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Lila M Gierasch Ph.D.

TitleDistinguished Professor
InstitutionUniversity of Massachusetts Amherst
DepartmentCollege of Natural Sciences
AddressN331 Life Sciences Lab
Amherst, MA 01003
Phone4135456094
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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. 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. 2022 Apr 21; 82(8):1403-1404. PMID: 35452610.
      Citations:    Fields:    Translation:Cells
    2. 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. 2021 11; 17(11):e1009567. PMID: 34735438.
      Citations:    Fields:    Translation:Cells
    3. Clerico EM, Pozhidaeva AK, Jansen RM, Özden C, Tilitsky JM, Gierasch LM. Selective promiscuity in the binding of E. coli Hsp70 to an unfolded protein. Proc Natl Acad Sci U S A. 2021 10 12; 118(41). PMID: 34625496.
      Citations: 1     Fields:    Translation:Cells
    4. Powers ET, Gierasch LM. The Proteome Folding Problem and Cellular Proteostasis. J Mol Biol. 2021 10 01; 433(20):167197. PMID: 34391802.
      Citations: 1     Fields:    Translation:HumansAnimalsCells
    5. Gierasch LM. Reflecting on an incredible journey with JBC. J Biol Chem. 2021 07; 297(1):100875. PMID: 34218140.
      Citations:    Fields:    
    6. Gierasch LM, Berman HM. How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 2. J Biol Chem. 2021 Jan-Jun; 296:100748. PMID: 33957128.
      Citations:    Fields:    Translation:Cells
    7. Berman HM, Gierasch LM. How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 1. J Biol Chem. 2021 Jan-Jun; 296:100608. PMID: 33785358.
      Citations: 2     Fields:    Translation:Cells
    8. Gierasch LM. Welcome to a new year and a new OPEN ACCESS JBC! J Biol Chem. 2021 Jan-Jun; 296:100199. PMID: 33410397.
      Citations:    Fields:    
    9. Gierasch LM, DeMartino GN. 2021 JBC Herbert Tabor Early Career Investigator Awards: Call for nominations. J Biol Chem. 2020 09 25; 295(39):13697. PMID: 33731253.
      Citations:    Fields:    
    10. Gierasch LM. In JBC we trust. J Biol Chem. 2020 09 18; 295(38):13409. PMID: 33731259.
      Citations:    Fields:    
    11. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. Opening ASBMB publications freely to all. J Lipid Res. 2020 07; 61(7):969-970. PMID: 32398265.
      Citations:    Fields:    
    12. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. Opening ASBMB publications freely to all. Mol Cell Proteomics. 2020 06; 19(6):914-915. PMID: 32398347.
      Citations:    Fields:    
    13. Gierasch LM. Wish you were here: Meetings, no meetings, meeting reports. J Biol Chem. 2020 04 17; 295(16):5534. PMID: 33720016.
      Citations:    Fields:    
    14. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. The data must be accessible to all. J Lipid Res. 2020 04; 61(4):465. PMID: 32071074.
      Citations: 1     Fields:    
    15. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. The Data Must Be Accessible to All. Mol Cell Proteomics. 2020 04; 19(4):569-570. PMID: 32071148.
      Citations: 1     Fields:    
    16. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. The data must be accessible to all. J Biol Chem. 2020 03 27; 295(13):4371. PMID: 32071082.
      Citations: 1     Fields:    Translation:Humans
    17. Gierasch LM. Faster publication advances your science: The three R's. J Biol Chem. 2020 01 10; 295(2):672. PMID: 31924678.
      Citations: 3     Fields:    Translation:Humans
    18. Mayer MP, Gierasch LM. Correction: Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J Biol Chem. 2020 Jan 03; 295(1):288. PMID: 31900370.
      Citations: 1     Fields:    
    19. Pobre KFR, Powers DL, Ghosh K, Gierasch LM, Powers ET. Erratum to "Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment". Protein Sci. 2019 Dec; 28(12):2144. PMID: 31743539.
      Citations:    Fields:    
    20. Adams BM, Ke H, Gierasch LM, Gershenson A, Hebert DN. Proper secretion of the serpin antithrombin relies strictly on thiol-dependent quality control. J Biol Chem. 2019 12 13; 294(50):18992-19011. PMID: 31662433.
      Citations: 2     Fields:    Translation:HumansAnimalsCells
    21. Gierasch LM. Celebrating and cultivating excellent peer review at JBC. J Biol Chem. 2019 09 13; 294(37):13850-13851. PMID: 31519762.
      Citations: 2     Fields:    Translation:Humans
    22. Gierasch LM, DeMartino GN. 2020 Herbert Tabor Early Career Investigator Awards: Call for nominations. J Biol Chem. 2019 09 06; 294(36):13526. PMID: 31492734.
