarafdar S, Joseph RE, Andreotti AH, Smithgall TE, Engen JR, and Wales TE. (2016). Dynamics of the Tec-family tyrosine kinase SH3 domains. Protein Sci. 25, 852-864. DOI: 10.1002/pro.2887. Pubmed: 26808198.

Das M, Wilson CJ, Mei X, Wales TE, Engen JR, and Gursky O. (2016). Structural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic? J. Mol. Biol. 428, 449-462. DOI: 10.1016/j.jmb.2015.10.029. Pubmed: 26562506.

Wales TE, Hochrein JM, Morgan CR, Emert-Sedlak LA, Smithgall TE, and Engen JR. (2015). Subtle Dynamic Changes Accompany Hck Activation by HIV-1 Nef and are Reversed by an Antiretroviral Kinase Inhibitor. Biochemistry 54, 6382-6391. DOI: 10.1021/acs.biochem.5b00875. Pubmed: 26440750.

Pirrone GF, Vernon BC, Kent MS, and Engen JR. (2015). Hydrogen Exchange Mass Spectrometry of Proteins at Langmuir Monolayers. Anal. Chem. 87, 7022-7029. DOI: 10.1021/acs.analchem.5b01724. Pubmed: 26134943.

Pirrone GF, Emert-Sedlak LA, Wales TE, Smithgall TE, Kent MS, and Engen JR. (2015). Membrane-Associated Conformation of HIV-1 Nef Investigated with Hydrogen Exchange Mass Spectrometry at a Langmuir Monolayer. Anal. Chem. 87, 7030-7035. DOI: 10.1021/acs.analchem.5b01725. Pubmed: 26133569.

Engen JR, and Wales TE. (2015). Analytical Aspects of Hydrogen Exchange Mass Spectrometry. Annu. Rev. Anal. Chem. (Palo Alto Calif.) 8, 127-148. DOI: 10.1146/annurev-anchem-062011-143113. Pubmed: 26048552.

Moroco JA, and Engen JR. (2015). Replication in bioanalytical studies with HDX MS: aim as high as possible. Bioanalysis 7, 1065-1067. DOI: 10.4155/bio.15.46. Pubmed: 26039804.

Marcsisin SR, Liptak C, Marineau J, Bradner JE, and Engen JR. (2015). Tag and Capture Flow Hydrogen Exchange Mass Spectrometry with a Fluorous-Immobilized Probe. Anal. Chem. 87, 6349-6356. DOI: 10.1021/acs.analchem.5b01220. Pubmed: 26023704.

Black WA, Stocks BB, Mellors JS, Engen JR, and Ramsey JM. (2015). Utilizing Microchip Capillary Electrophoresis Electrospray Ionization for Hydrogen Exchange Mass Spectrometry. Anal. Chem. 87, 6280-6287. DOI: 10.1021/acs.analchem.5b01179. Pubmed: 25992468.

Nevin P, Lu X, Zhang K, Engen JR, and Beuning PJ. (2015). Noncognate DNA damage prevents the formation of the active conformation of the Y-family DNA polymerases DinB and DNA polymerase kappa. FEBS J. 282, 2646-2660. DOI: 10.1111/febs.13304. Pubmed: 25899385.

Iacob RE, Krystek SR, Huang RY, Wei H, Tao L, Lin Z, Morin PE, Doyle ML, Tymiak AA, Engen JR, and Chen G. (2015). Hydrogen/deuterium exchange mass spectrometry applied to IL-23 interaction characteristics: potential impact for therapeutics. Expert Rev. Proteomics 12, 159-169. DOI: 10.1586/14789450.2015.1018897. Pubmed: 25711416.

Nevin P, Engen JR, and Beuning PJ. (2015). Steric gate residues of Y-family DNA polymerases DinB and pol kappa are crucial for dNTP-induced conformational change. DNA Repair (Amst) 29, 65-73. DOI: 10.1016/j.dnarep.2015.01.012. Pubmed: 25684709.

Barclay LA, Wales TE, Garner TP, Wachter F, Lee S, Guerra RM, Stewart ML, Braun CR, Bird GH, Gavathiotis E, Engen JR, and Walensky LD. (2015). Inhibition of Pro-apoptotic BAX by a noncanonical interaction mechanism. Mol. Cell 57, 873-886. DOI: 10.1016/j.molcel.2015.01.014. Pubmed: 25684204.

