Archives of Englander Lab Publications

 

  1. S. Walter Englander (2023) HX and Me: Understanding Allostery, Folding, and Protein Machines. Annual Review of Biophysics 52:4.1–4.18.
  2. Shi, F., Mendrola, J. M., Sheetz, J. B., Wu, N., Sommer, A., Speer, K. F., . . . Lemmon, M. A. (2021) ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Reports 37:109834.
  3. Ye, X., Mayne, L., and Englander, S. W. (2021) A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors. J Biol Chem 297(3):101066.
  4. A. K. Hatstat, H. D. Ahrandt, S. W. Englander, L. Mayne, D. G. McCafferty (2021) Characterization of small molecule induced changes in Parkinson’s-related trafficking via the Nedd4 ubiquitin signaling cascade. Cell Chemical Biology 28(1):14-25.
  5. Xiang Ye, JiaBei Lin, Leland Mayne, James Shorter, and S. Walter Englander (2020) Structural and kinetic basis for the regulation and potentiation of Hsp104 function. Proc Natl Acad Sci USA 117(17):9384-9392.
  6. E. A. Sweeny et al., (2019) Structural and mechanistic insights into Hsp104 function revealed by synchrotron X-ray footprinting. J Biol Chem 295(6):1517-1538.
  7. Z. Y. Kan, X. Ye, J. J. Skinner, L. Mayne, S. W. Englander, (2019) ExMS2: An Integrated Solution for Hydrogen-Deuterium Exchange Mass Spectrometry Data Analysis. Anal Chem 91(11):7474-7481.
  8. Xiang Ye, JiaBei Lin, Leland Mayne, James Shorter, and S. Walter Englander (2019) Hydrogen exchange reveals Hsp104 architecture, structural dynamics, and energetics in physiological solution. Proc Natl Acad Sci USA 116(15):7333-7342.
  9. G. R. Masson et al., (2019) Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nat Methods 16:595-602.
  10. K. R. Karch et al., (2018) Hydrogen-Deuterium Exchange Coupled to Top- and Middle-Down Mass Spectrometry Reveals Histone Tail Dynamics before and after Nucleosome Assembly. Structure 26(12):1651-1663 e1653.
  11. D. Nguyen, L. Mayne, M. C. Phillips, S. Walter Englander, (2018) Reference Parameters for Protein Hydrogen Exchange Rates. J Am Soc Mass Spectrom 29(9):1936-1939.
  12. Ye X, Mayne L, Kan ZY, & Englander SW (2018) Folding of maltose binding protein outside of and in GroEL. Proc Natl Acad Sci USA 115(3):519-524.
  13. Englander SW & Mayne L (2017) Reply to Eaton and Wolynes: How do proteins fold? Proc Natl Acad Sci USA 114(46):E9761-E9762.
  14. Englander SW & Mayne L (2017) The case for defined protein folding pathways. Proc Natl Acad Sci USA 114(31):8253-8258.
  15. Chetty PS, Mayne L, Lund-Katz S, Englander SW, & Phillips MC (2017) Helical structure, stability, and dynamics in human apolipoprotein e3 and e4 by hydrogen exchange and mass spectrometry. Proc Natl Acad Sci USA 114(5):968-973.
  16. Tischer A, Machha VR, Frontroth JP, Brehm MA, Obser T, Reinhard Schneppenheim, Mayne L, Englander SW, and Auton M (2017) Enhanced Local Disorder in a Clinically Elusive von Willebrand Factor Provokes High-Affinity Platelet Clumping J. Mol. Bio. 429(14):2161-2167
  17. Hu W, Kan ZY, Mayne L, & Englander SW (2016) Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway. Proc Natl Acad Sci USA 113(14):3809-3814.
  18. Englander SW, Mayne L, Kan ZY, & Hu W (2016) Protein folding-how and why: By hydrogen exchange, fragment separation, and mass spectrometry. Annu Rev Biophys 45:135-152.
  19. Mayne L (2016) Hydrogen exchange mass spectrometry. Methods Enzymol 566:335-356.
  20. Veronica C. Casina, Wenbing Hu, Jian-Hua Mao, Rui-Nan Lu, Hayley A. Hanby, Brandy Pickens, Zhong-Yuan Kan, Woon K. Lim, Leland Mayne, Eric M. Ostertag, Stephen Kacir, Don L. Siegel, S. Walter Englander, and X. Long Zheng (2015) High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune ttp syndrome. Proc Natl Acad Sci USA 112(31):9620-9625.