      Citations:    Fields:    Translation:Humans
    23. Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. Biochem J. 2019 06 14; 476(11):1653-1677. PMID: 31201219.
      Citations: 21     Fields:    Translation:HumansCells
    24. Pobre KFR, Powers DL, Ghosh K, Gierasch LM, Powers ET. Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment. Protein Sci. 2019 07; 28(7):1324-1339. PMID: 31074892.
      Citations: 1     Fields:    Translation:Cells
    25. Gierasch LM, DeMartino G. Celebrating science's next generation. J Biol Chem. 2019 03 01; 294(9):3323-3324. PMID: 30824573.
      Citations: 1     Fields:    
    26. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. For the sake of science. J Biol Chem. 2019 02 22; 294(8):2976. PMID: 30760528.
      Citations:    Fields:    Translation:Humans
    27. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. For the sake of science. J Lipid Res. 2019 04; 60(4):719-720. PMID: 30760539.
      Citations: 1     Fields:    
    28. Gierasch LM, Davidson NO, Rye KA, Burlingame AL. For the Sake of Science. Mol Cell Proteomics. 2019 03; 18(3):406-407. PMID: 30760536.
      Citations: 1     Fields:    Translation:Humans
    29. Gierasch LM, Guengerich FP. Celebrating the scientific legacy of Herbert Tabor. J Biol Chem. 2019 02 01; 294(5):1635-1637. PMID: 30710010.
      Citations:    Fields:    Translation:Humans
    30. Gierasch LM. Introducing JBC Reviews. J Biol Chem. 2019 01 04; 294(1):389. PMID: 30610127.
      Citations: 1     Fields:    
    31. Gierasch LM, Guengerich FP. Happy centennial birthday to Herb Tabor, pillar of JBC. J Biol Chem. 2018 11 30; 293(48):18803. PMID: 30504284.
      Citations: 2     Fields:    
    32. Mayer MP, Gierasch LM. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J Biol Chem. 2019 02 08; 294(6):2085-2097. PMID: 30455352.
      Citations: 67     Fields:    Translation:HumansAnimalsCells
    33. Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proc Natl Acad Sci U S A. 2018 11 20; 115(47):11970-11975. PMID: 30397123.
      Citations: 13     Fields:    Translation:HumansAnimalsCells
    34. Thakur AK, Meng W, Gierasch LM. Local and non-local topological information in the denatured state ensemble of a ?-barrel protein. Protein Sci. 2018 12; 27(12):2062-2072. PMID: 30252171.
      Citations: 1     Fields:    Translation:HumansCells
    35. Smock RG, Blackburn ME, Gierasch LM. Correction: Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. J Biol Chem. 2018 09 14; 293(37):14295. PMID: 30217867.
      Citations: 1     Fields:    
    36. Gierasch LM. Looking back at the last two years: Coming home to JBC. J Biol Chem. 2018 07 13; 293(28):11254. PMID: 30006389.
      Citations: 2     Fields:    Translation:Humans
    37. Gierasch LM. A new journal from ASBMB. J Biol Chem. 2018 04 20; 293(16):6212-6213. PMID: 29678890.
      Citations: 1     Fields:    
    38. Gierasch LM, DeMartino G. The Herbert Tabor Young Investigator Awards: Meet the awardees! J Biol Chem. 2018 03 02; 293(9):3468-3469. PMID: 29500271.
      Citations: 3     Fields:    
    39. Gierasch LM. JBC's New Year's resolutions: Check them off! J Biol Chem. 2017 12 29; 292(52):21705-21706. PMID: 29288242.
      Citations: 5     Fields:    
    40. Gierasch LM, DeMartino G. The Herbert Tabor Best Paper Awards: Celebrating young authors who contribute top content to JBC. J Biol Chem. 2017 10 13; 292(41):17576. PMID: 29030539.
      Citations: 4     Fields:    
    41. Gierasch LM. On the costs of scientific publishing. J Biol Chem. 2017 09 29; 292(39):16395-16396. PMID: 28963340.
      Citations: 8     Fields:    
    42. English CA, Sherman W, Meng W, Gierasch LM. The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains. J Biol Chem. 2017 09 08; 292(36):14765-14774. PMID: 28754691.
      Citations: 26     Fields:    Translation:Cells
    43. Gierasch LM. JBC is on a mission to facilitate scientific discovery. J Biol Chem. 2017 04 21; 292(16):6853-6854. PMID: 28432178.
      Citations: 9     Fields:    
    44. 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. J Biol Chem. 2017 05 26; 292(21):8773-8785. PMID: 28428246.
      Citations: 24     Fields:    Translation:Cells
    45. Hingorani KS, Metcalf MC, Deming DT, Garman SC, Powers ET, Gierasch LM. Ligand-promoted protein folding by biased kinetic partitioning. Nat Chem Biol. 2017 04; 13(4):369-371. PMID: 28218913.