Pirrone GF, Iacob RE, and Engen JR. (2015). Applications of hydrogen/deuterium exchange MS from 2012 to 2014. Anal. Chem. 87, 99-118. DOI: 10.1021/ac5040242. Pubmed: 25398026.

Iacob RE, Chen G, Ahn J, Houel S, Wei H, Mo J, Tao L, Cohen D, Xie D, Lin Z, Morin PE, Doyle ML, Tymiak AA, and Engen JR. (2014). The influence of adnectin binding on the extracellular domain of epidermal growth factor receptor. J. Am. Soc. Mass Spectrom. 25, 2093-2102. DOI: 10.1007/s13361-014-0973-1. Pubmed: 25223306.

Boyken SE, Chopra N, Xie Q, Joseph RE, Wales TE, Fulton DB, Engen JR, Jernigan RL, and Andreotti AH. (2014). A conserved isoleucine maintains the inactive state of Bruton’s tyrosine kinase. J. Mol. Biol. 426, 3656-3669. DOI: 10.1016/j.jmb.2014.08.018. Pubmed: 25193673.

Moroco JA, Craigo JK, Iacob RE, Wales TE, Engen JR, and Smithgall TE. (2014). Differential sensitivity of Src-family kinases to activation by SH3 domain displacement. PLoS One 9, e105629. DOI: 10.1371/journal.pone.0105629. Pubmed: 25144189.

Wang W, Iacob RE, Luoh RP, Engen JR, and Lippard SJ. (2014). Electron transfer control in soluble methane monooxygenase. J. Am. Chem. Soc. 136, 9754-9762. DOI: 10.1021/ja504688z. Pubmed: 24937475.

Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, and Hartl FU. (2014). GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding. Cell 157, 922-934. DOI: 10.1016/j.cell.2014.03.038. Pubmed: 24813614.

Fang J, Nevin P, Kairys V, Venclovas C, Engen JR, and Beuning PJ. (2014). Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics. Structure 22, 572-581. DOI: 10.1016/j.str.2014.02.001. Pubmed: 24613485.

Parker CH, Morgan CR, Rand KD, Engen JR, Jorgenson JW, and Stafford DW. (2014). A conformational investigation of propeptide binding to the integral membrane protein gamma-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry. Biochemistry 53, 1511-1520. DOI: 10.1021/bi401536m. Pubmed: 24512177.

Lim SM, Westover KD, Ficarro SB, Harrison RA, Choi HG, Pacold ME, Carrasco M, Hunter J, Kim ND, Xie T, Sim T, Janne PA, Meyerson M, Marto JA, Engen JR, and Gray NS. (2014). Therapeutic targeting of oncogenic K-Ras by a covalent catalytic site inhibitor. Angew. Chem. Int. Ed. Engl. 53, 199-204. DOI: 10.1002/anie.201307387. Pubmed: 24259466.

Wei H, Mo J, Tao L, Russell RJ, Tymiak AA, Chen G, Iacob RE, and Engen JR. (2014). Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications. Drug Discov. Today 19, 95-102. DOI: 10.1016/j.drudis.2013.07.019. Pubmed: 23928097.

Shi XE, Wales TE, Elkin C, Kawahata N, Engen JR, and Annis DA. (2013). Hydrogen exchange-mass spectrometry measures stapled peptide conformational dynamics and predicts pharmacokinetic properties. Anal. Chem. 85, 11185-11188. DOI: 10.1021/ac403173p. Pubmed: 24215480.

Iacob RE, Bou-Assaf GM, Makowski L, Engen JR, Berkowitz SA, and Houde D. (2013). Investigating monoclonal antibody aggregation using a combination of H/DX-MS and other biophysical measurements. J. Pharm. Sci. 102, 4315-4329. DOI: 10.1002/jps.23754. Pubmed: 24136070.

Akgun B, Satija S, Nanda H, Pirrone GF, Shi X, Engen JR, and Kent MS. (2013). Conformational transition of membrane-associated terminally acylated HIV-1 Nef. Structure 21, 1822-1833. DOI: 10.1016/j.str.2013.08.008. Pubmed: 24035710.

Guttman M, Weis DD, Engen JR, and Lee KK. (2013). Analysis of overlapped and noisy hydrogen/deuterium exchange mass spectra. J. Am. Soc. Mass Spectrom. 24, 1906-1912. DOI: 10.1007/s13361-013-0727-5. Pubmed: 24018862.

Joseph RE, Kleino I, Wales TE, Xie Q, Fulton DB, Engen JR, Berg LJ, and Andreotti AH. (2013). Activation loop dynamics determine the different catalytic efficiencies of B cell- and T cell-specific tec kinases. Sci. Signal 6(290), ra76. DOI: 10.1126/scisignal.2004298. Pubmed: 23982207.

