All Publications

1. L. G.(Gierasch) Pease, C. M. Deber, and E. R. Blout, Cyclic Peptides, V. ¹H and ¹³C Nuclear Magnetic Resonance Determination of the Preferred β Conformation for Proline–Containing Cyclic Hexapeptides, J. Am. Chem. Soc., 95, 258–260 (1973).


2. E. R. Blout, C. M. Deber, and L. G. Pease, Cyclic Peptides, in Polypeptides, Peptides, and Proteins, E. R. Blout, F. A. Bovey, M. Goodman, and N. Lotan, Eds., Interscience, New York, pp. 266–281 (1974).


3. D. Baron, L. G. Pease, and E. R. Blout, Cyclic Peptides, XIX. Cation Binding of a Cyclic Dodecapeptide Cyclo–(L–Val–Gly–Gly–L–Pro)₃ in an Aprotic Medium, J. Am. Chem. Soc., 99, 8299–8306 (1977).


4. L. G. Pease and C. Watson,Conformational and Ion Binding Studies on a Cyclic Pentapeptide: Evidence for β and γ Turns in Solution, in Peptides: Proceedings of the Fifth American Peptide Symposium, M. Goodman, and J. Meienhofer, Eds., John Wiley and Sons, New York , pp. 346–349 (1977).


5. C.–H. Niu, L. G. Pease and E. R. Blout, Cyclic Peptides. XVIII. ¹³C Spin–Lattice Relaxation Times of (X–L–Pro–Y)₂ Cyclic Hexapeptides, Biopolymers, 17, 115–123 (1978).


6. L. G. Pease and C. Watson, Conformational and Ion Binding Studies of a Cyclic Pentapeptide: Evidence for β and γ Turns in Solution, J. Am. Chem. Soc., 100, 1279–1286 (1978).


7. C.–H. Niu, V. Madison, L. G. Pease and E. R. Blout, Cyclic Peptides, XXII. Cation Binding by a Cyclic Hexapeptide, Cyclo(D–Ala–L–Pro–Gly)₂, Biopolymers, 17, 2747–2751 (1978).


8. B. Dietrich, T. Fyles, J. M. Lehn, L. G. Pease and D. L. Fyles, Anion Receptor Molecules. Synthesis and Some Anion Binding Properties of Macrocyclic Guanidinium Salts, JCS Chem. Comm., pp. 934–936 (1978).


9. K. L. Williamson, L. G. Pease and J. D. Roberts, Conformational Analysis by Nuclear Magnetic Resonance Spectroscopy: ¹⁵N NMR of a Cyclic Pentapeptide, J. Am. Chem. Soc., 101, 714–716 (1979).


10. K. R. K. Easwaran, L. G. Pease and E. R. Blout, Cyclic Peptides, XXIII. Conformations of an Ion–Binding Cyclic Peptide Analog of Valinomycin, Cyclo(L–Val–Gly–Gly–L–Pro)₃, Biochemistry, 18, 61–67 (1979).


11. L. G. Pease, C.–H. Niu and G. Zimmermann, Solution Conformation of Cyclo(Gly–Pro–Ser–D–Ala–Pro). Hydrogen–Bonded Reverse Turns in Cyclic Pentapeptides, J. Am. Chem. Soc., 101, 184–191 (1979).


12. L. G. Pease, Preferred Hydrogen–Bonded Conformations of Cyclic Pentapeptides, in Peptides: Structure and Biological Function, Proceedings of the Sixth American Peptide Symposium, E. Gross and J. Meienhofer, Eds., Pierce Chem. Co., Rockford, IL, pp. 197–200 (1979).


13. L. G. Pease, D. Baron, K. R. K. Easwaran and E. R. Blout, A Valinomycin Analogue Containing Only Naturally–Occurring Amino Acids, in Frontiers of Bio–Organic Chemistry and Molecular Energy, S. N. Ananchenko, Ed., Pergamon Press, Oxford, pp. 81–91 (1980).


14. J. A. Smith and L. G. Pease, Reverse Turns in Peptides and Proteins, CRC Crit.Rev. Biochemistry, 8, 315–400 (1980).


15. L. G. Pease, M. H. Frey and S. J. Opella, Observation of Conformationally Distinct Proline Residues in Two Model Peptides by Solid–State Nuclear Magnetic Resonance, J. Am. Chem. Soc., 103, 467–468 (1981).


16. L. M. Gierasch, C. M. Deber, V. Madison, C.–H. Niu and E. R. Blout, Conformations of (X–L–Pro–Y)₂ Cyclic Hexapeptides. Preferred β –Turn Conformers and Implications for β Turns in Proteins, Biochemistry, 20, 4730–4738 (1981).


17. T. H. Walter, G. L. McIntire, E. E. Bancroft, E. R. Davis, L. M. Gierasch and H. N. Blount, Interfacial Spin Trapping in Model Membrane Systems, Biochem.Biophys. Res. Comm., 102, 1350–1357 (1981).


18. J. E. Lacy, K. F. Thompson, P. I. Watnick and L. M. Gierasch, Conformations of Model Peptides in Membrane–Mimetic Environments, in Peptides: Synthesis, Structure and Function, D. H. Rich and E. Gross, Eds., Pierce Chem. Co., Rockford, IL, pp. 339–342 (1981).


19. A. C. Bach, II, A. A. Bothner–By and L. M. Gierasch, Estimation of Proline Ring Nonplanarity in Cyclic Pentapeptides from Proton Spin–Spin Coupling Constants, in Peptides: Synthesis, Structure and Function, D. H. Rich and E. Gross, Eds., Pierce Chem. Co., Rockford, IL, pp. 343–346 (1981).


20. L. M. Gierasch, S. J. Opella and M. H. Frey, Solid–State NMR of Peptides, in Peptides: Synthesis, Structure and Function, D. H. Rich and E. Gross, Eds., Pierce Chem. Co., Rockford, IL, pp. 267–275 (1981).


21. L. M. Gierasch, J. E. Lacy, K. F. Thompson, A. L. Rockwell and P. I. Watnick, Conformations of Model Peptides in Membrane–Mimetic Environments, Biophys. J., 37, 275–284 (1982).


22. A. C. Bach, II., A. A. Bothner–By and L. M. Gierasch, Determination of Proline Ring Nonplanarity from Proton Spin–Spin Coupling Constants: Applications to Two Cyclic Pentapeptides, J. Am. Chem. Soc., 104, 572–576 (1982).


23. L. M. Gierasch, M. H. Frey, J. G. Hexem and S. J. Opella, Solid State NMR of Linear and Cyclic Peptides, in NMR Spectroscopy: New Methods and Applications, George C. Levy, Ed., ACS Symposium Ser. No. 191, Washington, D.C., 233–247 (1982).


24. T. H. Walter, E. E. Bancroft, G. L. McIntire, E. R. Davis, L. M. Gierasch, H. N. Blount, H. J. Stronks and E. G. Janzen, Spin Trapping in Heterogeneous Electron Transfer Processes, Canadian J. Chem., 60, 1621–1636 (1982).



25. A. F. Spatola, L. M. Gierasch and A. L. Rockwell, A Conformational Comparison of Cyclic Peptide and Pseudopeptide Structures with Intramolecular Hydrogen Bonding, Biopolymers, 22, 147–151 (1983).


26. L. M. Gierasch, J. E. Lacy, G. Anderle, R. Lalancette and R. Mendelsohn, Spectroscopic Studies of a Hydrophobic Peptide in Membrane–Like Environments, Biopolymers, 22, 381–385 (1983).


27. G. D. Rose, W. B. Young and L. M. Gierasch, Interior Turns in Globular Proteins, Nature, 304, 654–657 (1983).


28. J. L. Flippen–Anderson, R. Gilardi, I. L. Karle, M. H. Frey, S. J. Opella, L. M. Gierasch, M. Goodman, V. Madison and N. G. Delaney, Crystal Structures, Molecular Conformations, Infrared Spectra and 13C NMR Spectra of Methylproline Peptides in the Solid State, J. Am. Chem. Soc., 105, 6609–6614 (1983).


29. M. H. Frey, J. G. Hexem, G. D. Leo, P. Tsang, S. J. Opella, A. L. Rockwell and L. M. Gierasch, Solid State NMR of Peptides in Membrane Bilayers, in Proceedings of the Eighth American Peptide Symposium, V. Hruby and D. H. Rich, Eds., Pierce Chem. Co., Rockford, IL, pp. 763–771 (1983).


