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Lila M. Gierasch - Publications

University of Massachusetts, Amherst, Amherst, MA 
protein folding

204 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. The Biochemical Journal. 476: 1653-1677. PMID 31201219 DOI: 10.1042/BCJ20170380  0.44
2018 Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proceedings of the National Academy of Sciences of the United States of America. 115: 11970-11975. PMID 30397123 DOI: 10.1073/pnas.1811105115  0.44
2018 Smock RG, Blackburn ME, Gierasch LM. Correction: Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK chaperone activity. The Journal of Biological Chemistry. 293: 14295. PMID 30217867 DOI: 10.1074/jbc.AAC118.005458  1
2017 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 in Molecular Biology (Clifton, N.J.). 1639: 195-209. PMID 28752459 DOI: 10.1007/978-1-4939-7163-3_19  0.44
2017 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. The Journal of Biological Chemistry. PMID 28428246 DOI: 10.1074/jbc.M116.770404  0.56
2016 Hebert DN, Clerico EM, Gierasch LM. Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences. Molecular Cell. 63: 721-3. PMID 27588598 DOI: 10.1016/j.molcel.2016.08.017  0.44
2016 Chandrasekhar K, Ke H, Wang N, Goodwin T, Gierasch LM, Gershenson A, Hebert DN. Cellular folding pathway of a metastable serpin. Proceedings of the National Academy of Sciences of the United States of America. PMID 27222580 DOI: 10.1073/pnas.1603386113  1
2015 Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proceedings of the National Academy of Sciences of the United States of America. 112: E2865-73. PMID 26038563 DOI: 10.1073/pnas.1506692112  1
2015 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 Reports. 11: 321-33. PMID 25843722 DOI: 10.1016/j.celrep.2015.03.018  1
2015 Clerico EM, Tilitsky JM, Meng W, Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. Journal of Molecular Biology. 427: 1575-88. PMID 25683596 DOI: 10.1016/j.jmb.2015.02.004  1
2015 Hong J, Gierasch LM, Liu Z. Its Preferential Interactions with Biopolymers Account for Diverse Observed Effects of Trehalose Biophysical Journal. 109: 144-153. DOI: 10.1016/j.bpj.2015.05.037  1
2014 Chien P, Gierasch LM. Challenges and dreams: physics of weak interactions essential to life. Molecular Biology of the Cell. 25: 3474-7. PMID 25368424 DOI: 10.1091/mbc.E14-06-1035  1
2014 Gershenson A, Gierasch LM, Pastore A, Radford SE. Energy landscapes of functional proteins are inherently risky. Nature Chemical Biology. 10: 884-91. PMID 25325699 DOI: 10.1038/nchembio.1670  1
2014 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). Chemical Reviews. 114: 6661-714. PMID 24901537 DOI: 10.1021/cr400695p  1
2014 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 Computational Biology. 10: e1003624. PMID 24831085 DOI: 10.1371/journal.pcbi.1003624  1
2014 Hingorani KS, Gierasch LM. Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Current Opinion in Structural Biology. 24: 81-90. PMID 24434632 DOI: 10.1016/  1
2013 Ferrolino MC, Zhuravleva A, Budyak IL, Krishnan B, Gierasch LM. Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein. Biochemistry. 52: 8843-54. PMID 24236614 DOI: 10.1021/bi4013462  1
2013 Budyak IL, Zhuravleva A, Gierasch LM. The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets. Journal of Molecular Biology. 425: 3522-35. PMID 23810905 DOI: 10.1016/j.jmb.2013.06.030  1
2013 Hingorani KS, Gierasch LM. How bacteria survive an acid trip. Proceedings of the National Academy of Sciences of the United States of America. 110: 5279-80. PMID 23530238 DOI: 10.1073/pnas.1303297110  1
2013 Budyak IL, Krishnan B, Marcelino-Cruz AM, Ferrolino MC, Zhuravleva A, Gierasch LM. Early folding events protect aggregation-prone regions of a β-rich protein. Structure (London, England : 1993). 21: 476-85. PMID 23454187 DOI: 10.1016/j.str.2013.01.013  1
2013 Gierasch LM, Lynn DG, Schneider JP. The Sixth Peptide Engineering Meeting PEM6, Emory University Conference Center, Atlanta, Georgia, October 2 to 5, 2012 Biopolymers. 100: vii. DOI: 10.1002/bip.22427  1
2012 Gierasch LM, Lynn DG, Schneider J. The Sixth Peptide Engineering Meeting PEM6, Emory University Conference Center, Atlanta, Georgia, October 2 to 5, 2012. Biopolymers. 98: iii. PMID 23325561 DOI: 10.1002/bip.22021  1
2012 Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell. 151: 1296-307. PMID 23217711 DOI: 10.1016/j.cell.2012.11.002  1
2012 Hebert DN, Chandrasekhar KD, Gierasch LM. You got to know when to hold (or unfold) 'em…. Molecular Cell. 48: 3-4. PMID 23062952 DOI: 10.1016/j.molcel.2012.09.022  1
2012 Powers ET, Powers DL, Gierasch LM. FoldEco: a model for proteostasis in E. coli. Cell Reports. 1: 265-76. PMID 22509487 DOI: 10.1016/j.celrep.2012.02.011  1