Karageorgos I, Wales TE, Janero DR, Zvonok N, Vemuri VK, Engen JR, and Makriyannis A. (2013). Active-site inhibitors modulate the dynamic properties of human monoacylglycerol lipase: a hydrogen exchange mass spectrometry study. Biochemistry 52, 5016-5026. DOI: 10.1021/bi400430k. Pubmed: 23795559.

Tiyanont K, Wales TE, Siebel CW, Engen JR, and Blacklow SC. (2013). Insights into Notch3 activation and inhibition mediated by antibodies directed against its negative regulatory region. J. Mol. Biol. 425, 3192-3204. DOI: 10.1016/j.jmb.2013.05.025. Pubmed: 23747483.

Tsukamoto K, Wales TE, Daniels K, Pal R, Sheng R, Cho W, Stafford W, Engen JR, Krieger M, and Kocher O. (2013). Noncanonical role of the PDZ4 domain of the adaptor protein PDZK1 in the regulation of the hepatic high density lipoprotein receptor scavenger receptor class B, type I (SR-BI). J. Biol. Chem. 288, 19845-19860. DOI: 10.1074/jbc.M113.460170. Pubmed: 23720744.

Engen JR, Wales TE, Chen S, Marzluff EM, Hassell KM, Weis DD, and Smithgall TE. (2013). Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry. Int. Rev. Phys. Chem. 32, 96-127. DOI: 10.1080/0144235X.2012.751175. Pubmed: 23682200.

Wales TE, Eggertson MJ, and Engen JR. (2013). Considerations in the analysis of hydrogen exchange mass spectrometry data. Methods Mol. Biol. 1007, 263-288. DOI: 10.1007/978-1-62703-392-3_11. Pubmed: 23666730.

Nasr ML, Shi X, Bowman AL, Johnson M, Zvonok N, Janero DR, Vemuri VK, Wales TE, Engen JR, and Makriyannis A. (2013). Membrane phospholipid bilayer as a determinant of monoacylglycerol lipase kinetic profile and conformational repertoire. Protein Sci. 22, 774-787. DOI: 10.1002/pro.2257. Pubmed: 23553709.

Houde D, and Engen JR. (2013). Conformational analysis of recombinant monoclonal antibodies with hydrogen/deuterium exchange mass spectrometry. Methods Mol. Biol. 988, 269-289. DOI: 10.1007/978-1-62703-327-5_17. Pubmed: 23475726.

Panjarian S, Iacob RE, Chen S, Engen JR, and Smithgall TE. (2013). Structure and dynamic regulation of Abl kinases. J. Biol. Chem. 288, 5443-5450. DOI: 10.1074/jbc.R112.438382. Pubmed: 23316053.

Ahn J, Engen JR. (2013). The use of Hydrogen/Deuterium exchange mass spectrometry in epitope mapping. Chimica Oggi / Chemistry Today 31(1), 25-28.

Panjarian S, Iacob RE, Chen S, Wales TE, Engen JR, and Smithgall TE. (2013). Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitors. J. Biol. Chem. 288, 6116-6129. DOI: 10.1074/jbc.M112.431312. Pubmed: 23303187.

Ahn J, Cao MJ, Yu YQ, and Engen JR. (2013). Accessing the reproducibility and specificity of pepsin and other aspartic proteases. Biochim. Biophys. Acta. 1834, 1222-1229. DOI: 10.1016/j.bbapap.2012.10.003. Pubmed: 23063535.

Yu W, Chory EJ, Wernimont AK, Tempel W, Scopton A, Federation A, Marineau JJ, Qi J, Barsyte-Lovejoy D, Yi J, Marcellus R, Iacob RE, Engen JR, Griffin C, Aman A, Wienholds E, Li F, Pineda J, Estiu G, Shatseva T, Hajian T, Al-Awar R, Dick JE, Vedadi M, Brown PJ, Arrowsmith CH, Bradner JE, and Schapira M. (2012). Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors. Nat. Commun. 3, 1288. DOI: 10.1038/ncomms2304. Pubmed: 23250418.

Alapafuja SO, Nikas SP, Bharathan IT, Shukla VG, Nasr ML, Bowman AL, Zvonok N, Li J, Shi X, Engen JR, and Makriyannis A. (2012). Sulfonyl fluoride inhibitors of fatty acid amide hydrolase. J. Med. Chem. 55, 10074-10089. DOI: 10.1021/jm301205j. Pubmed: 23083016.