  21. Englander, S.W. & Mayne, L. (2014) The nature of protein folding pathways. Proc Natl Acad Sci USA 111:15873-15880.
  22. Walters BT, Mayne L, Hinshaw JR, Sosnick TR, & Englander SW (2013) Folding of a large protein at high structural resolution.Proc Natl Acad Sci USA 110:18898-18903.
  23. Kan ZY, Walters BT, Mayne L, & Englander SW (2013) Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis. Proc Natl Acad Sci USA 110:16438-16443.
  24. Hu W, Walters BT, Kan ZY, Mayne L, Rosen LE, Marqusee S, & Englander SW (2013) Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. Proc Natl Acad Sci USA 110:7684-7689.
  25. Sevugan Chetty P, Nguyen D, Nickel M, Lund-Katz S, Mayne L, Englander SW, & Phillips MC (2013) Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry.  J Lipid Res 54:1589-1597.
  26. Walters BT, Ricciuti A, Mayne L, & Englander SW (2012) Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment. J Amer Soc Mass Spec 23:2132-2139.
  27. Skinner JJ, Lim WK, Bedard S, Black BE, & Englander SW (2012) Protein hydrogen exchange: Testing current models. Protein Sci 21:987-995.
  28. Skinner JJ, Lim WK, Bedard S, Black BE, & Englander SW (2012) Protein dynamics viewed by hydrogen exchange. Protein Sci  21:996-1005.
  29. Sevugan Chetty P, Mayne L, Kan ZY, Lund-Katz S, Englander SW, & Phillips MC (2012) Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry. Proc Natl Acad Sci US 109:11687-11692.
  30. Zhong-Yuan Kan, Leland Mayne, Palaniappan Sevugan Chetty, and S. Walter Englander (2011). ExMS: Data Analysis for HX-MS Experiments. JASMS 22
  31. Leland Mayne, Zhong-Yuan Kan, Palaniappan Sevugan Chetty, Alec Ricciuti, Benjamin T. Walters, and S. Walter Englander (2011). Many Overlapping Peptides for Protein Hydrogen Exchange Experiments by the Fragment Separation-Mass Spectrometry Method. JASMS 22
  32. Panchenko T, Sorensen TC, Woodcock CL, Kan ZY, Wood S, Resch MG, Luger K, Englander SW, Hansen JC, Black BE (2011) Replacement of histone H3 with CENP-A directs global nucleosome array condensation and loosening of nucleosome superhelical termini. Proc Natl Acad Sci U S A 108:16588-16593.
  33. Palaniappan S. Chetty, Leland Mayne, Sissel Lund-Katz, David Stranz,, S. Walter Englander, Michael C. Phillips  (2009) Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry. Proceedings of the National Academy of Sciences USA, in press.
  34. Weisha Liu., Jon N. Rumbley, S. Walter Englander, A. Joshua Wand (2009) Fast structural dynamics in reduced and oxidized cytochrome c. Protein Science,18, 670-674.
  35. Woon K. Lim, Jörg Rösgen, S. Walter Englander (2009) Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group. Proceedings of the National Academy of Sciences USA 106:2595-2600.
  36. John J. Skinner, Wood, S., James S. Shorter, Walter Englander, Ben E. Black, (2008) The Mad2 Partial Unfolding Model: Regulating Mitosis Through Mad2 Conformational Switching. Journal of Cell Biology. 183, 761-768. 
  37. Sabrina Bédard, Mallella M.G. Krishna, Leland Mayne, Walter Englander (2008) Protein folding: Independent unrelated pathways or predetermined pathway with optional errors. Proceedings of the National Academy of Sciences USA 105, 7182 7187.
  38. S. Walter Englander, Leland Mayne, Mallella M.G. Krishna (2008) Protein folding and misfolding: mechanism and principles. Quarterly Reviews of Biophysics, 40, 287-326.
  39. Sabrina Bédard, Leland Mayne, Ronald W.Peterson, A. Joshua Wand, S. Walter Englander (2007) The foldon substructure of staphylococcal nuclease. Journal of Molecular Biology 376, 1142 1154.