2012 Maki JL, Krishnan B, Gierasch LM. Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry. 51: 1369-79. PMID 22304380 DOI: 10.1021/bi201793e  1
2012 Horwich AL, Buchner J, Smock RG, Gierasch LM, Saibil HR. Chaperones and protein folding Comprehensive Biophysics. 3: 212-237. DOI: 10.1016/B978-0-12-374920-8.00313-1  1
2011 Wang Q, Zhuravleva A, Gierasch LM. Exploring weak, transient protein--protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry. 50: 9225-36. PMID 21942871 DOI: 10.1021/bi201287e  1
2011 Smock RG, Blackburn ME, Gierasch LM. Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. The Journal of Biological Chemistry. 286: 31821-9. PMID 21768118 DOI: 10.1074/jbc.M111.265835  1
2011 Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proceedings of the National Academy of Sciences of the United States of America. 108: 6987-92. PMID 21482798 DOI: 10.1073/pnas.1014448108  1
2011 Gierasch LM. A career pathway in protein folding: from model peptides to postreductionist protein science. Protein Science : a Publication of the Protein Society. 20: 783-90. PMID 21404361 DOI: 10.1002/pro.615  1
2011 Krishnan B, Gierasch LM. Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nature Structural & Molecular Biology. 18: 222-6. PMID 21258324 DOI: 10.1038/nsmb.1976  1
2011 Gierasch LM. How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity. Molecular Cell. 41: 129-31. PMID 21255721 DOI: 10.1016/j.molcel.2011.01.003  1
2011 Gershenson A, Gierasch LM. Protein folding in the cell: challenges and progress. Current Opinion in Structural Biology. 21: 32-41. PMID 21112769 DOI: 10.1016/  1
2011 Gierasch LM. The power of physical chemistry unleashed on proteins Journal of Physical Chemistry Letters. 2: 327-328. DOI: 10.1021/jz200086z  1
2010 Smock RG, Rivoire O, Russ WP, Swain JF, Leibler S, Ranganathan R, Gierasch LM. An interdomain sector mediating allostery in Hsp70 molecular chaperones. Molecular Systems Biology. 6: 414. PMID 20865007 DOI: 10.1038/msb.2010.65  1
2010 Liu Y, Gierasch LM, Bahar I. Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs. Plos Computational Biology. 6. PMID 20862304 DOI: 10.1371/journal.pcbi.1000931  1
2010 Hong J, Gierasch LM. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. Journal of the American Chemical Society. 132: 10445-52. PMID 20662522 DOI: 10.1021/ja103166y  1
2010 Clerico EM, Zhuravleva A, Smock RG, Gierasch LM. Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers. 94: 742-52. PMID 20564022 DOI: 10.1002/bip.21426  1
2010 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. PMID 20405910 DOI: 10.1021/bi9019753  1
2010 Eyles SJ, Gierasch LM. Nature's molecular sponges: small heat shock proteins grow into their chaperone roles. Proceedings of the National Academy of Sciences of the United States of America. 107: 2727-8. PMID 20133678 DOI: 10.1073/pnas.0915160107  1
2009 Gierasch LM, Gershenson A. Post-reductionist protein science, or putting Humpty Dumpty back together again. Nature Chemical Biology. 5: 774-7. PMID 19841622 DOI: 10.1038/nchembio.241  1
2009 Hebert DN, Gierasch LM. The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner. Molecular Cell. 34: 635-6. PMID 19560414 DOI: 10.1016/j.molcel.2009.06.006  1
2009 Smock RG, Gierasch LM. Sending signals dynamically. Science (New York, N.Y.). 324: 198-203. PMID 19359576 DOI: 10.1126/science.1169377  1
2009 Clérico EM, Szyma?ska A, Gierasch LM. Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers. 92: 201-11. PMID 19280642 DOI: 10.1002/bip.21181  1
2009 Ignatova Z, Gierasch LM. A method for direct measurement of protein stability in vivo. Methods in Molecular Biology (Clifton, N.J.). 490: 165-78. PMID 19157083 DOI: 10.1007/978-1-59745-367-7_7  1
2008 Ignatova Z, Gierasch LM. Chapter 3: A fluorescent window into protein folding and aggregation in cells. Methods in Cell Biology. 89: 59-70. PMID 19118672 DOI: 10.1016/S0091-679X(08)00603-1  1
2008 Krishnan B, Gierasch LM. Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein. Chemistry & Biology. 15: 1104-15. PMID 18940670 DOI: 10.1016/j.chembiol.2008.09.006  1
2008 Gierasch LM. Our field is in good hands. Biopolymers. 90: 479. PMID 18561307 DOI: 10.1002/bip.21026  1
2008 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. The Journal of Biological Chemistry. 283: 20523-34. PMID 18499664 DOI: 10.1074/jbc.M803021200  1
2008 Gierasch LM. A tribute to the career of a gentle giant of peptide science. Biopolymers. 90: 153. PMID 18428152 DOI: 10.1002/bip.20987  1
2008 Hinz J, Gierasch LM, Ignatova Z. Orthogonal cross-seeding: an approach to explore protein aggregates in living cells. Biochemistry. 47: 4196-200. PMID 18330996 DOI: 10.1021/bi800002j  1
2008 Gierasch LM, Deber CM, Brodsky B. Celebrating the scientific legacy of Elkan R. Blout. Biopolymers. 89: 323. PMID 18307218 DOI: 10.1002/bip.20965  1