30. K. Yenal, A. L. Rockwell, J. P. Cook, S. Dworetsky and L. M. Gierasch, Comparison of Cation Binding by Three Cyclic Pentapeptides, in Proceedings of the Eighth American Peptide Symposium, V. Hruby and D. H. Rich, Eds., Pierce Chem. Co., Rockford, IL, pp. 499–502 (1983).


31. A. C. Bach, II, B. S. Dunn, L. M. Gierasch, Y. Shimohigashi and C. S. Stammer, Conformational Consequences of Incorporating ΔPhe in an Enkephalin Analogue and in Related Peptides, in Proceedings of the Eighth American Symposium, V. Hruby and D. H. Rich, Eds., Pierce Chem. Co., Rockford, IL, pp. 299–302 (1983).


32. J. E. Lacy, L. M. Gierasch, A. L. Rockwell, and G. D. Rose, Reverse Turns in Hydrophobic Environments, in Proceedings of the Eighth American Peptide Symposium, V. Hruby and D. H. Rich, Eds., Pierce Chem. Co., Rockford, IL, pp. 781–784 (1983).


33. A. C. Bach, II, A. A. Baldwin, L. M. Gierasch and A. L. Rheingold, Characterization of a Methoxylated 5–Oxazolone Derivative: An Unexpected Intermediate in a Dehydropeptide Synthesis, JCS Chem. Comm., pp. 1398–1399 (1983).


34. L. M. Gierasch, K. F. Thompson, J. E. Lacy and A. L. Rockwell, Exploring Peptide Interactions with Interfacial Water Using Reversed Micelles, in Biological and Technological Relevance of Reverse Micelles and Other Amphiphilic Structures in Apolar Media, P. L. Luisi, Ed., Plenum Press, New York, pp. 265–277 (1984).


35. K. F. Thompson and L. M. Gierasch, The Conformation of a Peptide Solubilizate in a Reversed Micelle Water Pool, J. Am. Chem. Soc., 106, 3648–3652 (1984).


36. M. S. Briggs and L. M. Gierasch, Exploring the Conformational Roles of Signal Sequences: Synthesis and Conformational Analysis of Lambda Receptor Protein Wild Type and Mutant Signal Peptides, Biochemistry, 23, 3111–3114 (1984).


37. L. M. Gierasch, A. L. Rockwell, K. F. Thompson and M. S. Briggs, Conformation–Function Relationships in Hydrophobic Peptides: Interior Turns and Signal Sequences, Biopolymers, 24, 117–135 (1985).


38. M. D. Bruch, J. H. Noggle and L. M. Gierasch, Conformational Analysis of a Cyclic Pentapeptide by One– and Two–Dimensional Nuclear Overhauser Effect Spectroscopy, J. Am. Chem. Soc., 107, 1400–1407 (1985).


39. G. D. Rose, L. M. Gierasch and J. A. Smith, Turns in Peptides and Proteins, Adv. Protein Chem., Vol. 37, C. B. Anfinsen, J. T. Edsall and F. M. Richards, Eds., Academic Press, New York, pp. 1–109 (1985).


40. M. H. Frey, S. J. Opella, A. L. Rockwell and L. M. Gierasch, Solid State NMR of Cyclic Pentapeptides, J. Am. Chem. Soc., 107, 1946–1951 (1985).


41. M. S. Briggs, L. M. Gierasch, A. Zlotnick, J. Lear and W. F. DeGrado, In Vivo Function and Membrane Binding Properties Are Correlated for E. coli LamB Signal Peptides, Science, 228, 1096–1099 (1985).


42. L. M. Gierasch, I. L. Karle, A. L. Rockwell and K. Yenal, Crystal and Solution Structures of Cyclo(Ala–Pro–Gly–D–Phe–Pro): A New Type of Cyclic Pentapeptide Which Undergoes Cis–Trans Isomerization of the Ala–Pro Bond, J. Am. Chem. Soc., 107, 3321–3327 (1985).


43. A. C. Bach, II and L. M. Gierasch, Dehydrophenylalanine as the i+2th Residue of a β Turn: Synthesis and Conformation Analysis of Cyclo–(Gly–Pro–Δ^z–Phe–D–Ala–Pro) and Cyclo(Gly–Pro–D–Phe–D–Ala–Pro), J. Am. Chem. Soc., 107, 3349–3350 (1985).


44. M. K. Jain, J. Rogers, L. Simpson, and L. M. Gierasch, Effect of Tryptophan Derivatives on the Phase Properties of Bilayers, Biochim. Biophys. Acta, 816, 153–162 (1985).


45. S. J. Opella and L. M. Gierasch, Solid State Nuclear Magnetic Resonance of Peptides, in The Peptides, Vol. 7, V. J. Hruby and J. Meienhofer, Eds., Academic Press, NY, pp. 405–436 (1985).


46. M. S. Briggs and L. M. Gierasch, Biophysical Studies of Genetically Defined Synthetic Signal Sequences, in Proceedings of the Ninth American Peptide Symposium, K. D. Kopple and C. M. Deber, Eds., Pierce Chem. Co., Rockford, IL, pp. 883–886 (1985).


47. A. C. Bach, II, L. M. Gierasch, and A. L. Rheingold, Synthesis and Conformational Analysis of Three Dehydrophenylalanine–Containing Cyclic Pentapeptides, in Proceedings of the Ninth American Peptide Symposium, K. D. Kopple and C. M. Deber, Eds., Pierce Chem. Co., Rockford, IL, pp. 181–184 (1985).


48. L. M. Mueller, M. H. Frey, A. L. Rockwell, L. M. Gierasch and S. J. Opella, Dynamics of a Hydrophobic Peptide in Membrane Bilayers by Solid State NMR, Biochemistry, 25, 557–561 (1986).


49. A. F. Spatola, M. K. Anwer, A. L. Rockwell and L. M. Gierasch, Compatibility of β– and γ–Turn Features with a Peptide Backbone Modification: Synthesis and Conformational Analysis of a Model Cyclic Pseudopeptide, J. Am. Chem. Soc., 108, 825–831 (1986).


50. L. M. Gierasch, M. S. Briggs, and D. G. Cornell, Physical Properties of Genetically–Defined Synthetic Signal Sequences Suggest Initial Steps in Protein Export, in Protein Engineering, M. Inouye and R. Sarma, Eds., Academic Press, Orlando, FL, pp. 173–191 (1986).


51. M. S. Briggs and L. M. Gierasch, Molecular Mechanisms of Protein Secretion: The Role of the Signal Sequence, Adv. Protein Chem., Vol. 38, C. B. Anfinsen, F. M. Richards and J. T. Edsall, Eds., Academic Press, 109–180 (1986).


52. A. C. Bach, II and L. M. Gierasch, Dehydrophenylalanine Can Occur in Various Reverse Turn Sites: Conformational Analysis of ΔPhe–Containing Model Peptides, Biopolymers, 25, S175–S191 (1986).


53. M. S. Briggs, D. G. Cornell, R. A. Dluhy and L. M. Gierasch, Conformations of Signal Peptides Induced by Lipids Suggest Initial Steps in Protein Export, Science, 233, 206–208 (1986).


54. D. W. Hoyt, C. J. McKnight, M. S. Briggs, A. N. Stroup and L. M. Gierasch, Biophysical Properties of Synthetic Presequences Suggest Conformations Important for Protein Localization, in Peptides 1986, D. Theodoropoulos, Ed., Walter de Gruyter & Co., Berlin, pp. 373–376 (1986).


55. E. L. Baniak, II, J. E. Rivier, A. T. Hagler, and L. M. Gierasch, Nuclear Magnetic Resonance Analysis and Conformational Characterization of a Cyclic Decapeptide Antagonist of Gonadotropin–Releasing Hormone, Biochemistry, 26, 2642–2656 (1987).


56. L. Chen, P. C. Tai, M. S. Briggs and L. M. Gierasch, Protein Translocation into E. coli Membrane Vesicles Is Inhibited by Functional Synthetic Signal Sequences, J. Biol. Chem.,, 262, 1427–1429 (1987).


57. K. G. Valentine, A. L. Rockwell, L. M. Gierasch and S. J. Opella, ¹⁵N Chemical Shift Tensor of the Imide Nitrogen in the Alanyl–Prolyl Peptide Bond, J. Mag. Res., 73, 519–523 (1987).


58. A. N. Stroup, A. L. Rockwell and L. M. Gierasch, Crystal Structure of Cyclo(Gly–L–Pro–D–Phe–Gly–Val): An Example of a New Type of Three Residue Turn, J. Am. Chem. Soc., 109, 7146–7150 (1987).