      Citations: 7     Fields:    Translation:HumansCells
    46. Guengerich FP, Gierasch LM. What Happens When You Submit a Paper to JBC? J Biol Chem. 2017 01 20; 292(3):1535-1537. PMID: 28108617.
      Citations: 2     Fields:    
    47. 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. 2017; 1639:195-209. PMID: 28752459.
      Citations: 2     Fields:    Translation:HumansCells
    48. Gierasch LM. A Loyal Friend of ASBMB and JBC: Howard Schachman, 1918-2016. J Biol Chem. 2016 09 09; 291(37):19724. PMID: 27613957.
      Citations:    Fields:    Translation:Humans
    49. Hebert DN, Clerico EM, Gierasch LM. Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences. Mol Cell. 2016 09 01; 63(5):721-3. PMID: 27588598.
      Citations: 1     Fields:    Translation:HumansAnimalsCells
    50. Gierasch LM. What's in a Name? J Biol Chem. 2016 08 26; 291(35):19208-9. PMID: 27566814.
      Citations:    Fields:    Translation:HumansAnimalsCells
    51. Gierasch LM. The Journal of Biological Chemistry: 2016 Onward. J Biol Chem. 2016 Jul 01; 291(27):15406-15407. PMID: 27371571.
      Citations: 2     Fields:    
    52. 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. 2016 Jun 07; 113(23):6484-9. PMID: 27222580.
      Citations: 10     Fields:    Translation:HumansAnimalsCells
    53. Hong J, Gierasch LM, Liu Z. Its preferential interactions with biopolymers account for diverse observed effects of trehalose. Biophys J. 2015 Jul 07; 109(1):144-53. PMID: 26153711.
      Citations: 8     Fields:    
    54. Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proc Natl Acad Sci U S A. 2015 Jun 02; 112(22):E2865-73. PMID: 26038563.
      Citations: 59     Fields:    Translation:Cells
    55. 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. 2015 Apr 14; 11(2):321-33. PMID: 25843722.
      Citations: 22     Fields:    Translation:Cells
    56. Clerico EM, Tilitsky JM, Meng W, Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J Mol Biol. 2015 Apr 10; 427(7):1575-88. PMID: 25683596.
      Citations: 124     Fields:    Translation:HumansAnimalsCells
    57. Chien P, Gierasch LM. Challenges and dreams: physics of weak interactions essential to life. Mol Biol Cell. 2014 Nov 05; 25(22):3474-7. PMID: 25368424.
      Citations: 20     Fields:    Translation:Cells
    58. Gershenson A, Gierasch LM, Pastore A, Radford SE. Energy landscapes of functional proteins are inherently risky. Nat Chem Biol. 2014 Nov; 10(11):884-91. PMID: 25325699.
      Citations: 35     Fields:    Translation:HumansCells
    59. 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. 2014 Jul 09; 114(13):6661-714. PMID: 24901537.
      Citations: 113     Fields:    Translation:HumansAnimalsCells
    60. 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. 2014 May; 10(5):e1003624. PMID: 24831085.
      Citations: 35     Fields:    Translation:Cells
    61. Hingorani KS, Gierasch LM. Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Curr Opin Struct Biol. 2014 Feb; 24:81-90. PMID: 24434632.
      Citations: 32     Fields:    Translation:HumansAnimalsCells
    62. Ferrolino MC, Zhuravleva A, Budyak IL, Krishnan B, Gierasch LM. Delicate balance between functionally required flexibility and aggregation risk in a ?-rich protein. Biochemistry. 2013 Dec 10; 52(49):8843-54. PMID: 24236614.
      Citations: 6     Fields:    Translation:AnimalsCells
    63. Gierasch LM, Lynn DG, Schneider JP. The Sixth Peptide Engineering Meeting PEM6, Emory University Conference Center, Atlanta, Georgia, October 2 to 5, 2012. Biopolymers. 2013 Nov; 100(6):vii. PMID: 24281724.
      Citations:    Fields:    Translation:Humans
    64. Budyak IL, Zhuravleva A, Gierasch LM. The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of ?-Sheets. J Mol Biol. 2013 Sep 23; 425(18):3522-35. PMID: 23810905.
      Citations: 12     Fields:    Translation:HumansAnimalsCells
    65. Hingorani KS, Gierasch LM. How bacteria survive an acid trip. Proc Natl Acad Sci U S A. 2013 Apr 02; 110(14):5279-80. PMID: 23530238.
      Citations: 7     Fields:    Translation:Cells
    66. Budyak IL, Krishnan B, Marcelino-Cruz AM, Ferrolino MC, Zhuravleva A, Gierasch LM. Early folding events protect aggregation-prone regions of a ?-rich protein. Structure. 2013 Mar 05; 21(3):476-85. PMID: 23454187.