2008 Marcelino AM, Gierasch LM. Roles of beta-turns in protein folding: from peptide models to protein engineering. Biopolymers. 89: 380-91. PMID 18275088 DOI: 10.1002/bip.20960  1
2008 Clérico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers. 90: 307-19. PMID 17918185 DOI: 10.1002/bip.20856  1
2008 Gierasch LM. Highlighting an exciting topic as discussed in a stimulating venue Biopolymers - Peptide Science Section. 90: 587. DOI: 10.1002/bip.21068  1
2008 Gierasch LM. A message from the editor-in-chief of Biopolymers-Peptide Science Biopolymers. 89: vi. DOI: 10.1002/bip.20896  1
2007 Ignatova Z, Thakur AK, Wetzel R, Gierasch LM. In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. The Journal of Biological Chemistry. 282: 36736-43. PMID 17942400 DOI: 10.1074/jbc.M703682200  1
2007 Ignatova Z, Gierasch LM. Effects of osmolytes on protein folding and aggregation in cells. Methods in Enzymology. 428: 355-72. PMID 17875429 DOI: 10.1016/S0076-6879(07)28021-8  1
2007 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. Molecular Cell. 26: 27-39. PMID 17434124 DOI: 10.1016/j.molcel.2007.02.020  1
2007 Krishnan B, Szymanska A, Gierasch LM. Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chemical Biology & Drug Design. 69: 31-40. PMID 17313455 DOI: 10.1111/j.1747-0285.2007.00463.x  1
2007 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. PMID 17206628 DOI: 10.1002/bip.20665  1
2007 Gierasch LM. New and upcoming Biopolymers - Peptide Science Section. 88: iv. DOI: 10.1002/bip.20876  1
2007 Gierasch LM. Editorial: The Fourth Peptide Engineering Meeting, Yokohama, Japan Biopolymers - Peptide Science Section. 88: 96. DOI: 10.1002/bip.20695  1
2006 Lin BR, Gierasch LM, Jiang C, Tai PC. Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels. The Journal of Membrane Biology. 214: 103-13. PMID 17530158 DOI: 10.1007/s00232-006-0079-1  1
2006 Mainprize IL, Beniac DR, Falkovskaia E, Cleverley RM, Gierasch LM, Ottensmeyer FP, Andrews DW. The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy. Molecular Biology of the Cell. 17: 5063-74. PMID 16987964 DOI: 10.1091/mbc.E06-05-0384  1
2006 Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proceedings of the National Academy of Sciences of the United States of America. 103: 13357-61. PMID 16899544 DOI: 10.1073/pnas.0603772103  1
2006 Gierasch LM. Editorial: Passing of a gentle giant of peptide science: in memoriam, R. Bruce Merrifield. Biopolymers. 84: 433-4. PMID 16850497 DOI: 10.1002/bip.20574  1
2006 Cavanaugh LF, Palmer AG, Gierasch LM, Hunt JF. Disorder breathes life into a DEAD motor. Nature Structural & Molecular Biology. 13: 566-9. PMID 16826229 DOI: 10.1038/nsmb0706-566  1
2006 Ignatova Z, Gierasch LM. Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein. The Journal of Biological Chemistry. 281: 12959-67. PMID 16524881 DOI: 10.1074/jbc.M511523200  1
2006 Marcelino AM, Smock RG, Gierasch LM. Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins. 63: 373-84. PMID 16477649 DOI: 10.1002/prot.20860  1
2006 Swain JF, Gierasch LM. The changing landscape of protein allostery. Current Opinion in Structural Biology. 16: 102-8. PMID 16423525 DOI: 10.1016/  1
2006 Swain JF, Schulz EG, Gierasch LM. Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states. The Journal of Biological Chemistry. 281: 1605-11. PMID 16275641 DOI: 10.1074/jbc.M509356200  1
2006 Rotondi KS, Gierasch LM. Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers. 84: 13-22. PMID 16235261 DOI: 10.1002/bip.20390  1
2006 Gierasch LM. Editorial: Peptides as templates Biopolymers - Peptide Science Section. 84: 1. DOI: 10.1002/bip.20437  1
2005 Smock RG, Gierasch LM. Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 122: 832-4. PMID 16179253 DOI: 10.1016/j.cell.2005.09.005  1
2005 Swain JF, Gierasch LM. First glimpses of a chaperonin-bound folding intermediate. Proceedings of the National Academy of Sciences of the United States of America. 102: 13715-6. PMID 16172384 DOI: 10.1073/pnas.0506510102  1
2005 Chou YT, Gierasch LM. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. The Journal of Biological Chemistry. 280: 32753-60. PMID 16046390 DOI: 10.1074/jbc.M507532200  1
2005 Sinha N, Grant CV, Rotondi KS, Feduik-Rotondi L, Gierasch LM, Opella SJ. Peptides and the development of double- and triple-resonance solid-state NMR of aligned samples. The Journal of Peptide Research : Official Journal of the American Peptide Society. 65: 605-20. PMID 15885119 DOI: 10.1111/j.1399-3011.2005.00262.x  1
2005 Ignatova Z, Gierasch LM. Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus. Biochemistry. 44: 7266-74. PMID 15882065 DOI: 10.1021/bi047404e  1
2005 Rotondi KS, Gierasch LM. A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers. 80: 374-85. PMID 15815985 DOI: 10.1002/bip.20238  1
2005 Deber CM, Gierasch LM. Editorial: The Murray Goodman memorial issue Biopolymers - Peptide Science Section. 80: 59-62. DOI: 10.1002/bip.20255  1