Karageorgos I, Zvonok N, Janero DR, Vemuri VK, Shukla V, Wales TE, Engen JR, and Makriyannis A. (2012). Endocannabinoid enzyme engineering: soluble human thio-monoacylglycerol lipase (sol-S-hMGL). ACS Chem. Neurosci. 3, 393-399. DOI: 10.1021/cn3000263. Pubmed: 22860208.

Ahn J, Jung MC, Wyndham K, Yu YQ, and Engen JR. (2012). Pepsin immobilized on high-strength hybrid particles for continuous flow online digestion at 10,000 psi. Anal. Chem. 84, 7256-7262. DOI: 10.1021/ac301749h. Pubmed: 22856522.

Berkowitz SA, Engen JR, Mazzeo JR, and Jones GB. (2012). Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars. Nat. Rev. Drug Discov. 11, 527-540. DOI: 10.1038/nrd3746. Pubmed: 22743980.

Sorensen PM, Iacob RE, Fritzsche M, Engen JR, Brieher WM, Charras G, and Eggert US. (2012). The natural product cucurbitacin E inhibits depolymerization of actin filaments. ACS Chem. Biol. 7, 1502-1508. DOI: 10.1021/cb300254s. Pubmed: 22724897.

Iacob RE, and Engen JR. (2012). Hydrogen exchange mass spectrometry: are we out of the quicksand? J. Am. Soc. Mass Spectrom. 23, 1003-1010. DOI: 10.1007/s13361-012-0377-z. Pubmed: 22476891.

Pene-Dumitrescu T, Shu ST, Wales TE, Alvarado JJ, Shi H, Narute P, Moroco JA, Yeh JI, Engen JR, and Smithgall TE. (2012). HIV-1 Nef interaction influences the ATP-binding site of the Src-family kinase, Hck. BMC Chem. Biol. 12, 1. DOI: 10.1186/1472-6769-12-1. Pubmed: 22420777.

Choi SH, Wales TE, Nam Y, O’Donovan DJ, Sliz P, Engen JR, and Blacklow SC. (2012). Conformational locking upon cooperative assembly of notch transcription complexes. Structure 20, 340-349. DOI: 10.1016/j.str.2011.12.011. Pubmed: 22325781.

Wei H, Ahn J, Yu YQ, Tymiak A, Engen JR, and Chen G. (2012). Using hydrogen/deuterium exchange mass spectrometry to study conformational changes in granulocyte colony stimulating factor upon PEGylation. J. Am. Soc. Mass Spectrom. 23, 498-504. DOI: 10.1007/s13361-011-0310-x. Pubmed: 22227798.

Kim M, Sun ZY, Rand KD, Shi X, Song L, Cheng Y, Fahmy AF, Majumdar S, Ofek G, Yang Y, Kwong PD, Wang JH, Engen JR, Wagner G, and Reinherz EL. (2011). Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization. Nat. Struct. Mol. Biol. 18, 1235-1243. DOI: 10.1038/nsmb.2154. Pubmed: 22002224.

Engen JR, Wales TE, Shi X. (2011). Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins. Encyclopedia of Analytical Chemistry. Online ISBN: 9780470027318, Wiley, Robert A. Meyers, Editor-in-Chief. DOI: 10.1002/9780470027318.a9201.

Rand KD, Pringle SD, Morris M, Engen JR, and Brown JM. (2011). ETD in a traveling wave ion guide at tuned Z-spray ion source conditions allows for site-specific hydrogen/deuterium exchange measurements. J. Am. Soc. Mass Spectrom. 22, 1784-1793. DOI: 10.1007/s13361-011-0196-7. Pubmed: 21952892.

Marcsisin SR, Narute PS, Emert-Sedlak LA, Kloczewiak M, Smithgall TE, and Engen JR. (2011). On the solution conformation and dynamics of the HIV-1 viral infectivity factor. J. Mol. Biol. 410, 1008-1022. DOI: 10.1016/j.jmb.2011.04.053. Pubmed: 21763503.

Morgan CR, Hebling CM, Rand KD, Stafford DW, Jorgenson JW, and Engen JR. (2011). Conformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscs. Mol. Cell Proteomics 10, M111 010876. DOI: 10.1074/mcp.M111.010876. Pubmed: 21715319.