  40. R. Horst, Wayne A. Fenton, S. Walter Englander, Kurt Wthrich, Arthur L. Horwich, (2007) Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proceedings of the National Academy of Sciences USA 104, 20788-20792.
  41. Mallella M.G. Krishna, Haripada Maity, Jon N. Rumbley, S. Walter Englander. (2007) Branching in the sequential folding pathway of cytochrome c. Protein Science,16, 1-11.
  42. Mallella M.G. Krishna, S. Walter Englander (2007) A unified mechanism for protein folding. Predetermined pathways with optional errors. Protein Science,16, 449-464.
  43. S. Walter Englander (2006) Hydrogen exchange and mass spectrometry: a historical perspective. Journal of the American Society of Mass Spectrometry 17, 1481-1489.
  44. Mallela M. G. Krishna, Haripada Maity, Jon N. Rumbley, Yan Lin, S. Walter Englander (2006). Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. Journal of Molecular Biology 359, 1410-1419.
  45. Haripada Maity, Jon N. Rumbley, S. Walter Englander (2006). Functional role of a protein foldon An W-loop foldon controls the alkaline transition in ferricytochrome c. Proteins: Structure, Function, and Bioinformatics 63, 349-355.
  46. Charyl Del Mar, Eric A. Greenbaum, Leland Mayne, S. Walter Englander, and Virgil L. Woods, Jr. (2005). Structure and properties of a-synuclein and other amyloids determined at the amino acid level. Proceedings of the National Academy of Sciences 102, 15477-15482.
  47. Eric A. Greenbaum, Charles L. Graves, Amanda J. Mishizen-Eberz, Michael A. Lupoli, David R. Lynch, S. Walter Englander, Paul H. Axelsen, and Benoit I. Giasson (2005). The E46K mutation in a-synuclein increases amyloid fibril formation. The Journal of Biological Chemistry 280, 7800-7807.
  48. Haripada Maity, Mita Maity, Mallela M. G. Krishna, Leland Mayne, and S. Walter Englander (2005). Protein folding: The stepwise assembly of foldon units. Proceedings of the National Academy of Sciences 102, 4741-4746.
  49. Mallela M. G. Krishna, and S. Walter Englander (2005). The N-terminal to C-terminal motif in protein folding and function. Proceedings of the National Academy of Sciences 102, 1053-1058.
  50. Mallela M. G. Krishna, Yan Lin, and S. Walter Englander (2004). Protein misfolding: optional barriers, misfolded intermediates, and pathway heterogeneity. Journal of Molecular Biology 343, 1095-1109.
  51. Haripada Maity, Mita Maity, and S. Walter Englander (2004). How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization. Journal of Molecular Biology 343, 223-233.
  52. Mallela M. G. Krishna, Linh Hoang, Yan Lin, and S. Walter Englander (2004). Hydrogen exchange methods to study protein folding. Methods 34, 51-64.
  53. Mallela M. G. Krishna, Yan Lin, Leland Mayne, and S. Walter Englander (2003). Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. Journal of Molecular Biology 334, 501-513.
  54. Weixia Liu, Jon Rumbley, S. Walter Englander, and A. Joshua Wand (2003). Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c. Protein Science 12, 2104-2108.
  55. Linh Hoang, Haripada Maity, Mallela M. G. Krishna, Yan Lin, and S. Walter Englander (2003). Folding Units Govern the Cytochrome c Alkaline Transition. Journal of Molecular Biology 331, 37-43.
  56. Mallela M. G. Krishna, Yan Lin, Jon N. Rumbley, and S. Walter Englander (2003). Cooperative omega loops in Cytochrome c: Role in folding and function. Journal of Molecular Biology 331, 29-36.
  57. Joan J. Englander, Charyl Del Mar, Will Li, S. Walter Englander, Jack S. Kim, David D. Stranz, Yoshitomo Hamuro, and Virgil L. Woods, Jr. (2003). Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry. Proceedings of the National Academy of Sciences 100, 7057-7062.
  58. Haripada Maity, Woon Ki Lim, Jon N. Rumbley, and S. Walter Englander (2003). Protein hydrogen exchange mechanism: Local fluctuations. Protein Science 12, 153-160.
  59. S. Walter Englander, Leland Mayne, and Jon N. Rumbley (2002). Submolecular cooperativity produces multi-state protein unfolding and refolding. Biophysical Chemistry 101-102, 57-65.