2004 Fak JJ, Itkin A, Ciobanu DD, Lin EC, Song XJ, Chou YT, Gierasch LM, Hunt JF. 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. PMID 15182175 DOI: 10.1021/bi0357208  1
2004 Ignatova Z, Gierasch LM. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proceedings of the National Academy of Sciences of the United States of America. 101: 523-8. PMID 14701904 DOI: 10.1073/pnas.0304533101  1
2004 Gunasekaran K, Hagler AT, Gierasch LM. Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions. Proteins. 54: 179-94. PMID 14696180 DOI: 10.1002/prot.10520  1
2004 Gierasch LM. Biopolymers - Peptide Science Section: Editorial Biopolymers - Peptide Science Section. 76: 281. DOI: 10.1002/bip.20152  1
2004 Gierasch LM. Biopdymers-Peptide Science Section: Editorial Biopolymers - Peptide Science Section. 76: 205. DOI: 10.1002/bip.20097  1
2004 Gierasch LM. Biopolymers-Peptide Science: Inaugural Editorial Biopolymers - Peptide Science Section. 76: 1-2. DOI: 10.1002/bip.20028  1
2003 Rotondi KS, Gierasch LM. Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns. Biopolymers. 71: 638-51. PMID 14991674 DOI: 10.1002/bip.10592  1
2003 Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL. Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Molecular Biology of the Cell. 14: 3437-48. PMID 12925775 DOI: 10.1091/mbc.E02-12-0847  1
2003 Rotondi KS, Gierasch LM. Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns. Biochemistry. 42: 7976-85. PMID 12834350 DOI: 10.1021/bi034304k  1
2003 Rotondi KS, Rotondi LF, Gierasch LM. Native structural propensity in cellular retinoic acid-binding protein I 64-88: the role of locally encoded structure in the folding of a beta-barrel protein. Biophysical Chemistry. 100: 421-36. PMID 12646381 DOI: 10.1016/S0301-4622(02)00296-X  1
2003 Benach J, Chou YT, Fak JJ, Itkin A, Nicolae DD, Smith PC, Wittrock G, Floyd DL, Golsaz CM, Gierasch LM, Hunt JF. Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. The Journal of Biological Chemistry. 278: 3628-38. PMID 12403785 DOI: 10.1074/jbc.M205992200  1
2003 Gierasch LM, Deber CM. Editorial: In Memory of Arno F. Spatola Biopolymers - Peptide Science Section. 71: 601. DOI: 10.1002/bip.10589  1
2002 Chou YT, Swain JF, Gierasch LM. Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR. The Journal of Biological Chemistry. 277: 50985-90. PMID 12397065 DOI: 10.1074/jbc.M209237200  1
2002 Cleverley RM, Gierasch LM. Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. The Journal of Biological Chemistry. 277: 46763-8. PMID 12244111 DOI: 10.1074/jbc.M207427200  1
2002 Swain JF, Gierasch LM. A new twist for an Hsp70 chaperone. Nature Structural Biology. 9: 406-8. PMID 12032550 DOI: 10.1038/nsb0602-406  1
2002 Gierasch LM. Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine. Molecular Cell. 9: 3-5. PMID 11804578 DOI: 10.1016/S1097-2765(02)00432-X  1
2001 Swain JF, Sivendran R, Gierasch LM. Defining the structure of the substrate-free state of the DnaK molecular chaperone. Biochemical Society Symposium. 69-82. PMID 11573348  1
2001 Triplett TL, Sgrignoli AR, Gao FB, Yang YB, Tai PC, Gierasch LM. Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity. The Journal of Biological Chemistry. 276: 19648-55. PMID 11279006 DOI: 10.1074/jbc.M100098200  1
2001 Cleverley RM, Zheng N, Gierasch LM. The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle. The Journal of Biological Chemistry. 276: 19327-31. PMID 11278844 DOI: 10.1074/jbc.M011130200  1
2001 Gunasekaran K, Eyles SJ, Hagler AT, Gierasch LM. Keeping it in the family: folding studies of related proteins. Current Opinion in Structural Biology. 11: 83-93. PMID 11179896 DOI: 10.1016/S0959-440X(00)00173-1  1
2001 Swain JF, Gierasch LM. Signal peptides bind and aggregate RNA. An alternative explanation for GTPase inhibition in the signal recognition particle. The Journal of Biological Chemistry. 276: 12222-7. PMID 11148214 DOI: 10.1074/jbc.M011128200  1
2000 Eyles SJ, Gierasch LM. Multiple roles of prolyl residues in structure and folding. Journal of Molecular Biology. 301: 737-47. PMID 10966780 DOI: 10.1006/jmbi.2000.4002  1
2000 Krishnan VV, Sukumar M, Gierasch LM, Cosman M. Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding. Biochemistry. 39: 9119-29. PMID 10924105 DOI: 10.1021/bi000296l  1
2000 Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER. Structural insights into substrate binding by the molecular chaperone DnaK. Nature Structural Biology. 7: 298-303. PMID 10742174 DOI: 10.1038/74062  1
2000 Feltham JL, Gierasch LM. GroEL-substrate interactions: molding the fold, or folding the mold? Cell. 100: 193-6. PMID 10660042  1
2000 Eyles SJ, Speir JP, Kruppa GH, Gierasch LM, Kaltashov IA. Protein conformational stability probed by fourier transform ion cyclotron resonance mass spectrometry Journal of the American Chemical Society. 122: 495-500. DOI: 10.1021/ja991149h  1