Fang J, Engen JR, and Beuning PJ. (2011). Escherichia coli processivity clamp beta from DNA polymerase III is dynamic in solution. Biochemistry 50, 5958-5968. DOI: 10.1021/bi200580b. Pubmed: 21657794.

Fang J, Rand KD, Beuning PJ, and Engen JR. (2011). False EX1 signatures caused by sample carryover during HX MS analyses. Int. J. Mass Spectrom. 302, 19-25. DOI: 10.1016/j.ijms.2010.06.039. Pubmed: 21643454.

Engen JR, Jørgensen TJ. (2011). Special focus issue: Hydrogen Exchange Mass Spectrometry. Int. J. Mass. Spectrom. 302(1-3), 1-2. DOI: 10.1016/j.ijms.2011.02.010

Houde D, Berkowitz SA, and Engen JR. (2011). The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J. Pharm. Sci. 100, 2071-2086. DOI: 10.1002/jps.22432. Pubmed: 21491437.

Tiyanont K, Wales TE, Aste-Amezaga M, Aster JC, Engen JR, and Blacklow SC. (2011). Evidence for increased exposure of the Notch1 metalloprotease cleavage site upon conversion to an activated conformation. Structure 19, 546-554. DOI: 10.1016/j.str.2011.01.016. Pubmed: 21481777.

Morgan CR, Miglionico BV, and Engen JR. (2011). Effects of HIV-1 Nef on human N-myristoyltransferase 1. Biochemistry 50, 3394-3403. DOI: 10.1021/bi200197e. Pubmed: 21449607.

Iacob RE, Zhang J, Gray NS, and Engen JR. (2011). Allosteric interactions between the myristate- and ATP-site of the Abl kinase. PLoS One 6, e15929. DOI: 10.1371/journal.pone.0015929. Pubmed: 21264348.

Kent MS, Murton JK, Sasaki DY, Satija S, Akgun B, Nanda H, Curtis JE, Majewski J, Morgan CR, and Engen JR. (2010). Neutron reflectometry study of the conformation of HIV Nef bound to lipid membranes. Biophys. J. 99, 1940-1948. DOI: 10.1016/j.bpj.2010.07.016. Pubmed: 20858440.

Marcsisin SR, and Engen JR. (2010). Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif. J. Mol. Biol. 402, 892-904. DOI: 10.1016/j.jmb.2010.08.026. Pubmed: 20728451.

Hebling CM, Morgan CR, Stafford DW, Jorgenson JW, Rand KD, and Engen JR. (2010). Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry. Anal. Chem. 82, 5415-5419. DOI: 10.1021/ac100962c. Pubmed: 20518534.

Fang J, Rand KD, Silva MC, Wales TE, Engen JR, and Beuning PJ. (2010). Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD’. J. Mol. Biol. 398, 40-53. DOI: 10.1016/j.jmb.2010.02.040. Pubmed: 20206636.

Marcsisin SR, and Engen JR. (2010). Hydrogen exchange mass spectrometry: what is it and what can it tell us? Anal. Bioanal. Chem. 397, 967-972. DOI: 10.1007/s00216-010-3556-4. Pubmed: 20195578.

Houde D, Peng Y, Berkowitz SA, and Engen JR. (2010). Post-translational modifications differentially affect IgG1 conformation and receptor binding. Mol. Cell Proteomics 9, 1716-1728. DOI: 10.1074/mcp.M900540-MCP200. Pubmed: 20103567.

Zhang J, Adrian FJ, Jahnke W, Cowan-Jacob SW, Li AG, Iacob RE, Sim T, Powers J, Dierks C, Sun F, Guo GR, Ding Q, Okram B, Choi Y, Wojciechowski A, Deng X, Liu G, Fendrich G, Strauss A, Vajpai N, Grzesiek S, Tuntland T, Liu Y, Bursulaya B, Azam M, Manley PW, Engen JR, Daley GQ, Warmuth M, and Gray NS. (2010). Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 463, 501-506. DOI: 10.1038/nature08675. Pubmed: 20072125.

Zhou W, Ercan D, Chen L, Yun CH, Li D, Capelletti M, Cortot AB, Chirieac L, Iacob RE, Padera R, Engen JR, Wong KK, Eck MJ, Gray NS, and Janne PA. (2009). Novel mutant-selective EGFR kinase inhibitors against EGFR T790M. Nature 462, 1070-1074. DOI: 10.1038/nature08622. Pubmed: 20033049.

Morgan CR, and Engen JR. (2009). Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry. Curr. Protoc. Protein Sci. Chapter 17, Unit 17 16 11-17. DOI: 10.1002/0471140864.ps1706s58. Pubmed: 19937720.