      Citations: 8     Fields:    Translation:AnimalsCells
    67. Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell. 2012 Dec 07; 151(6):1296-307. PMID: 23217711.
      Citations: 139     Fields:    Translation:Cells
    68. Hebert DN, Chandrasekhar KD, Gierasch LM. You got to know when to hold (or unfold) 'em…. Mol Cell. 2012 Oct 12; 48(1):3-4. PMID: 23062952.
      Citations: 2     Fields:    
    69. Powers ET, Powers DL, Gierasch LM. FoldEco: a model for proteostasis in E. coli. Cell Rep. 2012 Mar 29; 1(3):265-76. PMID: 22509487.
      Citations: 39     Fields:    Translation:Cells
    70. Maki JL, Krishnan B, Gierasch LM. Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry. 2012 Feb 21; 51(7):1369-79. PMID: 22304380.
      Citations: 4     Fields:    Translation:Cells
    71. Gierasch LM, Lynn DG, Schneider J. The Sixth Peptide Engineering Meeting PEM6, Emory University Conference Center, Atlanta, Georgia, October 2 to 5, 2012. Biopolymers. 2012; 98(1):iii. PMID: 23325561.
      Citations:    Fields:    Translation:Humans
    72. 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. 2011 Nov 01; 50(43):9225-36. PMID: 21942871.
      Citations: 52     Fields:    Translation:Cells
    73. Smock RG, Blackburn ME, Gierasch LM. Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. J Biol Chem. 2011 Sep 09; 286(36):31821-9. PMID: 21768118.
      Citations: 34     Fields:    Translation:Cells
    74. Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci U S A. 2011 Apr 26; 108(17):6987-92. PMID: 21482798.
      Citations: 75     Fields:    Translation:Cells
    75. Gierasch LM. A career pathway in protein folding: from model peptides to postreductionist protein science. Protein Sci. 2011 May; 20(5):783-90. PMID: 21404361.
      Citations: 2     Fields:    Translation:Cells
    76. Krishnan B, Gierasch LM. Dynamic local unfolding in the serpin ?-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat Struct Mol Biol. 2011 Feb; 18(2):222-6. PMID: 21258324.
      Citations: 25     Fields:    Translation:HumansCells
    77. Gierasch LM. How one bad protein spoils the barrel: structural details of ?2-microglobulin amyloidogenicity. Mol Cell. 2011 Jan 21; 41(2):129-31. PMID: 21255721.
      Citations:    Fields:    
    78. Gershenson A, Gierasch LM. Protein folding in the cell: challenges and progress. Curr Opin Struct Biol. 2011 Feb; 21(1):32-41. PMID: 21112769.
      Citations: 63     Fields:    Translation:HumansCells
    79. Smock RG, Rivoire O, Russ WP, Swain JF, Leibler S, Ranganathan R, Gierasch LM. An interdomain sector mediating allostery in Hsp70 molecular chaperones. Mol Syst Biol. 2010 Sep 21; 6:414. PMID: 20865007.
      Citations: 67     Fields:    Translation:AnimalsCells
    80. Liu Y, Gierasch LM, Bahar I. Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs. PLoS Comput Biol. 2010 Sep 16; 6(9). PMID: 20862304.
      Citations: 31     Fields:    Translation:HumansAnimalsCells
    81. Hong J, Gierasch LM. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. J Am Chem Soc. 2010 Aug 04; 132(30):10445-52. PMID: 20662522.
      Citations: 53     Fields:    Translation:Cells
    82. 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. 2010 May 25; 49(20):4395-410. PMID: 20405910.
      Citations: 54     Fields:    Translation:HumansCells
    83. Eyles SJ, Gierasch LM. Nature's molecular sponges: small heat shock proteins grow into their chaperone roles. Proc Natl Acad Sci U S A. 2010 Feb 16; 107(7):2727-8. PMID: 20133678.
      Citations: 36     Fields:    Translation:Cells
    84. Clerico EM, Zhuravleva A, Smock RG, Gierasch LM. Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers. 2010; 94(6):742-52. PMID: 20564022.
      Citations: 11     Fields:    Translation:Cells
    85. Gierasch LM, Gershenson A. Post-reductionist protein science, or putting Humpty Dumpty back together again. Nat Chem Biol. 2009 Nov; 5(11):774-7. PMID: 19841622.
      Citations: 36     Fields:    Translation:Cells
    86. 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. 2009 Jun 26; 34(6):635-6. PMID: 19560414.
      Citations: 1     Fields:    Translation:AnimalsCells
    87. Smock RG, Gierasch LM. Sending signals dynamically. Science. 2009 Apr 10; 324(5924):198-203. PMID: 19359576.
      Citations: 211     Fields:    Translation:Cells
    88. 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. 2009; 92(3):201-11. PMID: 19280642.