59. E. L. Baniak and L. M. Gierasch, NMR Analysis and Conformational Characterization of Cyclic Antagonists of Gonadotropin Releasing Hormone, in Peptides: Chemistry and Biology, G. Marshall, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 457–458 (1988).


60. L. R. Sanza, L. M. Gierasch, J. A. Berzofsky, G. K. Buckenmeyer, K. B. Cease and C. S. Ouyang, Formation of Amphipathic Secondary Structure Is Correlated to T–Cell Antigenicity in a Series of Synthetic Peptides from Sperm Whale Myoglobin, in Peptides: Chemistry and Biology, G. Marshall, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 549–550 (1988).


61. L. M. Gierasch, M. S. Briggs and C. J. McKnight, Role of the Signal Sequence in Protein Secretion, in Peptides: Chemistry and Biology, G. Marshall, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 313–317 (1988).


62. A. N. Stroup, A. L. Rockwell, A. L. Rheingold and L. M. Gierasch, Crystal Structure of Cyclo(Gly₁–L–Pro₂–D–Phe₃–L–Ala₄–L–Pro₅): A Cyclic Pentapeptide with a Gly–L–Pro δ Turn, J. Am. Chem. Soc., 110, 5157–5161 (1988).


63. R. A. Schiksnis, A. L. Rockwell, L. M. Gierasch, and S. J. Opella, Detection of a Structural Interconversion in a Peptide in Solution with Sensitivity–Enhanced ¹⁵N Chemical–Exchange NMR Spectroscopy, J. Mag. Res., 79, 318–321 (1988).


64. L. M. Gierasch, Signal Sequences, Biochemistry,28, 923–930 (1989).


65. D. G. Cornell, R. A. Dluhy, M. S. Briggs, C. J. McKnight, and L. M. Gierasch, Conformations and Orientations of a Signal Peptide Interacting with Phospholipid Monolayers, Biochemistry, 28, 2789–2797 (1989).


66. E. L. Baniak II, Y.–C. Ma, L. M. Gierasch, and B. Munson, Ring–Opening of Cyclic Pentapeptides by Electron Impact Mass Spectrometry: Correlation with Peptide Bond Nonplanarity, J. Am. Chem. Soc., 111, 5487–5488 (1989).


67. C. J. McKnight, M. S. Briggs, and L. M. Gierasch, Functional and Nonfunctional LamB Signal Sequences Can Be Distinguished by their Biophysical Properties, J. Biol. Chem., 264, 17293–17297 (1989).


68. M. D. Bruch, C. J. McKnight, and L. M. Gierasch, Helix Formation and Stability in a Signal Sequence, Biochemistry, 28, 8554–8561 (1989).


69. L. R. Lark, J. A. Berzofsky, and L. M. Gierasch, T–Cell Antigenic Peptides from Sperm Whale Myoglobin Fold as Amphipathic Helices: A Possible Determinant for Immunodominance?, Peptide Research, 2, 314–321 (1989).


70. M. D. Bruch and L. M. Gierasch, Comparison of Helix Stability in Wildtype and Mutant LamB Signal Sequences, J. Biol.l Chem., 265, 3851–3858 (1990).


71. S. J. Stradley, J. Rizo, M. D. Bruch, A. N. Stroup, and L. M. Gierasch, Cyclic Pentapeptides as Models for Reverse Turns: Determination of the Equilibrium Distribution between Type I and Type II Conformations of Pro–Asn and Pro–Ala β Turns, Biopolymers, 29, 263–287 (1990).


72. J. Rivier, C. Rivier, W. Vale, S. Koerber, A. Corrigan, J. Porter, L. Gierasch, and A. Hagler, Bicyclic Gonadotropin Releasing Hormone (GnRH) Antagonists, in Peptides: Chemistry, Structure, and Biology, J. Rivier and G. Marshall, Eds., ESCOM Science Publishers, Leiden, The Netherlands, pp. 33–37 (1990).


73. S. J. Stradley, J. Rizo, M. D. Bruch, Z.–P. Liu, and L. M. Gierasch, Influence of Asparagine on Turn Formation in Cyclic Pentapeptides, in Peptides: Chemistry, Structure, and Biology, J. Rivier and G. Marshall, Eds., ESCOM Science Publishers, Leiden, The Netherlands, pp. 644–646 (1990).


74. T. Siahaan, L. R. Lark, M. Pierschbacher, E. Ruoslahti, and L. M. Gierasch, A Conformationally Constrained ‘RGD’ Analogue Specific for the Vitronectin Receptor: A Model for Receptor Binding, in Peptides: Chemistry, Structure, and Biology, J. Rivier and G. Marshall, Eds., ESCOM Science Publishers, Leiden, The Netherlands, pp. 699–701 (1990).


75. M. D. Bruch, C. J. McKnight, and L. M. Gierasch, NMR Analysis of Structural Stability and Specific Residue Conformations in Wild Type and Mutant LamB Signal Sequences, in Peptides: Chemistry, Structure, and Biology, J. Rivier and G. Marshall, Eds., ESCOM Science Publishers, Leiden, The Netherlands, pp. 548–551 (1990).


76. L. M. Gierasch, Conformation and Interactions of Signal Peptides: Approaches to Elucidating the Role of the Signal Sequence in Protein Secretion, in Protein Folding: Deciphering the Second Half of the Genetic Code, L. M. Gierasch and J. King, Eds., AAAS Publications, Washington, D.C., pp. 211–219 (1990).


77. Protein Folding: Deciphering the Second Half of the Genetic Code, L. M. Gierasch and J. King, Eds., AAAS Publications, Washington, D.C. (1990).


78. A. Bansal, S. J. Stradley, and L. M. Gierasch, Conformational Studies of Peptides Corresponding to the LDL Receptor Cytoplasmic Tail and Transmembrane Domain, in Current Research in Protein Chemistry, J. Villafranca, Ed., Academic Press, San Diego, CA, pp. 331–338 (1990).


79. J. D. Jones, C. J. McKnight, and L. M. Gierasch, Biophysical Studies of Signal Peptides: Implications for Signal Sequence Functions and the Involvement of Lipid in Protein Export, J. Bioenerg. Biomembr., 22, 213–232 (1990).


80. A. N. Stroup and L. M. Gierasch, Reduced Tendency to Form a β Turn in Peptides from the P22 Tailspike Protein Correlates With a Temperature–Sensitive Folding Defect, Biochemistry, 29, 9765–9771 (1990).


81. R. S. Struthers, G. Tanaka, S. Koerber, T. Solmajer, E. L. Baniak, L. M. Gierasch, W. Vale, J. Rivier, and A. T. Hagler, Design of Conformationally Constrained GnRH Antagonists, Proteins: Structure, Function, and Genetics, 8, 295–304 (1990).


82. A. N. Stroup, L. B. Cole, M. M. Dhingra, and L. M. Gierasch, Synthesis and Crystal Structures of Boc–L–Asn–L–Pro–OBzl CH₃OH and Dehydration Side Product, Boc–β–Cyano–L–Alanine–L–Pro–OBzl, Intl. J. Pept. Prot. Res., 36, 531–537 (1990).


83. Y. Reiss, S. J. Stradley, L. M. Gierasch, M. S. Brown, and J. L. Goldstein, Sequence Requirement for Peptide Recognition by Rat Brain p21^ras Protein Farnesyltransferase, Proc. Natl. Acad. Sci. USA, 88, 732–736 (1991).


84. S. J. Landry and L. M. Gierasch, Recognition of Nascent Polypeptides for Targeting and Folding, Trends Biochem. Sci., 16, 159–163, (1991).


85. J. Rizo, M. M. Dhingra, and L. M. Gierasch, A Cyclic Hexapeptide Model for Asparagine Side–chain/backbone Interactions in a Protein β Turn, in Peptides: Proceedings of the Twenty–First European Peptide Symposium, E. Giralt and D. Andreu, Eds., ESCOM Science Publishers, Leiden, The Netherlands, pp. 468–471 (1991).


86. M. D. Bruch, M. M. Dhingra, and L. M. Gierasch, Side Chain–Backbone Hydrogen Bonding Contributes to Helix Stability in Peptides Derived from an α–Helical Region of Carboxypeptidase A, Proteins: Structure, Function, and Genetics, 10, 130–139 (1991).


87. C. J. McKnight, M. Rafalski, and L. M. Gierasch, Fluorescence Analysis of Tryptophan–Containing Variants of the LamB Signal Sequence Upon Insertion into a Lipid Bilayer, Biochemistry, 30, 6241–6246 (1991).