1999 Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. Journal of Mass Spectrometry : Jms. 34: 1289-95. PMID 10587623 DOI: 10.1002/(SICI)1096-9888(199912)34:12<1289::AID-JMS882>3.0.CO;2-U  1
1999 Wang Z, Feng Hp, Landry SJ, Maxwell J, Gierasch LM. Basis of substrate binding by the chaperonin GroEL. Biochemistry. 38: 12537-46. PMID 10504222 DOI: 10.1021/bi991070p  1
1999 Montgomery DL, Morimoto RI, Gierasch LM. Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. Journal of Molecular Biology. 286: 915-32. PMID 10024459 DOI: 10.1006/jmbi.1998.2514  1
1998 Clark PL, Weston BF, Gierasch LM. Probing the folding pathway of a beta-clam protein with single-tryptophan constructs. Folding & Design. 3: 401-12. PMID 9806942 DOI: 10.1016/S1359-0278(98)00053-4  1
1998 Kibbey RG, Rizo J, Gierasch LM, Anderson RG. The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation. The Journal of Cell Biology. 142: 59-67. PMID 9660863 DOI: 10.1083/jcb.142.1.59  1
1998 Feng HP, Gierasch LM. Molecular chaperones: clamps for the Clps? Current Biology : Cb. 8: R464-7. PMID 9651675  1
1997 Zheng N, Gierasch LM. Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain. Molecular Cell. 1: 79-87. PMID 9659905  1
1997 Clark PL, Liu ZP, Rizo J, Gierasch LM. Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein. Nature Structural Biology. 4: 883-6. PMID 9360599 DOI: 10.1038/nsb1197-883  1
1997 Sukumar M, Gierasch LM. Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment. Folding & Design. 2: 211-22. PMID 9269562 DOI: 10.1016/S1359-0278(97)00030-8  1
1997 Clark PL, Sukumar M, Liu ZP, Rizo J, Rotondi K, Gierasch LM. Folding of a predominantly beta sheet protein with a central cavity Faseb Journal. 11: A871.  1
1996 Rivier J, Jiang GC, Lahrichi SL, Porter J, Koerber SC, Rizo J, Corrigan A, Gierasch L, Hagler A, Vale W, Rivier C. Dose relationship between GnRH antagonists and pituitary suppression. Human Reproduction (Oxford, England). 11: 133-47. PMID 9147108 DOI: 10.1093/humrep/11.suppl_3.133  1
1996 Bechinger B, Gierasch LM, Montal M, Zasloff M, Opella SJ. Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy. Solid State Nuclear Magnetic Resonance. 7: 185-91. PMID 9050156 DOI: 10.1016/0926-2040(95)01224-9  1
1996 Zheng N, Gierasch LM. Signal sequences: the same yet different. Cell. 86: 849-52. PMID 8808619 DOI: 10.1016/S0092-8674(00)80159-2  1
1996 Clark PL, Liu ZP, Zhang J, Gierasch LM. Intrinsic tryptophans of CRABPI as probes of structure and folding. Protein Science : a Publication of the Protein Society. 5: 1108-17. PMID 8762142 DOI: 10.1002/pro.5560050613  1
1996 Ramamoorthy A, Gierasch LM, Opella SJ. Three-dimensional solid-state NMR correlation experiment with 1H homonuclear spin exchange. Journal of Magnetic Resonance. Series B. 111: 81-4. PMID 8620287 DOI: 10.1006/jmrb.1996.0063  0.52
1996 Ramamoorthy A, Gierasch LM, Opella SJ. Resolved two-dimensional anisotropic-chemical-shift/heteronuclear dipolar coupling powder-pattern spectra by three-dimensional solid-state NMR spectroscopy. Journal of Magnetic Resonance. Series B. 110: 102-6. PMID 8556232 DOI: 10.1006/jmrb.1996.0016  0.52
1996 Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature. 379: 37-45. PMID 8538739 DOI: 10.1038/379037a0  1
1996 Rizo J, Sutton RB, Breslau J, Koerber SC, Porter J, Hagler AT, Rivier JE, Gierasch LM. A novel conformation in a highly potent, constrained gonadotropin-releasing hormone antagonist Journal of the American Chemical Society. 118: 970-976. DOI: 10.1021/ja953207e  1
1995 Ramamoorthy A, Gierasch LM, Opella SJ. 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. Journal of Magnetic Resonance. Series B. 109: 112-6. PMID 8581306 DOI: 10.1006/jmrb.1995.1157  0.52
1995 Sukumar M, Rizo J, Wall M, Dreyfus LA, Kupersztoch YM, Gierasch LM. The structure of Escherichia coli heat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism. Protein Science : a Publication of the Protein Society. 4: 1718-29. PMID 8528070 DOI: 10.1002/pro.5560040907  1
1995 Wu CH, Ramamoorthy A, Gierasch LM, Opella SJ. Simultaneous characterization of the amide 1H chemical shift, 1H-15N dipolar, and 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR spectroscopy Journal of the American Chemical Society. 117: 6148-6149. DOI: 10.1021/ja00127a039  1
1994 Liu ZP, Rizo J, Gierasch LM. Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly beta-sheet protein. Biochemistry. 33: 134-42. PMID 8286330  1
1994 Sankaram MB, Marsh D, Gierasch LM, Thompson TE. Reorganization of lipid domain structure in membranes by a transmembrane peptide: an ESR spin label study on the effect of the Escherichia coli outer membrane protein A signal peptide on the fluid lipid domain connectivity in binary mixtures of dimyristoyl phosphatidylcholine and distearoyl phosphatidylcholine. Biophysical Journal. 66: 1959-68. PMID 8075330 DOI: 10.1016/S0006-3495(94)80989-0  1