      Citations: 6     Fields:    Translation:Cells
    89. Ignatova Z, Gierasch LM. A method for direct measurement of protein stability in vivo. Methods Mol Biol. 2009; 490:165-78. PMID: 19157083.
      Citations: 2     Fields:    Translation:Cells
    90. Krishnan B, Gierasch LM. Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein. Chem Biol. 2008 Oct 20; 15(10):1104-15. PMID: 18940670.
      Citations: 16     Fields:    Translation:Cells
    91. 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. J Biol Chem. 2008 Jul 18; 283(29):20523-34. PMID: 18499664.
      Citations: 34     Fields:    Translation:HumansCells
    92. Marcelino AM, Gierasch LM. Roles of beta-turns in protein folding: from peptide models to protein engineering. Biopolymers. 2008 May; 89(5):380-91. PMID: 18275088.
      Citations: 48     Fields:    Translation:Cells
    93. Gierasch LM, Deber CM, Brodsky B. Celebrating the scientific legacy of Elkan R. Blout. Biopolymers. 2008 May; 89(5):323. PMID: 18307218.
      Citations:    Fields:    
    94. Hinz J, Gierasch LM, Ignatova Z. Orthogonal cross-seeding: an approach to explore protein aggregates in living cells. Biochemistry. 2008 Apr 08; 47(14):4196-200. PMID: 18330996.
      Citations: 6     Fields:    Translation:AnimalsCells
    95. Ignatova Z, Gierasch LM. Chapter 3: A fluorescent window into protein folding and aggregation in cells. Methods Cell Biol. 2008; 89:59-70. PMID: 19118672.
      Citations: 1     Fields:    Translation:HumansCells
    96. Clérico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers. 2008; 90(3):307-19. PMID: 17918185.
      Citations: 9     Fields:    Translation:Cells
    97. Gierasch LM. Our field is in good hands. Biopolymers. 2008; 90(4):479. PMID: 18561307.
      Citations:    Fields:    Translation:Humans
    98. Gierasch LM. A tribute to the career of a gentle giant of peptide science. Biopolymers. 2008; 90(3):153. PMID: 18428152.
      Citations:    Fields:    Translation:HumansAnimals
    99. 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. J Biol Chem. 2007 Dec 14; 282(50):36736-43. PMID: 17942400.
      Citations: 32     Fields:    Translation:HumansAnimalsCells
    100. 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. 2006; 214(2):103-13. PMID: 17530158.
      Citations: 13     Fields:    Translation:AnimalsCells
    101. 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. 2007 Apr 13; 26(1):27-39. PMID: 17434124.
      Citations: 165     Fields:    Translation:Cells
    102. Ignatova Z, Gierasch LM. Effects of osmolytes on protein folding and aggregation in cells. Methods Enzymol. 2007; 428:355-72. PMID: 17875429.
      Citations: 12     Fields:    Translation:Cells
    103. 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. 2007; 88(2):157-63. PMID: 17206628.
      Citations: 54     Fields:    Translation:AnimalsCells
    104. Krishnan B, Szymanska A, Gierasch LM. Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des. 2007 Jan; 69(1):31-40. PMID: 17313455.
      Citations: 8     Fields:    Translation:Cells
    105. 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. Mol Biol Cell. 2006 Dec; 17(12):5063-74. PMID: 16987964.
      Citations: 4     Fields:    Translation:Cells
    106. Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci U S A. 2006 Sep 05; 103(36):13357-61. PMID: 16899544.
      Citations: 99     Fields:    Translation:HumansCells
    107. Cavanaugh LF, Palmer AG, Gierasch LM, Hunt JF. Disorder breathes life into a DEAD motor. Nat Struct Mol Biol. 2006 Jul; 13(7):566-9. PMID: 16826229.
      Citations: 4     Fields:    Translation:Cells
    108. Marcelino AM, Smock RG, Gierasch LM. Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins. 2006 May 01; 63(2):373-84. PMID: 16477649.
      Citations: 16     Fields:    Translation:Cells
    109. Ignatova Z, Gierasch LM. Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein. J Biol Chem. 2006 May 05; 281(18):12959-67. PMID: 16524881.
      Citations: 32     Fields:    Translation:HumansCells
    110. Swain JF, Gierasch LM. The changing landscape of protein allostery. Curr Opin Struct Biol. 2006 Feb; 16(1):102-8. PMID: 16423525.
      Citations: 132     Fields:    Translation:Cells
    111. Gierasch LM. Editorial: Passing of a gentle giant of peptide science: in memoriam, R. Bruce Merrifield. Biopolymers. 2006; 84(5):433-4. PMID: 16850497.
      Citations:    Fields:    
    112. Rotondi KS, Gierasch LM. Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers. 2006; 84(1):13-22. PMID: 16235261.