88. C. J. McKnight, S. J. Stradley, J. D. Jones, and L. M. Gierasch, Conformational and Membrane–Binding Properties of a Signal Sequence Are Largely Unaltered by Its Adjacent Mature Region, Proc. Natl. Acad. Sci. USA, 88, 5799–5803 (1991).


89. S. J. Landry and L. M. Gierasch, The Chaperonin GroEL Binds a Polypeptide in an α–Helical Conformation, Biochemistry, 30, 7359–7362 (1991).


90. D. W. Hoyt and L. M. Gierasch, A Peptide Corresponding to an Export–defective Mutant OmpA Signal Sequence with Asparagine in the Hydrophobic Core Is Unable to Insert into Model Membranes, J. Biol. Chem., 266, 14406–14412 (1991).


91. J. L. Goldstein, M. S. Brown, S. J. Stradley, Y. Reiss, and L. M. Gierasch, Nonfarnesylated Tetrapeptide Inhibitors of Protein Farnesyltransferase, J. Biol. Chem., 266, 15575–15578 (1991).


92. D. W. Hoyt, D. M. Cyr, L. M. Gierasch, and M. G. Douglas, Interaction of Peptides Corresponding to Mitochondrial Presequences with Membranes, J. Biol. Chem., 266, 21693–21699 (1991).


93. D. W. Hoyt and L. M. Gierasch, Hydrophobic Content and Lipid Interactions of Wild–Type and Mutant OmpA Signal Peptides Correlate with Their In Vivo Function, Biochemistry, 30, 10155–10163 (1991).


94. A. Bansal and L. M. Gierasch, The NPXY Internalization Signal of the LDL Receptor Adopts a Reverse Turn Conformation, Cell, 67, 1195–1201 (1991).


95. J. Rizo, M. M. Dhingra, and L. M. Gierasch, Peptide Models for Reverse Turns, The Role of Asparagine in the i Position of a β Turn, in Molecular Conformation and Biological Interactions, P. Balaram and S. Ramaseshan, Eds., Indian Academy of Sciences, Bangalore, India pp. 469–496 (1991).


96. L. M. Gierasch, Relation of Amino Acid Sequence to Structure and Folding, in Conformations and Forces in Protein Folding, Barry T. Nall and Ken A. Dill, Eds., American Association for the Advancement of Science, Washington, D.C., pp. 67–68 (1991).


97. S. J. Landry, R. Jordan, R. McMacken, and L. M. Gierasch, Different Conformations for the Same Polypeptide Bound to Chaperones DnaK and GroEL, Nature, 355, 455–457 (1992).


98. L. M. Gierasch, J. D. Jones, S. J. Landry, and S. J. Stradley, Biophysical Studies of Recognition Sequences for Targeting and Folding, Antonie van Leeuwenhoek, Journal of Microbiology, 61, 93–99 (1992).


99. S. J. Stradley, Y. Reiss, M. S. Brown, J. L. Goldstein, and L. M. Gierasch, Tetrapeptides Compete with p21^ras for Farnesylation Catalyzed by Protein Farnesyltransferase, in Peptides: Chemistry and Biology, J. A. Smith, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 933–934 (1992).


100. J. Rizo, F. Blanco, B. Kobe, M. D. Bruch, D. W. Hoyt, and L. M. Gierasch, Conformations of Wild–type and Mutant OmpA Signal Sequencesin Membrane–Mimetic Environments, in Peptides: Chemistry and Biology, J. A. Smith, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 265–267 (1992).


101. R. J. Bienstock, S. C. Koerber, J. Rizo, J. Rivier, A. T. Hagler, and L. M. Gierasch, Conformation of a Highly Potent Bicyclic GnRH Antagonist by Combined Molecular Dynamics and Two–Dimensional NMR Analyses, in Peptides: Chemistry and Biology, J. A. Smith, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 262–264 (1992).


102. S. J. Landry and L. M. Gierasch, Recognition of Peptides by the E. coli Molecular Chaperones, GroEL and DnaK, in Peptides: Chemistry and Biology, J. A. Smith, Ed., ESCOM Science Publishers, Leiden, The Netherlands, pp. 206–208 (1992).


103. J. Rizo and L. M. Gierasch, Constrained Peptides: Models of Bioactive Peptides and Protein Substructures, Ann. Rev. Biochem., 61, 387–418 (1992).


104. B. Nagel, H. Dellweg and L. M. Gierasch, Glossary for Chemists of Terms Used in Biotechnology (IUPAC Recommendations 1992), Pure & Appl. Chem., 64, 143–168 (1992).


105. J. Rizo, S. C. Koerber, R. J. Bienstock, J. Rivier, A. T. Hagler, and L. M. Gierasch, Conformational Analysis of a Highly Potent, Constrained Gonadotropin–Releasing Hormone Antagonist I. Nuclear Magnetic Resonance, J. Am. Chem. Soc., 114, 2852–2859 (1992).


106. J. Rizo, S. C. Koerber, R. J. Bienstock, J. Rivier, L. M. Gierasch, and A. T. Hagler, Conformational Analysis of a Highly Potent, Constrained Gonadotropin–Releasing Hormone Antagonist II. Molecular Dynamics Simulations, J. Am. Chem. Soc., 114, 2860–2871 (1992).


107. W. Zhi, S. J. Landry, L. M. Gierasch, and P. A. Srere, Renaturation of Citrate Synthase: Influence of Denaturant and Folding Assistants, Protein Sci., 1, 522–529 (1992).


108. J. Zhang, Z.–P. Liu, T. A. Jones, L. M. Gierasch, and J. F. Sambrook, Mutating the Charged Residues in the Binding Pocket of Cellular Retinoic Acid–Binding Protein Simultaneously Reduces Its Binding Affinity to Retinoic Acid and Increases Its Thermostability, Proteins: Structure, Function, and Genetics, 13, 87–99 (1992).


109. J. Rivier, S. Koerber, C. Rivier, A. Hagler, M. Perrin, L. Gierasch, A. Corrigan, J. Porter, and W. Vale, Design, Physico–Chemical Characterization, and Biological Activity of Gonadotropin Releasing Hormone (GnRH) Antagonists as Potential Contraceptives, in Proceedings of the International Symposium on Frontiers in Reproductive Research: the Role of Growth Factors Oncogenes, Receptors and Gonadal Polypeptides, Li, Chen, Hahn and McGuire, Eds., Beijing Medical University, The National Institute of Child Health and Human Development, U. S. Department of Health and Human Services, pp. 15–37 (1992).


110. A. N. Stroup, A. L. Rockwell, and L. M. Gierasch, Solution Conformation of Two Flexible Cyclic Pentapeptides: cyclo(Gly–Pro–D–Phe–Gly–Ala) and cyclo(Gly–Pro–D–Phe–Gly–Val), Biopolymers, 32, 1713–1725 (1992).


111. Z.–P. Liu and L. M. Gierasch, Combined Use of Molecular Dynamics Simulations and NMR to Explore Peptide Bond Isomerization and Multiple Intramolecular Hydrogen Bonding Possibilities in a Cyclic Pentapeptide, Cyclo(Gly–Pro–D–Phe–Gly–Val), Biopolymers, 32, 1727–1739 (1992).


112. M. D. Bruch, J. Rizo, and L. M. Gierasch, Impact of a Micellar Environment on the Conformations of Two Cyclic Pentapeptides, Biopolymers, 32, 1741–1754 (1992).


113. J. Rizo, F. J. Blanco, B. Kobe, M. D. Bruch and L. M. Gierasch, Conformational Behavior of E. coli OmpA Signal Peptides in Membrane Mimetic Environments, Biochemistry, 32, 4881–4894 (1993).


114. S. J. Landry, J. Zeilstra–Ryalls, O. Fayet, C. Georgopoulos, and L. M. Gierasch, Characterization of a Functionally Important Mobile Domain of GroES, Nature, 364, 255–258 (1993).


115. R. J. Bienstock, J. Rizo, S. C. Koerber, A. T. Hagler, J. Rivier, and L. M. Gierasch, Conformational Analysis of a Highly Potent Dicyclic Gonadotropin–Releasing Hormone Antagonist by Nuclear Magnetic Resonance and Molecular Dynamics, J. Med. Chem, 36, 3265–3273 (1993).


116. J. D. Miller, H. Wilhelm, L. M. Gierasch, R. Gilmore and P. Walter, GTP Binding and Hydrolysis by the Signal Recognition Particle During Initiation of Protein Translocation, Nature, 366, 351–354 (1993).


117. S. J. Stradley, J. Rizo, and L. M. Gierasch, The Conformation of a Heptapeptide Substrate Bound to Protein Farnesyltransferase, Biochemistry, 32, 12586–12590 (1993).