Rand KD, Pringle SD, Murphy JP, 3rd, Fadgen KE, Brown J, and Engen JR. (2009). Gas-phase hydrogen/deuterium exchange in a traveling wave ion guide for the examination of protein conformations. Anal. Chem. 81, 10019-10028. DOI: 10.1021/ac901897x. Pubmed: 19921790.

Engen JR. (2009). Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal. Chem. 81, 7870-7875. DOI: 10.1021/ac901154s. Pubmed: 19788312.

Houde D, Arndt J, Domeier W, Berkowitz S, and Engen JR. (2009). Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry. Anal. Chem. 81, 2644-2651. DOI: 10.1021/ac802575y. Pubmed: 19265386.

Chen S, Engen JR. (2009). Isotope Exchange and Covalent Modification Strategies for Studying Protein Structure and Function. Curr. Anal. Chem. 5(2), 205-212. Special Issue “The exciting ionic life of a protein in the hands of a mass spectrometrist”.

Houde D, Engen JR. (2009). Conformational Dynamics of Proteins by Mass Spectrometry: Hydrogen / Deuterium Exchange and Covalent Labeling Approaches. Chimica Oggi / Chemistry Today 27(2), 12-15.

De Luca V, Maria G, De Mauro G, Catara G, Carginale V, Ruggiero G, Capasso A, Parisi E, Brier S, Engen JR, and Capasso C. (2009). Aspartic proteinases in Antarctic fish. Mar. Genomics 2, 1-10. DOI: 10.1016/j.margen.2009.03.001. Pubmed: 21798166.

Iacob RE, Pene-Dumitrescu T, Zhang J, Gray NS, Smithgall TE, and Engen JR. (2009). Conformational disturbance in Abl kinase upon mutation and deregulation. Proc. Natl. Acad. Sci. U. S. A. 106, 1386-1391. DOI: 10.1073/pnas.0811912106. Pubmed: 19164531.

Mitchell JL, Engen JR. (2009). Protein Analysis with Hydrogen-Deuterium Exchange Mass Spectrometry. Chapter 4 of “Protein Mass Spectrometry“, Comprehensive Analytical Chemistry Series, Vol. 52, 83-102. ISBN: 978-0-444-53055-4, Elsevier, Julian Whitelegge, Editor. DOI: 10.1016/S0166-526X(08)00204-3.

Chen S, O’Reilly LP, Smithgall TE, and Engen JR. (2008). Tyrosine phosphorylation in the SH3 domain disrupts negative regulatory interactions within the c-Abl kinase core. J. Mol. Biol. 383, 414-423. DOI: 10.1016/j.jmb.2008.08.040. Pubmed: 18775435.

Iacob RE, Murphy JP, 3rd, and Engen JR. (2008). Ion mobility adds an additional dimension to mass spectrometric analysis of solution-phase hydrogen/deuterium exchange. Rapid Commun. Mass Spectrom. 22, 2898-2904. DOI: 10.1002/rcm.3688. Pubmed: 18727141.

Wales TE, Fadgen KE, Gerhardt GC, and Engen JR. (2008). High-speed and high-resolution UPLC separation at zero degrees Celsius. Anal. Chem. 80, 6815-6820. DOI: 10.1021/ac8008862. Pubmed: 18672890.

Engen JR, Wales TE, Hochrein JM, Meyn MA, 3rd, Banu Ozkan S, Bahar I, and Smithgall TE. (2008). Structure and dynamic regulation of Src-family kinases. Cell Mol. Life Sci. 65, 3058-3073. DOI: 10.1007/s00018-008-8122-2. Pubmed: 18563293.

Chen S, Dumitrescu TP, Smithgall TE, and Engen JR. (2008). Abl N-terminal cap stabilization of SH3 domain dynamics. Biochemistry 47, 5795-5803. DOI: 10.1021/bi800446b. Pubmed: 18452309.

Brier S, Engen JR. (2008). Hydrogen Exchange Mass Spectrometry: Principles and Capabilities. In “Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics“, pp 11-43. ISBN: 978-0-470-25886-6, Blackwell Publishing, Mark R. Chance, Editor. Link.

Raza A, Engen JR. (2008). Mass Spectrometry Applications in Redox Biology. In “Redox Biochemistry”, Section 6.1, pp 228-237. ISBN: 978-0-471-78625-5, John Wiley & Sons. Ruma Banerjee, Editor. Link.