      Citations: 10     Fields:    Translation:Cells
    113. Swain JF, Schulz EG, Gierasch LM. Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states. J Biol Chem. 2006 Jan 20; 281(3):1605-11. PMID: 16275641.
      Citations: 38     Fields:    Translation:Cells
    114. Smock RG, Gierasch LM. Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 2005 Sep 23; 122(6):832-4. PMID: 16179253.
      Citations:    Fields:    Translation:Cells
    115. Swain JF, Gierasch LM. First glimpses of a chaperonin-bound folding intermediate. Proc Natl Acad Sci U S A. 2005 Sep 27; 102(39):13715-6. PMID: 16172384.
      Citations: 4     Fields:    Translation:Cells
    116. Chou YT, Gierasch LM. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J Biol Chem. 2005 Sep 23; 280(38):32753-60. PMID: 16046390.
      Citations: 13     Fields:    Translation:Cells
    117. 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. J Pept Res. 2005 Jun; 65(6):605-20. PMID: 15885119.
      Citations: 5     Fields:    
    118. Ignatova Z, Gierasch LM. Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus. Biochemistry. 2005 May 17; 44(19):7266-74. PMID: 15882065.
      Citations: 20     Fields:    Translation:Cells
    119. Rotondi KS, Gierasch LM. A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers. 2005; 80(2-3):374-85. PMID: 15815985.
      Citations: 11     Fields:    Translation:Cells
    120. 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. 2004 Jun 15; 43(23):7307-27. PMID: 15182175.
      Citations: 19     Fields:    Translation:Cells
    121. Gunasekaran K, Hagler AT, Gierasch LM. Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions. Proteins. 2004 Feb 01; 54(2):179-94. PMID: 14696180.
      Citations: 18     Fields:    Translation:Cells
    122. Ignatova Z, Gierasch LM. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci U S A. 2004 Jan 13; 101(2):523-8. PMID: 14701904.
      Citations: 77     Fields:    
    123. Rotondi KS, Gierasch LM. Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns. Biochemistry. 2003 Jul 08; 42(26):7976-85. PMID: 12834350.
      Citations: 11     Fields:    Translation:Cells
    124. 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. Mol Biol Cell. 2003 Aug; 14(8):3437-48. PMID: 12925775.
      Citations: 56     Fields:    Translation:AnimalsCells
    125. Rotondi KS, Gierasch LM. Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns. Biopolymers. 2003; 71(6):638-51. PMID: 14991674.
      Citations: 5     Fields:    Translation:Cells
    126. 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. Biophys Chem. 2003; 100(1-3):421-36. PMID: 12646381.
      Citations: 3     Fields:    Translation:Cells
    127. 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. J Biol Chem. 2003 Feb 07; 278(6):3628-38. PMID: 12403785.
      Citations: 47     Fields:    Translation:Cells
    128. Chou YT, Swain JF, Gierasch LM. Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR. J Biol Chem. 2002 Dec 27; 277(52):50985-90. PMID: 12397065.
      Citations: 11     Fields:    Translation:Cells
    129. Cleverley RM, Gierasch LM. Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. J Biol Chem. 2002 Nov 29; 277(48):46763-8. PMID: 12244111.
      Citations: 14     Fields:    Translation:Cells
    130. Swain JF, Gierasch LM. A new twist for an Hsp70 chaperone. Nat Struct Biol. 2002 Jun; 9(6):406-8. PMID: 12032550.
      Citations: 2     Fields:    Translation:Cells
    131. Gierasch LM. Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine. Mol Cell. 2002 Jan; 9(1):3-5. PMID: 11804578.
      Citations: 1     Fields:    Translation:Cells
    132. 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. J Biol Chem. 2001 Jun 01; 276(22):19648-55. PMID: 11279006.
      Citations: 12     Fields:    Translation:Cells
    133. 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. J Biol Chem. 2001 Jun 01; 276(22):19327-31. PMID: 11278844.
      Citations: 5     Fields:    Translation:HumansAnimalsCells
    134. Gunasekaran K, Eyles SJ, Hagler AT, Gierasch LM. Keeping it in the family: folding studies of related proteins. Curr Opin Struct Biol. 2001 Feb; 11(1):83-93. PMID: 11179896.
      Citations: 26     Fields:    Translation:Cells
    135. Swain JF, Gierasch LM. Signal peptides bind and aggregate RNA. An alternative explanation for GTPase inhibition in the signal recognition particle. J Biol Chem. 2001 Apr 13; 276(15):12222-7. PMID: 11148214.
      Citations: 4     Fields:    Translation:Cells
    136. Swain JF, Sivendran R, Gierasch LM. Defining the structure of the substrate-free state of the DnaK molecular chaperone. Biochem Soc Symp. 2001; (68):69-82. PMID: 11573348.