118. Z. Wang, J. D. Jones, J. Rizo, and L. M. Gierasch, Membrane–Bound Conformation of a Signal Peptide: A Transferred Nuclear Overhauser Effect Analysis, Biochemistry, 32, 13991–13999 (1993).


119. L. M. Gierasch, Signal Sequences: Roles and Interactions by Biophysical Methods, in Biological Membranes: Structure, Biogenesis and Dynamics, J.A. F. Op den Kamp, Ed., Springer–Verlag, New York, pp. 191–198 (1993).


120. Z. P. Liu, J. Rizo, and L. M. Gierasch, Equilibrium Folding Studies of Cellular Retinoic Acid Binding Protein, a Predominantly β–Sheet Protein, Biochemistry, 33, 134–142 (1994).


121. L. M. Gierasch, Panning for Chaperone–Binding Peptides, Current Biology, 4, 173–174 (1994).


122. S. J. Landry and L. M. Gierasch, Polypeptide Interactions with Molecular Chaperones and the Relationship to In Vivo Protein Folding, Ann. Rev. Biophys. Biomol. Struct., 23, 645–669 (1994).


123. M. B. Sankaram, D. Marsh, L. M. Gierasch and T. E. Thompson, Reorganization of Lipid Domain Structure in Membranes by a Transmembrane Peptide, Biophys. Journal, 66, 1959–1968 (1994).


124. J. Rizo, R. B. Sutton, J. Breslau, S. C. Koerber, J. Porter, J. E. Rivier, A. T. Hagler and L. M. Gierasch, Defining the Active Conformation of Gonadotropin Releasing Hormone (GnRH) Through Design and Conformational Analysis of Constrained GnRH Analogs, in Proceedings of the Thirteenth American Peptide Symposium, R. S. Hodges and J. A. Smith, Eds., ESCOM Science Publishers, Lieden, The Netherlands, pp. 766–768 (1994).


125. J. D. Jones and L. M. Gierasch, Effect of Charged Residue Substitutions on the Membrane–Interactive Properties of Signal Sequences of the Escherichia coli LamB Protein, Biophys. Journal, 67, 1534–1545 (1994).


126. J. D. Jones and L. M. Gierasch, Effect of Charged Residue Substitutions on the Thermodynamics of Signal Peptide–Lipid Interactions of the Escherichia coli LamB Signal Sequence, Biophys. Journal, 67, 1546–1561 (1994).


127. J. Rizo, Z.–P. Liu and L. M. Gierasch, ¹H and ¹⁵N Resonance Assignments and Secondary Structure of Cellular Retinoic Acid Binding Protein With and Without Bound Ligand, J. Biomol. NMR, 4, 741–760 (1994).


128. C. H. Wu, A. Ramamoorthy, L. M. Gierasch, and S. J. Opella, Simultaneous Characterization of the Amide ¹H–¹⁵N Dipolar, and ¹⁵N Chemical Shift Interaction Tensors in a Peptide Bond by Three–Dimensional Solid–State NMR Spectroscopy, J. Am. Chem. Soc., 117, 6148–6149 (1995).


129. L. M. Gierasch, Z. Wang, J. Hunt, S. J. Landry, A. Weaver, and J. Deisenhofer, Chaperone–Substrate Interactions, Protein Eng., 8, Suppl., 14–18 (1995).


130. M. Sukumar, J. Rizo, M. Wall, L. A. Dreyfus, Y. M. Kuperstoch, and L. M. Gierasch, The Structure of Escherichia coli Heat–Stable Enterotoxin b by Nuclear Magnetic Resonance and Circular Dichroism, Protein Sci., 4, 1718–1729 (1995).


131. A. Ramamoorthy, L. M. Gierasch, and S. J. Opella, Four–Dimensional Solid–State NMR Experiment that Correlates the Chemical Shift and Dipolar Coupling Frequencies of Two Heteronuclei with the Exchange of Dilute Spin Magnetization, J. Magn. Res., Ser. B, 109, 112–116 (1995).


132. J. F. Hunt, A. Weaver, S. J. Landry, L. M. Gierasch, and J. Deisenhofer, The Crystal Structure of the GroES Co–Chaperonin at 2.8 Å Resolution, Nature, 379, 37–45 (1996).


133. J. Rizo and L. M. Gierasch, Peptide and Protein Secondary Structure Elements: β–turns, α–helices and β–sheets, in Encyclopedia of NMR, Eds. D. M. Grant and R. K. Harris, John Wiley & Sons, pp. 3517–3526 (1996).


134. A. Ramamoorthy, L. M. Gierasch, and S. J. Opella, Resolved Two–Dimensional Anisotropic Chemical Shift/Heteronuclear Dipolar Coupling Powder Pattern Spectra by Three–Dimensional Solid–State NMR Spectroscopy, J. Magn. Res., Ser. B, 110, 102–106 (1996).


135. J. Rizo, R. B. Sutton, J. Breslau, S. C. Koerber, J. Porter, A. T. Hagler, J. E. Rivier, and L. M. Gierasch, A Novel Conformation in a Highly Potent, Constrained Gonadotropin Releasing Hormone Antagonist, J. Am. Chem. Soc., 118, 970–976 (1996).


136. P. L. Clark, Z. P. Liu, J. H. Zhang, and L. M. Gierasch, Intrinsic Tryptophans of CRABPI as Probes of Structure and Folding, Protein Sci., 5, 1108–1117 (1996).


137. N. Zheng and L. M. Gierasch, Signal Sequences: The Same Yet Different, Cell, 86, 849–852 (1996).


138. B. Bechinger, L. M. Gierasch, M. Montal, M. Zasloff, and S. J. Opella, Orientations of Helical Peptides in Membrane Bilayers by Solid–State NMR Spectroscopy, J. Solid State Nuclear Magnetic Resonance, 7, 185–191 (1996).


139. A. Ramamoorthy, L. M. Gierasch, and S. J. Opella, Three–Dimensional Solid–State NMR Correlation Experiment with ¹H Homonuclear Spin–Exchange, J. Magn. Reson. B, 111, 81–84 (1996).


140. J. Rivier, G. C. Jiang, S. L. Lahrichi, J. Porter, S. C. Koerber, J. Rizo, A. Corrigan, L. Gierasch, A. Hagler, W. Vale, and C. Rivier. Dose relationship between GnRH antagonists and pituitary suppression. Hum. Reprod. (Suppl.) 3, 133–147 (1996).


141. M. Sukumar and L. M. Gierasch, Local Interactions in a Schellman Motif Dictate Interhelical Arrangement in a Protein Fragment, Folding & Design, 2, 211–222 (1997).


142. P. L. Clark, Z.–P. Liu, J. Rizo, and L. M. Gierasch, Cavity Formation Before Stable Hydrogen Bonding in the Folding of a β–clam Protein, Nature Struct. Biol., 4, 883–886 (1997).


143. N. Zheng and L. M. Gierasch, Domain Interactions in E. coli SRP: Stabilization of M Domain by RNA Is Required for Effective Signal Sequence Modulation of NG Domain, Mol. Cell, 1, 79–87 (1997).


144. N. Zheng, J. L. Feltham, and L. M. Gierasch, In Vitro Studies of the Interactions Between Signal Peptides and Signal Recognition Factors, in Molecular Mechanisms of Lipid and Protein Traffic, J. A. F. Op den Kamp, Ed., Springer–Verlag, pp. 125–139 (1998).


145. Z. P. Liu, J. Rizo, and L. M. Gierasch, Protein Folding, in Bioorganic Chemistry, S. M. Hecht, Ed., Oxford Press, pp. 224–257 (1998).


146. H. P. Feng and L. M. Gierasch, Molecular Chaperones: Clamps for the Clips, Current Biology, 8, R464–R467 (1998).


147. R. G. Kibbey, J. Rizo, L. M. Gierasch, R. G. W. Anderson, The LDL Receptor Clustering Motif Interacts with the Clathrin Terminal Domain in a Reverse Turn Conformation, J. Cell Biol., 142, 59–67 (1998).


148. P. L. Clark, B. F. Weston, and L. M. Gierasch, Probing the Folding Pathway of a β–Clam Protein with Single–Tryptophan Constructs, Folding & Design, 3, 401–412 (1998).


149. S. J. Eyles, I. Kaltashov, and L. M. Gierasch, Probing the Folding and Unfolding Dynamics of Cellular Retinoic Acid–Binding Protein Using H/D Exchange and Electrospray Ionization Mass Spectrometry, Proc. Amer. Soc. Mass Spectrom., 46, 380 (1998).