  60. Jon N. Rumbley, Linh Hoang, and S. Walter Englander (2002). Recombinant equine Cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants. Biochemistry 41, 13894-13901.
  61. Bryan A. Krantz, Leland Mayne, Jon Rumbley, S. Walter Englander, and Tobin R. Sosnick (2002). Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. Journal of Molecular Biology 324, 359-371.
  62. Linh Hoang, Sabrina Bedard, Mallela M. G. Krishna, Yan Lin, and S. Walter Englander (2002). Cytochrome c folding pathway: Kinetic hydrogen exchange. Proceedings of the National Academy of Sciences 99, 12173-12178.
  63. Umamaheswar Duvvuri, Ari D. Goldberg, James K. Kranz, Linh Hoang, Ravinder Reddy, Felix W. Wehrli, A. Joshua Wand, S. W. Englander, and John S. Leigh (2001). Water magnetic relaxation dispersion in biological systems: The contribution of proton exchange and implications for the noninvasive detection of cartilage degradation. Proceedings of the National Academy of Sciences 98 12479-12484.
  64. Jon Rumbley, Linh Hoang, Leland Mayne, and S. Walter Englander (2001). An amino acid code for protein folding. Proceedings of the National Academy of Sciences 98, 105-112.
  65. Huyghues-Despointes BM, Pace CN, Englander SW, Scholtz JM (2001) Measuring the conformational stability of a protein by hydrogen exchange. Methods in Molecular Biology 168:69-92.
  66. S. Walter Englander & Mallela M. G. Krishna (2001). Hydrogen Exchange. Nature Structural Biology 8, 1-2.
  67. S. Walter Englander & Reuben Hiller (2001). Dynamics and thermodynamics of hyperthermophili proteins by hydrogen exchange. Methods in Enzymology 334: 342-350.
  68. Leland Mayne & S. Walter Englander (2000). Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange. Protein Science 9, 1873-1877.
  69. S. Walter Englander (2000). Protein folding intermediates and pathways studied by hydrogen exchange. Annual Review of Biophysics and Biomolecular Structure 29, 213-38.
  70. John S. Milne, Yujia Xu, Leland C. Mayne, and S. Walter Englander (1999). Experimental study of the protein folding landscape: Unfolding reactions in Cytochrome c. Journal of Molecular Biology, 290, 811-822.
  71. Mark Shtilerman, George H. Lorimer, and S. Walter Englander (1999). Chaperonin function: Folding by forced unfolding. Science 284, 822-825.
  72. Joan J. Englander, Jon N. Rumbley, and S. Walter Englander (1998). Signal transmission between subunits in the hemoglobin T-state. Journal of Molecular Biology 284, 1707-1716.
  73. Joan J. Englander, Godfrey Louie, Russell E. McKinnie, and S. Walter Englander (1998). Energetic components of the allosteric machinaery in hemoglobin measured by hydrogen exchange. Journal of Molecular Biology 284, 1695-1706.
  74. S. Walter Englander, Tobin R. Sosnick, Leland Mayne, Mark Shtilerman, Phoebe X. Qi, and Yawen Bai (1998). Fast and slow folding in Cytochrome c. Accounts of Chemical Research 31, 737-744.
  75. Phoebe X. Qi, Tobin R. Sosnick and S. Walter Englander (1998). The burst phase in Ribonuclease A folding and solvent dependence of the unfolded state. Nature Structural Biology 5 882-884.
  76. Yujia Xu, Leland Mayne, and S. Walter Englander (1998). Evidence for an unfolding and refolding pathway in cytochrome c. Nature Structural Biology 5, 774-778.
  77. John S. Milne, Leland Mayne, H. Roder, A. Joshua Wand, and S. Walter Englaner (1998). Determinants of protein hydrogen exchange studied in equine Cytochrome c. Protein Science 7, 739-745.
  78. S. Walter Englander (1998). Native-state HX. Trends in Biochemical Sciences 23: 378.
  79. Leland Mayne, S. Walter Englander, Rong Qiu, Jianxin Yang, Youxiang Gong, Erik J. Spek, and Neville R. Kallenbach (1998). Stabilizing effect of a multiple salt bridge in a prenucleated peptide. Journal of The American Chemical Society 120, 10643-10645.