      Citations: 1     Fields:    Translation:Cells
    137. Eyles SJ, Gierasch LM. Multiple roles of prolyl residues in structure and folding. J Mol Biol. 2000 Aug 18; 301(3):737-47. PMID: 10966780.
      Citations: 21     Fields:    Translation:Cells
    138. 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. 2000 Aug 08; 39(31):9119-29. PMID: 10924105.
      Citations: 14     Fields:    Translation:Cells
    139. 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. Nat Struct Biol. 2000 Apr; 7(4):298-303. PMID: 10742174.
      Citations: 77     Fields:    Translation:Cells
    140. Feltham JL, Gierasch LM. GroEL-substrate interactions: molding the fold, or folding the mold? Cell. 2000 Jan 21; 100(2):193-6. PMID: 10660042.
      Citations: 8     Fields:    Translation:Cells
    141. Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. J Mass Spectrom. 1999 Dec; 34(12):1289-95. PMID: 10587623.
      Citations: 11     Fields:    Translation:Cells
    142. Wang Z, Feng Hp, Landry SJ, Maxwell J, Gierasch LM. Basis of substrate binding by the chaperonin GroEL. Biochemistry. 1999 Sep 28; 38(39):12537-46. PMID: 10504222.
      Citations: 23     Fields:    Translation:Cells
    143. 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. J Mol Biol. 1999 Feb 26; 286(3):915-32. PMID: 10024459.
      Citations: 66     Fields:    Translation:Cells
    144. Kibbey RG, Rizo J, Gierasch LM, Anderson RG. The LDL receptor clustering motif interacts with the clathrin terminal domain in a reverse turn conformation. J Cell Biol. 1998 Jul 13; 142(1):59-67. PMID: 9660863.
      Citations: 23     Fields:    Translation:AnimalsCells
    145. Feng HP, Gierasch LM. Molecular chaperones: clamps for the Clps? Curr Biol. 1998 Jun 18; 8(13):R464-7. PMID: 9651675.
      Citations: 2     Fields:    Translation:Cells
    146. Clark PL, Weston BF, Gierasch LM. Probing the folding pathway of a beta-clam protein with single-tryptophan constructs. Fold Des. 1998; 3(5):401-12. PMID: 9806942.
      Citations: 24     Fields:    Translation:Cells
    147. 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. Mol Cell. 1997 Dec; 1(1):79-87. PMID: 9659905.
      Citations: 25     Fields:    Translation:Cells
    148. Clark PL, Liu ZP, Rizo J, Gierasch LM. Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein. Nat Struct Biol. 1997 Nov; 4(11):883-6. PMID: 9360599.
      Citations: 18     Fields:    Translation:Cells
    149. Sukumar M, Gierasch LM. Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment. Fold Des. 1997; 2(4):211-22. PMID: 9269562.
      Citations: 8     Fields:    Translation:Cells
    150. Bechinger B, Gierasch LM, Montal M, Zasloff M, Opella SJ. Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy. Solid State Nucl Magn Reson. 1996 Dec; 7(3):185-91. PMID: 9050156.
      Citations: 21     Fields:    Translation:AnimalsCells
    151. 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. Hum Reprod. 1996 Nov; 11 Suppl 3:133-47. PMID: 9147108.
      Citations: 1     Fields:    Translation:AnimalsCells
    152. Zheng N, Gierasch LM. Signal sequences: the same yet different. Cell. 1996 Sep 20; 86(6):849-52. PMID: 8808619.
      Citations: 27     Fields:    Translation:AnimalsCells
    153. Clark PL, Liu ZP, Zhang J, Gierasch LM. Intrinsic tryptophans of CRABPI as probes of structure and folding. Protein Sci. 1996 Jun; 5(6):1108-17. PMID: 8762142.
      Citations: 23     Fields:    Translation:Cells
    154. Ramamoorthy A, Gierasch LM, Opella SJ. Three-dimensional solid-state NMR correlation experiment with 1H homonuclear spin exchange. J Magn Reson B. 1996 Apr; 111(1):81-4. PMID: 8620287.
      Citations: 11     Fields:    
    155. Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature. 1996 Jan 04; 379(6560):37-45. PMID: 8538739.
      Citations: 97     Fields:    Translation:Cells
    156. 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. J Magn Reson B. 1996 Jan; 110(1):102-6. PMID: 8556232.
      Citations: 2     Fields:    
    157. 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. J Magn Reson B. 1995 Oct; 109(1):112-6. PMID: 8581306.
      Citations: 10     Fields:    Translation:Humans
    158. 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 Sci. 1995 Sep; 4(9):1718-29. PMID: 8528070.
      Citations: 12     Fields:    Translation:Cells
    159. 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. J Biomol NMR. 1994 Nov; 4(6):741-60. PMID: 7812151.