150. D. L. Montgomery, R. I. Morimoto, and L. M. Gierasch, Mutations in the Substrate Binding Domain of the Escherichia coli 70 kDa Molecular Chaperone, DnaK, which Alter Substrate Affinity or Interdomain Coupling, J. Mol. Biol., 286, 915–932 (1999).


151. K. S. Rotondi and L. M. Gierasch, Using Peptides to Study the Folding of a Predominantly β–sheet Protein, in Peptide Science—Present and Future, Y. Shimonishi, Ed., Kluwer Acad. Publ., pp. 228–231 (1999).


152. P. L. Clark, Z.–P. Liu, J. Rizo, M. Sukumar, K. S. Rotondi, and L. M. Gierasch, Folding of a Predominantly β Sheet Protein with a Central Cavity, in Peptides: Frontiers of Peptide Science, J.P. Tam and P. T. P. Kaumaya, Eds., Kluwer/ESCOM, pp. 349–351 (1999).


153. Z. Wang, H. P. Feng, S. J. Landry, J. Maxwell, and L. M. Gierasch, Basis of Substrate Binding by the Chaperonin GroEL, Biochemistry, 38, 12537–12546 (1999).


154. S. J. Eyles, T. Dresch, L. M. Gierasch, and I. A. Kaltashov, Unfolding Dynamics of a β–sheet Protein Studied by Mass Spectrometry, J. Mass Spectrometry, 34, 1289–1295 (1999).


155. S. J. Eyles, J. P. Speir, G. H. Kruppa, L. M. Gierasch, and I. A. Kaltashov, Protein Conformational Stability Probed by Fourier Transform Ion Cyclotron Resonance Mass Spectrometry, J. Am. Chem. Soc., 122, 495–500 (2000).


156. J. L. Feltham and L. M. Gierasch, GroEL–Substrate Interactions: Molding the Fold, or Folding the Mold? Cell, 100, 193–196 (2000).


157. M. Pellecchia, D. L. Montgomery, S. Y. Stevens, C. W. Vander Kooi, H. P. Feng, L. M. Gierasch, and E. R. P. Zuiderweg, Structural Insights into Substrate Binding by the Molecular Chaperone DnaK, Nat. Struct. Biol., 7, 298–303 (2000).


158. S. J. Eyles and L. M. Gierasch, Multiple Roles of Prolyl Residues in Structure and Folding. J. Mol. Biol., 301, 737–747 (2000).


159. V. Krishnan, M. Sukumar, L. M. Gierasch, and M. Cosman, Dynamics of Cellular Retinoic Acid Binding Protein I on Multiple Time Scales with Implications for Ligand Binding, Biochemistry, 39, 9119–9129 (2000).


160. K. S. Rotondi, K. Gunasekaran, and L. M. Gierasch, Investigating the Roles of Turns in the Folding of a Predominantly β–Sheet Protein, in Peptides for the New Millennium, G. B. Fields, J.P. Tam and G. Barany, Eds., Kluwer/ESCOM, 32–33 (2000).


161. S. J. Eyles, J. A. Habink, K. Gunasekaran, and L. M. Gierasch, Roles of Proline Residues in the Structure and Folding of a β–Clam Protein, in Peptides for the New Millennium, G. B. Fields, J.P. Tam and G. Barany, Eds., Kluwer/ESCOM, pp. 313–315 (2000).


162. K. Gunasekaran, S. J. Eyles, A. T. Hagler, and L. M. Gierasch, Keeping It in the Family: Folding Studies of Related Proteins, Curr. Opin. Struc. Biol., 11, 83–93 (2001).


163. J. F. Swain, and L.M. Gierasch, Signal Peptides Bind and Aggregate RNA: an Alternative Explanation for GTPase Inhibition in the Signal Recognition Particle, J. Biol. Chem., 276, 12222–12227 (2001).


164. R. M. Cleverley, N. Zheng, and L. M. Gierasch, The Cost of Exposing a Hyrophobic ‘Finger’ Loop and Implications for the Functional Role of 4.5S RNA in the E. coli SRP, J. Biol. Chem., 276, 19327–19331 (2001).


165. T. L. Triplett, A. R. Sgrignoli, F. B. Gao, Y. B. Yang, P. C. Tai, and L. M. Gierasch, Functional Signal Peptides Bind a Soluble N–terminal Fragment of SecA and Inhibit Its ATPase Activity, J. Biol. Chem., 276, 19648–19655 (2001).


166. J. F. Swain, R. Sivendran, and L. M. Gierasch, Defining the Structure of the Substrate–free State of the DnaK Molecular Chaperone, in Biochemical Society Symposia No. 68: From Protein Folding to New Enzymes, A. Berry and S. E. Radford, Eds. Portland Press Ltd., London, 69–82 (2001).


167. C. M. McIntosh, K. S. Rotondi, M. Dhanasekaran, K. Gunasekaran, A. Kazantzis, A. Kapurniotu, and L. M. Gierasch, Conformational Analysis of Human Calcitonin in Aqueous Solution and Comparison with a Highly Potent Lactam–bridged Analogue, in Proceedings of the Seventeenth American Peptide Symposium, 338–339 (2001).


168. L. M. Gierasch, K. S. Rotondi, K. Gunasekaran, J. A. Habink, and A. T. Hagler, Local and Long–Range Sequence Contributions to the Folding of a Predominantly β–Sheet Protein, in Proceedings of the Seventeenth American Peptide Symposium, 391–393 (2001).


169. L. M. Gierasch, Caught in the Act: How ATP Binding Triggers Cooperative Conformational Changes in a Molecular Machine, Mol. Cell, 9, 3–5 (2002).


170. J. F. Swain and L. M. Gierasch, A New Twist for an Hsp70 Chaperone, Nat. Struct. Biol., 9, 406–408 (2002).


171. R. M. Cleverley, and L. M. Gierasch, Mapping the Signal Sequence–binding Site on SRP Reveals A Significant Role for the NG–domain, J. Biol. Chem., 277, 46763–46768 (2002).


172. Y. T. Chou, J. F. Swain, and L. M. Gierasch, Functionally Significant Mobile Regions of Escherichia coli SecA ATPase Identified by NMR, J. Biol. Chem., 277, 50985–50990 (2002).


173. J. Benach, Y. T. Chou, J. J. Fak, A. Itkin, D. D. Nicolae, P. C. Smith, G. Wittrock, D. L. Floyd, C. M. Golsaz, L. M. Gierasch, and J. F. Hunt, Phospholipid–Induced Monomerization and Signal Peptide–Induced Oligomerization of SecA, J. Biol. Chem., 278, 3628–3638 (2003).


174. K. S. Rotondi, L. F. Rotondi, and L. M. Gierasch, Native Structural Propensity in Cellular Retinoic Acid Binding Protein I 64–88: The Role of Locally Encoded Structure in the Folding of a β–barrel Protein, Biophys. Chem., 100, 421–436 (2003).


175. M. Kabani, S. H. Stewart, M. W. Morrow, D. L. Montgomery, R. Sivendran, M. D. Rose, L. M. Gierasch, and J. L. Brodsky, Dependence of Endoplasmic Reticulum Associated Degradation on the Peptide Binding Domain and Concentration of BiP, Mol. Biol. Cell, 14, 3437–3448 (2003).


176. K. S. Rotondi and L. M. Gierasch, The Role of Local Sequence in the Folding of Cellular Retinoic Acid–Binding Protein 1: Structural Propensities of Reverse Turns, Biochemistry, 42, 7976–7985 (2003).


177. K. S. Rotondi and L. M. Gierasch, The Role of Local Sequence in the Folding of Cellular Retinoic Acid–Binding Protein 1: Specific Residue Roles in β–Turns, Peptide Science, 71, 638–651 (2003).


178. K. Gunasekaran, A. T. Hagler, and L. M. Gierasch, Sequence and Structural Analysis of Cellular Retinoic Acid Binding Proteins Reveals a Network of Conserved Hydrophobic Interactions, Proteins: Structure Function and Bioinformatics, 54, 179–194 (2004).


179. Z. Ignatova and L. M. Gierasch, Monitoring Protein Stability and Aggregation In Vivo by Real–Time Fluorescent Labeling, Proc. Natl. Acad. Sci. USA, 101, 523–528 (2004).


180. J. J. Fak, A. Itkin, D. D. Ciobanu, E. C. Lin, X.–J. Song, Y.–T. Chou, L. M. Gierasch, and J. F. Hunt, Nucleotide Exchange from the High–Affinity ATP–Binding Site in SecA Is the Rate–Limiting Step in the ATPase Cycle of the Soluble Enzyme and Occurs through a Specialized Conformational State, Biochemistry, 43, 7307–27 (2004).