1994 Gierasch LM. Molecular chaperones. Panning for chaperone-binding peptides. Current Biology : Cb. 4: 173-4. PMID 7953525 DOI: 10.1016/S0960-9822(94)00042-4  1
1994 Landry SJ, Gierasch LM. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annual Review of Biophysics and Biomolecular Structure. 23: 645-69. PMID 7919795 DOI: 10.1146/  1
1994 Jones JD, Gierasch LM. Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence. Biophysical Journal. 67: 1546-61. PMID 7819487 DOI: 10.1016/S0006-3495(94)80628-9  1
1994 Jones JD, Gierasch LM. Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein. Biophysical Journal. 67: 1534-45. PMID 7819486 DOI: 10.1016/S0006-3495(94)80627-7  1
1994 Rizo J, Liu ZP, Gierasch LM. 1H and 15N resonance assignments and secondary structure of cellular retinoic acid-binding protein with and without bound ligand. Journal of Biomolecular Nmr. 4: 741-60. PMID 7812151 DOI: 10.1007/BF00398406  1
1994 Gierasch LM. Molecular chaperones: Panning for chaperone-binding peptides Current Biology. 4: 174-174.  1
1993 Rizo J, Blanco FJ, Kobe B, Bruch MD, Gierasch LM. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry. 32: 4881-94. PMID 8387821  1
1993 Wang Z, Jones JD, Rizo J, Gierasch LM. Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry. 32: 13991-9. PMID 8268177  1
1993 Stradley SJ, Rizo J, Gierasch LM. Conformation of a heptapeptide substrate bound to protein farnesyltransferase. Biochemistry. 32: 12586-90. PMID 8251476 DOI: 10.1021/bi00210a006  1
1993 Bienstock RJ, Rizo J, Koerber SC, Rivier JE, Hagler AT, Gierasch LM. Conformational analysis of a highly potent dicyclic gonadotropin-releasing hormone antagonist by nuclear magnetic resonance and molecular dynamics. Journal of Medicinal Chemistry. 36: 3265-73. PMID 8230116  1
1993 Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch LM. Characterization of a functionally important mobile domain of GroES. Nature. 364: 255-8. PMID 8100614 DOI: 10.1038/364255a0  1
1992 Rizo J, Gierasch LM. Constrained peptides: models of bioactive peptides and protein substructures. Annual Review of Biochemistry. 61: 387-418. PMID 1497316 DOI: 10.1146/  1
1992 Bruch MD, Rizo J, Gierasch LM. Impact of a micellar environment on the conformations of two cyclic pentapeptides. Biopolymers. 32: 1741-54. PMID 1472656 DOI: 10.1002/bip.360321215  1
1992 Liu ZP, Gierasch LM. 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: 1727-39. PMID 1472655 DOI: 10.1002/bip.360321214  1
1992 Stroup AN, Rockwell AL, Gierasch LM. Solution conformations of two flexible cyclic pentapeptides: cyclo(Gly-Pro-D-Phe-Gly-Ala) and cyclo(Gly-Pro-D-Phe-Gly-Val). Biopolymers. 32: 1713-25. PMID 1472654 DOI: 10.1002/bip.360321213  1
1992 Zhang J, Liu ZP, Jones TA, Gierasch LM, Sambrook JF. 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. 13: 87-99. PMID 1377826 DOI: 10.1002/prot.340130202  1
1992 Zhi W, Landry SJ, Gierasch LM, Srere PA. Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Science : a Publication of the Protein Society. 1: 522-9. PMID 1363914 DOI: 10.1002/pro.5560010407  1
1992 Gierasch LM, Jones JD, Landry SJ, Stradley SJ. Biophysical studies of recognition sequences for targeting and folding. Antonie Van Leeuwenhoek. 61: 93-9. PMID 1349802 DOI: 10.1007/BF00580613  1
1992 Landry SJ, Jordan R, McMacken R, Gierasch LM. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 355: 455-7. PMID 1346469 DOI: 10.1038/355455a0  1
1992 Nagel B, Dellweg H, Gierasch LM. Glossary for chemists of terms used in biotechnology Pure and Applied Chemistry. 64: 143-168. DOI: 10.1351/pac199264010143  1
1992 Rizo J, Koerber SC, Bienstock RJ, Rivier J, Gierasch LM, Hagler AT. Conformational analysis of a highly potent, constrained gonadotropin-releasing hormone antagonist. 2. Molecular dynamics simulations Journal of the American Chemical Society. 114: 2860-2871.  1
1992 Rizo J, Koerber SC, Bienstock RJ, Rivier J, Hagler AT, Gierasch LM. Conformational analysis of a highly potent, constrained gonadotropin-releasing hormone antagonist. 1. Nuclear magnetic resonance Journal of the American Chemical Society. 114: 2852-2859.  1
1991 McKnight CJ, Stradley SJ, Jones JD, Gierasch LM. Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature region. Proceedings of the National Academy of Sciences of the United States of America. 88: 5799-803. PMID 2062859  1
1991 McKnight CJ, Rafalski M, Gierasch LM. Fluorescence analysis of tryptophan-containing variants of the LamB signal sequence upon insertion into a lipid bilayer. Biochemistry. 30: 6241-6. PMID 2059631  1
1991 Reiss Y, Stradley SJ, Gierasch LM, Brown MS, Goldstein JL. Sequence requirement for peptide recognition by rat brain p21ras protein farnesyltransferase. Proceedings of the National Academy of Sciences of the United States of America. 88: 732-6. PMID 1992464  1