Brier S, Maria G, Carginale V, Capasso A, Wu Y, Taylor RM, Borotto NB, Capasso C, and Engen JR. (2007). Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii. FEBS J. 274, 6152-6166. DOI: 10.1111/j.1742-4658.2007.06136.x. Pubmed: 17976195.

Trible RP, Emert-Sedlak L, Wales TE, Ayyavoo V, Engen JR, and Smithgall TE. (2007). Allosteric loss-of-function mutations in HIV-1 Nef from a long-term non-progressor. J. Mol. Biol. 374, 121-129. DOI: 10.1016/j.jmb.2007.09.009. Pubmed: 17920628.

Weis DD, Kaveti S, Wu Y, Engen JR. (2007). Probing Protein Interactions using Hydrogen-Deuterium Exchange Mass Spectrometry. In “Mass Spectrometry of Protein Interactions”, ISBN: 978-0-471-79373-1, John Wiley & Sons. Kevin Downard, Editor. Link.

Chen S, Brier S, Smithgall TE, and Engen JR. (2007). The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding. Protein Sci. 16, 572-581. DOI: 10.1110/ps.062631007. Pubmed: 17327393.

Mitchell JL, Trible RP, Emert-Sedlak LA, Weis DD, Lerner EC, Applen JJ, Sefton BM, Smithgall TE, and Engen JR. (2007). Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein. J. Mol. Biol. 366, 1282-1293. DOI: 10.1016/j.jmb.2006.12.026. Pubmed: 17207813.

Weis DD, Kjellen P, Sefton BM, and Engen JR. (2006). Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Protein Sci. 15, 2402-2410. DOI: 10.1110/ps.052016406. Pubmed: 17008721.

Kaltashov IA, Engen JR, Gross ML. (2006). Hydrogen exchange and covalent modification: Focus on biomolecular structure, dynamics, and function. 18th Sanibel Conference on Mass Spectrometry. J. Am. Soc. Mass Spectrom. 17(11), I1-I2.

Weis DD, Engen JR, and Kass IJ. (2006). Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom. 17, 1700-1703. DOI: 10.1016/j.jasms.2006.07.025. Pubmed: 16931036.

Meyn MA, 3rd, Wilson MB, Abdi FA, Fahey N, Schiavone AP, Wu J, Hochrein JM, Engen JR, and Smithgall TE. (2006). Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. J. Biol. Chem. 281, 30907-30916. DOI: 10.1074/jbc.M605902200. Pubmed: 16912036.

Weis DD, Wales TE, Engen JR, Hotchko M, and Ten Eyck LF. (2006). Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis. J. Am. Soc. Mass Spectrom. 17, 1498-1509. DOI: 10.1016/j.jasms.2006.05.014. Pubmed: 16875839.

Hochrein JM, Wales TE, Lerner EC, Schiavone AP, Smithgall TE, and Engen JR. (2006). Conformational features of the full-length HIV and SIV Nef proteins determined by mass spectrometry. Biochemistry 45, 7733-7739. DOI: 10.1021/bi060438x. Pubmed: 16784224.

Kaveti S, and Engen JR. (2006). Protein interactions probed with mass spectrometry. Methods Mol. Biol. 316, 179-197. DOI: 10.1385/1-59259-964-8:179. Pubmed: 16671405.

Wu Y, Kaveti S, and Engen JR. (2006). Extensive deuterium back-exchange in certain immobilized pepsin columns used for H/D exchange mass spectrometry. Anal. Chem. 78, 1719-1723. DOI: 10.1021/ac0518497. Pubmed: 16503628.

Wales TE, and Engen JR. (2006). Partial unfolding of diverse SH3 domains on a wide timescale. J. Mol. Biol. 357, 1592-1604. DOI: 10.1016/j.jmb.2006.01.075. Pubmed: 16487539.

Wu Y, Engen JR, and Hobbins WB. (2006). Ultra performance liquid chromatography (UPLC) further improves hydrogen/deuterium exchange mass spectrometry. J. Am. Soc. Mass Spectrom. 17, 163-167. DOI: 10.1016/j.jasms.2005.10.009. Pubmed: 16406808.

Wales TE, and Engen JR. (2006). Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170. DOI: 10.1002/mas.20064. Pubmed: 16208684.

Hochrein JM, Lerner EC, Schiavone AP, Smithgall TE, and Engen JR. (2006). An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry. Protein Sci. 15, 65-73. DOI: 10.1110/ps.051782206. Pubmed: 16322569.