181. K. S. Rotondi and L. M. Gierasch, Solution Structure of Daptomycin, in Peptide Revolution: Genomics, Proteomics & Therapeutics, (M. Chorev and T. Sawyer, eds.), pp. 447–449 (2004).


182. K. S. Rotondi and L. M. Gierasch, A Well–Defined Amphipathic Conformation for the Calcium–Free Cyclic Lipopeptide Antibiotic, Daptomycin, in Aqueous Solution, Peptide Science, 80, 374–385 (2005).


183. N. Sinha, C. V. Grant, K. S. Rotondi, L. Feduik–Rotondi, L. M. Gierasch, and S. J. Opella, Peptides and the Development of Double– and Triple– Resonance Solid–State NMR of Aligned Samples, J. Pept. Res., 65, 605–620 (2005).


184. Z. Ignatova and L. M. Gierasch, Aggregation of a Slow–folding Mutant of a β–Clam Protein Proceeds through a Monomeric Nucleus, Biochemistry, 44, 7266–7274 (2005).


185. Y.–T. Chou and L. M. Gierasch, The Conformation of a Signal Peptide Bound by Escherichia coli Preprotein Translocase SecA, J. Biol. Chem., 280, 32753–32760 (2005).


186. J. F. Swain and L. M. Gierasch, First Glimpses of a Chaperonin–bound Folding Intermediate, Proc. Natl. Acad. Sci. USA, 102, 13715–13716 (2005).


187. R. G. Smock and L. M. Gierasch, Finding the Fittest Fold: Using the Evolutionary Record to Design New Proteins, Cell, 122, 832–834 (2005).


188. US Patent 6,991,927 B2, “Applying Far Infrared Radiation to Biological Matter,“ Inventors: M. R. Mross, T. H. Lowell, R. Durant, N. Dyer, L. M. Gierasch, and G. H. Pollack. Issued January 31, 2006.


189. K. S. Rotondi and L. M. Gierasch, Natural Polypeptide Scaffolds: β–Sheets, β–Turns, and β–Hairpins, Peptide Science, 84, 13–22 (2006).


190. J. F. Swain, E. G. Schulz, and L. M. Gierasch, Direct Comparison of a Stable Isolated Hsp70 Substrate–binding Domain in the Empty and Substrate–bound States, J. Biol. Chem., 281, 1605–11 (2006).


191. J. F. Swain and L. M. Gierasch, The Changing Landscape of Protein Allostery. Curr. Opin. Struct. Biol. 16, 102–108 (2006).


192. A. C. Marcelino, R. G. Smock, and L. M. Gierasch, Evolutionary Coupling of Structural and Functional Sequence Information in the Intracellular Lipid–Binding Protein Family, Proteins: Structure Function Bioinformatics, 63, 373–384 (2006).


193. Z. Ignatova and L. M. Gierasch, Extended PolyQ Tracts Cause Aggregation and Structural Perturbation of a Neighboring β–Barrel Protein, J. Biol. Chem., 281, 12959–67 (2006).


194. I. L. Mainprize, D. R. Beniac, E. Falkovskaia, R. M. Cleverley, L. M. Gierasch, F. P. Ottensmeyer, and D. W. Andrews, The Structure of E. coli Signal Recognition Particle Revealed by Scanning Transmission Electron Microscopy, Mol. Biol. Cell, 17:5063-74 (2006).


195. Cavanaugh LF, Palmer AG 3rd, Gierasch LM, Hunt JF. Disorder Breathes Life into a DEAD Motor, Nat Struct Mol Biol, 13, 566-9 (2006).


196. Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci, 103, 13357-61 (2006).


197. Lin BR, Gierasch LM, Jiang C, Tai PC. Electrophysiological Studies in Xenopus Oocytes for the Opening of Escherichia coli SecA-Dependent Protein-Conducting Channels. J Membr Biol 214, 103-13 (2006).


198. Ignatova Z, Krishnan B, Bombardier JP, Marcelino AM, Hong J, Gierasch LM. From the test tube to the cell: Exploring the folding and aggregation of a beta-clam protein. Biopolymers 88, 157-63 (2007).


199. Krishnan B, Szymanska A, Gierasch LM. Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des 69, 31-40 (2007).


200. Gierasch LM. In memoriam: A true statesman of science, Elkan R. Blout. Biopolymers 85, vi (2007).


201. Swain JF, Dinler G, Sivendran R, Montgomery DL, Stotz M, Gierasch LM. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol Cell 26, 27-39 (2007).


202. Ignatova Z, Gierasch LM. Effects of osmolytes on protein folding and aggregation in cells. Methods Enzymol 428, 355-72 (2007).


203. Clérico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers 90, 307-19 (2007).


204. Ignatova Z, Thakur AK, Wetzel R, Gierasch LM. In-cell aggregation of a polyglutamine-containing chimera is a multi-step process initiated by the flanking sequence. JBC 282, 36736-43 (2007).


205. Ignatova Z, Gierasch LM. A Fluorescent Window into Protein Folding and Aggregation in Cells. Methods Cell Biol. 89:59-70 (2008).


206. Marcelino AM, Gierasch LM. Roles of β-turns in protein folding: From peptide models to protein engineering. Biopolymers 89, 380-91 (2008).


207. Gierasch LM, Deber CM, Brodsky B. Celebrating the scientific legacy of Elkan R. Blout. Biopolymers 89, 323 (2008).


208. Hinz J, Gierasch LM, Ignatova Z. Orthogonal Cross-Seeding: An Approach To Explore Protein Aggregates In Living Cells. Biochemistry 47, 4196-4200 (2008).


209. Ghosh RP, Horowitz-Scherer RA, Nikitina T, Gierasch LM, Woodcock CL. Rett syndrome-causing mutations in human MeCP2 result in diverse structural changes that impact folding and DNA interactions. JBC 283, 20523-34 (2008).


210. Krishnan B, Gierasch LM. Cross-Strand Split Tetra-Cys Motifs as Structure Sensors in a β-Sheet Protein. Chem Biol 15, 1104-15 (2008).


211. Ignatova Z, Gierasch LM. A Method for Direct Measurement of Protein Stability In Vivo. Methods Mol. Biol. 490: 165-78 (2009).


212. Smock RG, Gierasch LM. Sending signals dynamically. Science 324: 198-203 (2009).


213. Clérico EM, Szymanska A, Gierasch LM. Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary cross-linking methods. Biopolymers 92:201-11(2009).


214. Hebert DN, Gierasch LM. The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner. Mol Cell 34:635-6 (2009).


215. Gierasch LM, Gershenson A. Post-reductionist protein science, or putting Humpty Dumpty back together again. Nat Chem Biol 5:774-7 (2009).


216. Eyles SJ, Gierasch LM. Nature's molecular sponges: Small heat shock proteins grow into their chaperone roles. PNAS 107: 2727-8 (2010).


217. Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry 49: 4395-410 (2010).


218. Clérico EM, Zhuravleva A, Smock RG, Gierasch LM. Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers 94: 742-52 (2010).


219. Hong J, Gierasch LM. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. J Am Chem Soc 132:10445-52 (2010).


220. Liu Y, Gierasch LM, Bahar I. Role of Hsp70 ATPase Domain Intrinsic Dynamics and Sequence Evolution in Enabling its Functional Interactions with NEFs. PLoS Comp Bio 6:9 (2010).


221. Smock RG, Rivoire O, Russ WP, Swain JF, Leibler S, Ranganathan R, Gierasch LM. An interdomain sector mediating allostery in Hsp70 molecular chaperones. Mol Sys Bio 6:414 (2010).


222. Gershenson A, Gierasch LM. Protein folding in the cell: challenges and progress. Curr Opin Struct Biol 21:32 (2011).


223. Gierasch, LM. How One Bad Protein Spoils the Barrel: Structural Details of β(2)-Microglobulin Amyloidogenicity. Mol Cell 41:129 (2011).


224. Krishnan B, Gierasch LM. Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat Struct Mol Biol 18:222 (2011).


225. Gierasch LM. A career pathway in protein folding: from model peptides to postreductionist protein science. Protein Sci 20:783 (2011).


226. Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. PNAS 108:6987 (2011).


227. Smock RG, Blackburn ME and Gierasch LM. The conserved, disordered C-terminus of DnaK enhances in vitro chaperone function and cellular survival upon stress. J Biol Chem 286:31821 (2011).