      Citations: 9     Fields:    Translation:Cells
    160. Jones JD, Gierasch LM. Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence. Biophys J. 1994 Oct; 67(4):1546-61. PMID: 7819487.
      Citations: 4     Fields:    Translation:Cells
    161. Jones JD, Gierasch LM. Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein. Biophys J. 1994 Oct; 67(4):1534-45. PMID: 7819486.
      Citations: 14     Fields:    Translation:Cells
    162. 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. Biophys J. 1994 Jun; 66(6):1959-68. PMID: 8075330.
      Citations: 7     Fields:    Translation:Cells
    163. Gierasch LM. Molecular chaperones. Panning for chaperone-binding peptides. Curr Biol. 1994 Feb 01; 4(2):173-4. PMID: 7953525.
      Citations:    Fields:    Translation:HumansAnimalsCells
    164. Liu ZP, Rizo J, Gierasch LM. Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly beta-sheet protein. Biochemistry. 1994 Jan 11; 33(1):134-42. PMID: 8286330.
      Citations: 14     Fields:    Translation:Cells
    165. Landry SJ, Gierasch LM. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu Rev Biophys Biomol Struct. 1994; 23:645-69. PMID: 7919795.
      Citations: 16     Fields:    Translation:AnimalsCells
    166. Wang Z, Jones JD, Rizo J, Gierasch LM. Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry. 1993 Dec 21; 32(50):13991-9. PMID: 8268177.
      Citations: 18     Fields:    Translation:Cells
    167. Stradley SJ, Rizo J, Gierasch LM. Conformation of a heptapeptide substrate bound to protein farnesyltransferase. Biochemistry. 1993 Nov 30; 32(47):12586-90. PMID: 8251476.
      Citations: 5     Fields:    Translation:Cells
    168. Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature. 1993 Nov 25; 366(6453):351-4. PMID: 8247130.
      Citations: 53     Fields:    Translation:Cells
    169. 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. J Med Chem. 1993 Oct 29; 36(22):3265-73. PMID: 8230116.
      Citations: 3     Fields:    Translation:Cells
    170. Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch LM. Characterization of a functionally important mobile domain of GroES. Nature. 1993 Jul 15; 364(6434):255-8. PMID: 8100614.
      Citations: 55     Fields:    Translation:Cells
    171. Rizo J, Blanco FJ, Kobe B, Bruch MD, Gierasch LM. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry. 1993 May 11; 32(18):4881-94. PMID: 8387821.
      Citations: 35     Fields:    Translation:Cells
    172. Bruch MD, Rizo J, Gierasch LM. Impact of a micellar environment on the conformations of two cyclic pentapeptides. Biopolymers. 1992 Dec; 32(12):1741-54. PMID: 1472656.
      Citations: 1     Fields:    Translation:Cells
    173. 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. 1992 Dec; 32(12):1727-39. PMID: 1472655.
      Citations: 2     Fields:    Translation:Cells
    174. 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. 1992 Dec; 32(12):1713-25. PMID: 1472654.
      Citations: 1     Fields:    Translation:Cells
    175. Zhi W, Landry SJ, Gierasch LM, Srere PA. Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci. 1992 Apr; 1(4):522-9. PMID: 1363914.
      Citations: 21     Fields:    Translation:Cells
    176. 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. 1992 Apr; 13(2):87-99. PMID: 1377826.
      Citations: 18     Fields:    Translation:Cells
    177. Gierasch LM, Jones JD, Landry SJ, Stradley SJ. Biophysical studies of recognition sequences for targeting and folding. Antonie Van Leeuwenhoek. 1992 Feb; 61(2):93-9. PMID: 1349802.
      Citations:    Fields:    Translation:Cells
    178. Landry SJ, Jordan R, McMacken R, Gierasch LM. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 1992 Jan 30; 355(6359):455-7. PMID: 1346469.
      Citations: 56     Fields:    Translation:Cells
    179. Rizo J, Gierasch LM. Constrained peptides: models of bioactive peptides and protein substructures. Annu Rev Biochem. 1992; 61:387-418. PMID: 1497316.
      Citations: 29     Fields:    Translation:AnimalsCells
    180. Bansal A, Gierasch LM. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell. 1991 Dec 20; 67(6):1195-201. PMID: 1760844.
      Citations: 65     Fields:    Translation:Cells
    181. Hoyt DW, Cyr DM, Gierasch LM, Douglas MG. Interaction of peptides corresponding to mitochondrial presequences with membranes. J Biol Chem. 1991 Nov 15; 266(32):21693-9. PMID: 1834660.
      Citations: 5     Fields:    Translation:AnimalsCells
    182. Hoyt DW, Gierasch LM. Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function. Biochemistry. 1991 Oct 22; 30(42):10155-63. PMID: 1931946.
      Citations: 15     Fields:    Translation:