  80. Tobin R. Sosnick, Mark D. Shtilerman, Leland Mayne, and S. Walter Englander (1997). Ultrafast signals in protein folding and the polypeptide contracted State. Proceedings of the National Academy of Sciences 94 8545-8550.
  81. Reuben Hiller, Zhi H. Zhou, Michael W. W. Adams, and S. Walter Englander (1997). Stability and Dynamics in a hyperthermophilic protein with melting temperature close to 200oC. Proceedings of the National Academy of Sciences 94 11329-11332.
  82. S. W. Englander, L. Mayne, Y. Bai, and T. R. Sosnick (1997). Hydrogen exchange: The modern legacy of Linderstrøm-Lang. Protein Science 6, 1101-1109.
  83. Tobin R. Sosnick, Sharon Jackson, Rosemarie R. Wilk, S. Walter Englander, and William F. DeGrado (1996). The role of helix formation in the folding of a fully a-helical coiled coil. Proteins: Structure, Function, and Genetics 24: 427-432.
  84. Tobin R. Sosnick, Leland Mayne, and S. Walter Englander (1996). Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins: Structure, Function, and Genetics 24, 413-426.
  85. S. Walter Englander, Tobin R. Sosnick, Joan J. Englander, and Leland Mayne (1996). Mechanisms and uses of hydrogen exchange. Current Opinion in Structural Biology 6: 18-23.
  86. Yawen Bai and S. Walter Englander (1996). Future directions in folding: The multi-state nature of protein structure. Proteins: Structure, Function, and Genetics 24: 145-151.
  87. Michael E. Rodgers, Joan J. Englander, S. Walter Englander, and William F. Harrington (1996). Measurement of protein structure change in active muscle by hydrogen-tritium exchange. Biophysical Chemistry 59: 221-230.
  88. A. Joshua Wand & S. Walter Englander (1996). Protein complexes studied by NMR spectroscopy. Current Opinion in Biotechnology 7, 403-408.
  89. Louis Carlacci and S. Walter Englander (1996). Loop problem in proteins: Developments on the Monte Carlo simulated annealing approach. Journal of Computational Chemistry 17: 1002-1012.
  90. Yawen Bai, Tobin R. Sosnick, Leland Mayne, and S. Walter Englander (1995). Protein folding intermediates: Native-state hydrogen exchange. Science 269 192-197.
  91. Yawen Bai, John S. Milne, Leland Mayne, and S. Walter Englander (1994). Protein stability parameters measured by hydrogen exchange. Proteins: Structure, Function, and Genetics 20: 4-14.
  92. TR. Sosnick, L. Mayne, R. Hiller and S.W. Englander (1994). The barriers in protein folding. Nature Structural Biology 1(3): 149-156.
  93. Yawen Bai and S. Walter Englander (1994). Hydrogen bond strength and b-sheet propensities: The role of a side chain blocking effect. Proteins: Structure, Function, and Genetics 18, 262-266.
  94. Gregory P. Connelly, Yawen Bai, Mei-Fen Jeng, and S. Walter Englander (1993). Isotope effects in peptide group hydrogen exchange. Proteins: Structure, Function, and Genetics 17, 87-92.
  95. Yawen Bai, John S. Milne, Leland Mayne, and S. Walter Englander (1993). Primary structure effects on peptide group hydrogen exchange. Proteins: Structure, Function, and Genetics 17, 75-86.
  96. Louis Carlacci and S. Walter Englander (1993). The loop problem in proteins: A Monte Carlo simulated annealing approach. Biopolymers 33: 1271-1286.
  97. Dorothy B. Calhoun, Jane M. Vanderkooi, Gary R. Holtom, and S. Walter Englander (1986). Protein fluorescence quenching by small molecules: Protein penetration versus solvent exposure. Proteins: Structure, Function, and Genetics 1:109-115.
  98. R. S. Preisler, C. Mandal, S. W. Englander, and N. R. Kallenbach (1984). Premelting and the hydrogen-exchange open state in synthetic RNA duplexes. Biopolymers 23: 2099-2125.
  99. R. S. Molday, S. W. Englander, and R· G. Kallen (1972). Primary Structure Effects on Peptide Group Hydrogen Exchange. BIOCHEMISTRY 11: 150-158.
  100. S. W. Englander and A. Poulsen (1969). Hydrogen-tritium exchange of the random chain polypeptide. Biopolymers 7: 379-393.

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