228. Wang Q, Zhuravleva A, Gierasch LM. Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy. Biochemistry 50:9225-9236 (2011).


229. Maki JL, Krishnan B, and Gierasch LM. Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry 51:1369-79 (2012).


230. Powers ET, Powers DL, and Gierasch LM. FoldEco: A model for proteostasis in E. coli. Cell Reports 1:265-276 (2012).


231. Horwich AL, Buchner J, Smock RG, Gierasch LM, and Saibil HR. Chaperones and Protein Folding. Comprehensive Biophysics Vol. 3, V. Daggett, Editor, Elsevier, pp. 212-237 (2012).


232. Hebert DN, Chandrasekhar KD, and Gierasch LM. You got to know when to hold (or unfold) 'em\85 Mol. Cell 48:3-4 (2012).


233. Zhuravleva A, Clerico EM, and Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151:1296-307 (2012).


234. Budyak I, Krishnan B, Marcelino-Cruz A, Ferrolino M, Zhuravleva A, and Gierasch LM. Early folding events protect aggregation-prone regions of a beta-rich protein. Structure 21:476-485 (2013).


235. Hingorani K and Gierasch LM. How bacteria survive an acid trip. Proc. Natl. Acad. Sci. USA 110:5279-80 (2013).


236. Budyak IL, Zhuravleva A, and Gierasch LM. The role of aromatic-aromatic interactions in strand-strand stabilization of β-sheets. J Mol Biol. 425:3522-35 (2013).


237. Ferrolino MC, Zhuravleva A, Budyak IL, Krishnan B, Gierasch LM. Delicate Balance between Functionally Required Flexibility and Aggregation Risk in a Beta-Rich Protein. Biochemistry. 52:8843-54 (2013).


238. Clerico EM and Gierasch LM. Structure and function of Hsp70 molecular chaperones. \93Inhibitors of Molecular Chaperones as Therapeutic Agents\94 T. D. Machajewski and Z. Gao, Editors, Royal Society of Chemistry Publishers, Ch. 3, pp. 65-125 (2014).


239. Hingorani KS, Gierasch LM. Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Curr Opin Struct Biol. 24:81-90 (2014).


240. General IJ, Liu Y, Blackburn ME, Mao W, Gierasch LM, Bahar I. ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones. PLoS Comput Biol. 10:e1003624. (2014).


241. Theillet FX, Binolfi A, Frembgen-Kesner T, Hingorani K, Sarkar M, Kyne C, Li C, Crowley PB, Gierasch L, Pielak GJ, Elcock AH, Gershenson A, Selenko P. Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs). Chem Rev. 114:6661-714 (2014).


242. Gershenson A, Gierasch LM, Pastore A, Radford S. Energy landscapes of functional proteins are inherently risky. Nat Chem Biol. 10:884-91 (2014).


243. Chien P, Gierasch LM. Challenges and dreams: physics of weak interactions essential to life. Mol Biol Cell. 25:3474-7 (2014).


244. Clerico EM, Tilitsky JM, Meng W, Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J Mol Biol. 427:1575-88 (2015).


245. Cho Y, Zhang X, Pobre KF, Liu Y, Powers DL, Kelly JW, Gierasch LM, Powers ET. Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli. Cell Rep. 11:321-33 (2015).


246. Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proc Natl Acad Sci U S A. 112:E2865-73 (2015).


247. Hong J, Gierasch LM, Liu Z. Its Preferential Interactions with Biopolymers Account for Diverse Observed Effects of Trehalose. Biophys J. 109:144-53 (2015).


248. Chandrasekhar K, Ke H, Wang N, Goodwin T, Gierasch LM, Gershenson A, Hebert DN. Cellular folding pathway of a metastable serpin. Proc Natl Acad Sci U S A. 113:6484-9 (2016).


249. Hebert DN, Clerico EM, Gierasch LM. Division of labor: ER-resident BiP co-chaperones martch substrates to fates based on specific binding sequences. Mol. Cell 63: 721-723 (2016).


250. Gierasch LM. Hsp70 molecular chaperones: Versatile modular nanomachines that mediate multiple biological functions. "Structure and Action of Molecular Chaperones" L. M. Gierasch, A. L. Horwich, C. Slingsby, S. Wickner, and D. Agard, Editors. World Scientific Publishers, Ch. 1, pp. 1-48 (2016).


251. Hingorani KS, Metcalf MC, Deming DT, Garman SC, Powers ET, Gierasch LM. Ligand-promoted protein folding by biased kinetic partitioning. Nat Chem Biol.13: 369-371 (2017).


252. Lai AL, Clerico EM, Blackburn ME, Patel NA, Robinson CV, Borbat PP, Freed JH, Gierasch LM. Key features of an Hsp70 chaperone allosteric landscape revealed by ion mobility native mass spectrometry and double electron-electron resonance. JBC 292(21):8773-8785 (2017).


253. Krishnan B, Hedstrom L, Hebert DN, Gierasch LM, Gershenson A. Expression and Purification of Active Recombinant Human Alpha-1 Antitrypsin (AAT) from Escherichia coli. Methods Mol Biol. 1639:195-209 (2017).


254. English CA, Sherman W, Meng W, Gierasch LM.The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains. JBC 292(36):14765-14774 (2017).


255. Thakur AK, Meng W, Gierasch LM.Local and non-local topological information in the denatured state ensemble of a \DF-barrel protein. Protein Sci. 12, 2062-2072 (2018).


256. Meng W, Clerico W, McArthur N, and Gierasch LM. The allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proc. Natl. Acad. Sci. U.S.A., 115, 11970-11975 (2018).


257. Mayer MP and Gierasch LM. Hsp70 Molecular Chaperones: Emerging Concepts. J. Biol. Chem., REV118.002810 (2018).


258. Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. Biochem J. 476(11):1653-1677 Review (2019).


259. Pobre KFR, Powers DL, Ghosh K, Gierasch LM, and Powers ET. Kinetic vs. Thermodynamic Control of Mutational Effects on Protein Homeostasis: A Perspective from Computational Modeling and Experiment. Protein Sci 28(7):1324-1339 (2019).


260. Adams BM, H. H, Gierasch LM, Gershenson A, and Hebert DN. Proper secretion of the serpin antithrombin relies strictly on thiol-dependent quality control.J Biol Chem 294: 18992-19011 (2019).


261. Berman HM, Gierasch LM, How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 1. J Biol Chem 296, 100608 (2021).


262. Berman HM, Gierasch LM, How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 2.J Biol Chem 296, 100748 (2021).


263. Powers ET, Gierasch LM. The proteome folding problem and cellular proteostasis.J Mol Biol 433: 167197 (2021).


264. Clerico EM, Pozhidaeva AK, Jansen RM, Özden C, Tilitsky JM, Gierasch LM. Selective promiscuity in binding of the E. coli Hsp70 chaperone to an unfolded protein. Proc Natl Acad Sci USA 118: e2016962118 (2021).


265. Nordquist EB, English CA, Clerico EM, Sherman W, Gierasch LM, Chen J. Physics- based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones. PLoS Comput Biol 17: e1009567 (2021).


266. Clerico EM, Gierasch LM. There are more Hsp90 chaperone mechanisms in heaven and earth, dear reader, than are dreamt of in your philosophy. Mol Cell 82:1403-1404 (2022).


267. Ke H, Guay KP, Flotte TR, Gierasch LM, Gershenson A, Hebert DN. Secretion of functional α1-antitrypsin is cell type dependent: Implications for intramuscular delivery for gene therapy. Proc Natl Acad Sci USA 119: e2206103119 (2022).


268. Nordquist EB, Clerico EM, Chen J, Gierasch LM. Computationally-aided modeling of Hsp70-client interactions: Past, present, and future. J Phys Chem B 126: 6780-6791 (2022).


269. Kaur U, Kihn KC, Ke H, Kuo W, Gierasch LM, Hebert DN, Wintrode PL, Deredge D, Gershenson A. The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality control. BioRxiv 2023.04.24.537978 (2023).


270. Guay KP, Ke H, Canniff NP, George GT, Eyles SJ, Mariappan M, Contessa JN, Gershenson A, Gierasch LM, Hebert DN. ER chaperones use a protein folding and quality control glyco-code. Mol Cell 83(24):4524-4537 (2023).


271. Guay KP, Ke H, Gierasch LM, Gershenson A, Hebert DN. Monitoring the Secretion and Activity of Alpha-1 Antitrypsin in Various Mammalian Cell Types. Methods Mol Biol 2024;2750:143-163 (2023).


272. Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. J Biol Chem 300(1):105574 (2024).