1991 Hoyt DW, Gierasch LM. Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function. Biochemistry. 30: 10155-63. PMID 1931946 DOI: 10.1021/bi00106a012  1
1991 Bruch MD, Dhingra MM, Gierasch LM. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A. Proteins. 10: 130-9. PMID 1896426 DOI: 10.1002/prot.340100206  1
1991 Goldstein JL, Brown MS, Stradley SJ, Reiss Y, Gierasch LM. Nonfarnesylated tetrapeptide inhibitors of protein farnesyltransferase. The Journal of Biological Chemistry. 266: 15575-8. PMID 1874715  1
1991 Hoyt DW, Gierasch LM. A peptide corresponding to an export-defective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes. The Journal of Biological Chemistry. 266: 14406-12. PMID 1860847  1
1991 Hoyt DW, Cyr DM, Gierasch LM, Douglas MG. Interaction of peptides corresponding to mitochondrial presequences with membranes. The Journal of Biological Chemistry. 266: 21693-9. PMID 1834660  1
1991 Bansal A, Gierasch LM. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell. 67: 1195-201. PMID 1760844 DOI: 10.1016/0092-8674(91)90295-A  1
1990 Bruch MD, Gierasch LM. Comparison of helix stability in wild-type and mutant LamB signal sequences Journal of Biological Chemistry. 265: 3851-3858. PMID 2406265  1
1990 Stradley SJ, Rizo J, Bruch MD, Stroup AN, Gierasch LM. 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. PMID 2328290  1
1990 Jones JD, McKnight CJ, Gierasch LM. Biophysical studies of signal peptides: Implications for signal sequence functions and the involvement of lipid in protein export Journal of Bioenergetics and Biomembranes. 22: 213-232. PMID 2202718 DOI: 10.1007/BF00763166  1
1990 Stroup AN, Gierasch LM. 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. PMID 2148688  1
1990 Struthers RS, Tanaka G, Koerber SC, Solmajer T, Baniak EL, Gierasch LM, Vale W, Rivier J, Hagler AT. Design of biologically active, conformationally constrained GnRH antagonists Proteins: Structure, Function and Genetics. 8: 295-304. PMID 2091022 DOI: 10.1002/prot.340080403  1
1990 Stroup AN, Cole LB, Dhingra MM, Gierasch LM. Synthesis and crystal structures of Boc-L-Asn-L-Pro-OBzl · CH3OH and dehydration side product, Boc-β-cyano-L-alanine-L-Pro-OBzl International Journal of Peptide and Protein Research. 36: 531-537. PMID 2090645  1
1989 McKnight CJ, Briggs MS, Gierasch LM. Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties Journal of Biological Chemistry. 264: 17293-17297. PMID 2677003  1
1989 Bruch MD, James McKnight C, Gierasch LM. Helix formation and stability in a signal sequence Biochemistry. 28: 8554-8561. PMID 2605206  1
1989 Cornell DG, Dluhy RA, Briggs MS, McKnight CJ, Gierasch LM. Conformations and orientations of a signal peptide interacting with phospholipid monolayers. Biochemistry. 28: 2789-97. PMID 2525918  1
1989 Lark LR, Berzofsky JA, Gierasch LM. T-cell antigenic peptides from sperm whale myoglobin fold as amphipathic helices: a possible determinant for immunodominance? Peptide Research. 2: 314-321. PMID 2520770  1
1989 Baniak EL, Ma YC, Gierasch LM, Munson B. Ring opening of cyclic pentapeptides by electron impact mass spectrometry: Correlation with peptide bond nonplanarity Journal of the American Chemical Society. 111: 5487-5488.  1
1988 Schiksnis RA, Rockwell AL, Gierasch LM, Opella SJ. Detection of a structural interconversion in a peptide in solution with sensitivity-enhanced 15N chemical-exchange NMR spectroscopy Journal of Magnetic Resonance (1969). 79: 318-321. DOI: 10.1016/0022-2364(88)90223-5  1
1988 Stroup AN, Rockwell AL, Rheingold AL, Gierasch LM. Crystal structure of cyclo(Gly1-L-Pro2-D-Phe3-L-Ala 4-L-Pro5): A cyclic pentapeptide with a Gly-L-Pro δ turn Journal of the American Chemical Society. 110: 5157-5161.  1
1987 Chen L, Tai PC, Briggs MS, Gierasch LM. Protein translocation into Escherichia coli membrane vesicles is inhibited by functional synthetic signal peptides Journal of Biological Chemistry. 262: 1427-1429. PMID 3543005  1
1987 Baniak EL, Rivier JE, Struthers RS, Hagler AT, Gierasch LM. Nuclear magnetic resonance analysis and conformational characterization of a cyclic decapeptide antagonist of gonadotropin-releasing hormone Biochemistry. 26: 2642-2656. PMID 3300777  1
1987 Valentine KG, Rockwell AL, Gierasch LM, Opella SJ. 15N chemical-shift tensor of the imide nitrogen in the alanyl-prolyl peptide bond Journal of Magnetic Resonance (1969). 73: 519-523. DOI: 10.1016/0022-2364(87)90015-1  1
1987 Stroup AN, Rheingold AL, Rockwell AL, Gierasch LM. Crystal structure of cyclo(Gly-L-Pro-D-Phe-Gly-L-Val): An example of a new type of three-residue turn Journal of the American Chemical Society. 109: 7146-7150.  1
1986 Bach AC, Gierasch LM. Dehydrophenylalanine can occur in various reverse-turn sites: Conformational analysis of ΔPhe-containing model peptides Biopolymers. 25: S175-S191. PMID 3779025  1