Lu X, Li L, Feng X, Wu Y, Dunaway-Mariano D, Engen JR, and Mariano PS. (2005). L-canavanine is a time-controlled mechanism-based inhibitor of Pseudomonas aeruginosa arginine deiminase. J. Am. Chem. Soc. 127, 16412-16413. DOI: 10.1021/ja056226p. Pubmed: 16305225.

Lerner EC, Trible RP, Schiavone AP, Hochrein JM, Engen JR, and Smithgall TE. (2005). Activation of the Src family kinase Hck without SH3-linker release. J. Biol. Chem. 280, 40832-40837. DOI: 10.1074/jbc.M508782200. Pubmed: 16210316.

Carter JM, Gurevich VV, Prossnitz ER, and Engen JR. (2005). Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry. J. Mol. Biol. 351, 865-878. DOI: 10.1016/j.jmb.2005.06.048. Pubmed: 16045931.

Caldeira JC, Wu Y, Mameli M, Purdy RH, Li PK, Akwa Y, Savage DD, Engen JR, and Valenzuela CF. (2004). Fetal alcohol exposure alters neurosteroid levels in the developing rat brain. J. Neurochem. 90, 1530-1539. DOI: 10.1111/j.1471-4159.2004.02686.x. Pubmed: 15341536.

Wu Y, and Engen JR. (2004). What mass spectrometry can reveal about protein function. Analyst 129, 290-296. DOI: 10.1039/b316341e. Pubmed: 15042158.

Engen JR. (2003). Analysis of protein complexes with hydrogen exchange and mass spectrometry. Analyst 128, 623-628. DOI: 10.1039/b212800b. Pubmed: 12866878.

Takashima Y, Delfino FJ, Engen JR, Superti-Furga G, and Smithgall TE. (2003). Regulation of c-Fes tyrosine kinase activity by coiled-coil and SH2 domains: analysis with Saccharomyces cerevisiae. Biochemistry 42, 3567-3574. DOI: 10.1021/bi0272499. Pubmed: 12653561.

Harris MN, Burchiel SW, Winyard PG, Engen JR, Mobarak CD, and Timmins GS. (2002). Determining the site of spin trapping of the equine myoglobin radical by combined use of EPR, electrophoretic purification, and mass spectrometry. Chem. Res. Toxicol. 15, 1589-1594. DOI: 10.1021/tx025594t. Pubmed: 12482241.

Engen JR, Bradbury EM, and Chen X. (2002). Using stable-isotope-labeled proteins for hydrogen exchange studies in complex mixtures. Anal. Chem. 74, 1680-1686. DOI: 10.1021/ac011122s. Pubmed: 12033260.

Gmeiner WH, Xu I, Horita DA, Smithgall TE, Engen JR, Smith DL, and Byrd RA. (2001). Intramolecular binding of a proximal PPII helix to an SH3 domain in the fusion protein SH3Hck : PPIIhGAP. Cell Biochem. Biophys. 35, 115-126. DOI: 10.1385/cbb:35:2:115. Pubmed: 11892787.

Dorey K, Engen JR, Kretzschmar J, Wilm M, Neubauer G, Schindler T, and Superti-Furga G. (2001). Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase. Oncogene 20, 8075-8084. DOI: 10.1038/sj.onc.1205017. Pubmed: 11781820.

Engen JR, and Smith DL. (2001). Investigating protein structure and dynamics by hydrogen exchange MS. Anal. Chem. 73, 256A-265A. DOI: 10.1021/ac012452f. Pubmed: 11354508.

Engen JR, and Smith DL. (2000). Investigating the higher order structure of proteins. Hydrogen exchange, proteolytic fragmentation, and mass spectrometry. Methods Mol. Biol. 146, 95-112. DOI: 10.1385/1-59259-045-4:95. Pubmed: 10948498.

Engen JR, Gmeiner WH, Smithgall TE, and Smith DL. (1999). Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2. Biochemistry 38, 8926-8935. DOI: 10.1021/bi982611y. Pubmed: 10413466.

Engen JR, Smithgall TE, Gmeiner WH, and Smith DL. (1999). Comparison of SH3 and SH2 domain dynamics when expressed alone or in an SH(3+2) construct: the role of protein dynamics in functional regulation. J. Mol. Biol. 287, 645-656. DOI: 10.1006/jmbi.1999.2619. Pubmed: 10092465.

Engen JR, Smithgall TE, Gmeiner WH, and Smith DL. (1997). Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry. Biochemistry 36, 14384-14391. DOI: 10.1021/bi971635m. Pubmed: 9398156.