1986 Mueller L, Frey MH, Rockwell AL, Gierasch LM, Opella SJ. Dynamics of a hydrophobic peptide in membrane bilayers by solid-state nuclear magnetic resonance Biochemistry. 25: 557-561. PMID 3754152 DOI: 10.1021/bi00351a007  1
1986 Briggs MS, Cornell DG, Dluhy RA, Gierasch LM. Conformations of signal peptides induced by lipids suggest initial steps in protein export Science. 233: 206-208. PMID 2941862  1
1986 Briggs MS, Gierasch LM. Molecular Mechanisms of Protein Secretion: The Role of the Signal Sequence Advances in Protein Chemistry. 38: 109-180. DOI: 10.1016/S0065-3233(08)60527-6  1
1986 Spatola AF, Anwer MK, Rockwell AL, Gierasch LM. Compatibility of β- and γ-turn features with a peptide backbone modification: Synthesis and conformational analysis of a model cyclic pseudopentapeptide Journal of the American Chemical Society. 108: 825-831.  1
1985 Jain MK, Rogers J, Simpson L, Gierasch LM. Effect of tryptophan derivatives on the phase properties of bilayers Bba - Biomembranes. 816: 153-162. PMID 4005234 DOI: 10.1016/0005-2736(85)90403-1  1
1985 Gierasch LM, Rockwell AL, Thompson KF, Briggs MS. Conformation-function relationships in hydrophobic peptides: interior turns and signal sequences. Biopolymers. 24: 117-35. PMID 3886031 DOI: 10.1002/bip.360240111  1
1985 Briggs MS, Gierasch LM, Zlotnick A, Lear JD, DeGrado WF. In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides Science. 228: 1096-1099. PMID 3158076 DOI: 10.1126/science.3158076  1
1985 Rose GD, Gierasch LM, Smith JA. Turns in peptides and proteins Advances in Protein Chemistry. 37: 1-109. PMID 2865874  1
1985 Frey MH, Opella SJ, Rockwell AL, Gierasch LM. Solid-state NMR of cyclic pentapeptides Journal of the American Chemical Society. 107: 1946-1951. DOI: 10.1021/ja00293a025  0.52
1985 FREY MH, OPELLA SJ, ROCKWELL AL, GIERASCH LM. ChemInform Abstract: SOLID-STATE NMR OF CYCLIC PENTAPEPTIDES Chemischer Informationsdienst. 16. DOI: 10.1002/chin.198533053  0.52
1985 Gierasch LM, Karle IL, Rockwell AL, Yenal K. 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 Journal of the American Chemical Society. 107: 3321-3327.  1
1985 Frey MH, Opella SJ, Rockwell AL, Gierasch LM. Solid-state NMR of cyclic pentapeptides Journal of the American Chemical Society. 107: 1946-1951.  1
1985 Bruch MD, Noggle JH, Gierasch LM. Conformational analysis of a cyclic pentapeptide by one-and two-dimensional nuclear overhauser effect spectroscopy Journal of the American Chemical Society. 107: 1400-1407.  1
1985 Bach AC, Gierasch LM. Dehydrophenylalanine as the i + 2th residue of a β turn: Synthesis and conformational analysis of cyclo (Gly-Pro-Δz-Phe-D-Ala-Pro) and cyclo (Gly-Pro-D-Phe-D-Ala-Pro) Journal of the American Chemical Society. 107: 3349-3350.  1
1984 Briggs MS, Gierasch LM. Exploring the conformational roles of signal sequences: Synthesis and conformational analysis of λ receptor protein wild-type and mutant signal peptides Biochemistry. 23: 3111-3114. PMID 6380582  1
1984 Thompson KF, Gierasch LM. Conformation of a peptide solubilizate in a reversed micelle water pool Journal of the American Chemical Society. 106: 3648-3652.  1
1983 Rose GD, Young WB, Gierasch LM. Interior turns in globular proteins Nature. 304: 654-657. PMID 6877386 DOI: 10.1038/304654a0  1
1983 Flippen-Anderson JL, Gilardi R, Karle IL, Frey MH, Opella SJ, Gierasch LM, Goodman M, Madison V, Delaney NG. Crystal structures, molecular conformations, infrared spectra, and carbon-13 NMR spectra of methylproline peptides in the solid state Journal of the American Chemical Society. 105: 6609-6614. DOI: 10.1021/ja00360a011  0.52
1983 Bach AC, Baldwin AA, Gierasch LM, Rheingold AL. Characterization of a methoxylated oxazol-5-one derivative: An unexpected by-product in a dehydropeptide synthesis Journal of the Chemical Society, Chemical Communications. 1398-1399.  1
1982 Gierasch LM, Lacy JE, Thompson KF, Rockwell AL, Watnick PI. Conformations of model peptides in membrane-mimetic environments. Biophysical Journal. 37: 275-84. PMID 7055624 DOI: 10.1016/S0006-3495(82)84676-6  1
1982 Bach AC, Bothner-By AA, Gierasch LM. Determination of proline ring nonplanarity from proton spin-spin coupling constants: Applications to two cyclic pentapeptides Journal of the American Chemical Society. 104: 572-576.  1
1981 Gierasch LM, Deber CM, Madison V, Niu CH, Blout ER. Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins. Biochemistry. 20: 4730-8. PMID 7295645  1
1981 Walter TH, McIntire GL, Bancroft EE, Davis ER, Gierasch LM, Blount HN. Interfacial spin trapping in model membrane systems. Biochemical and Biophysical Research Communications. 102: 1350-7. PMID 6274337 DOI: 10.1016/S0006-291X(81)80160-X  1
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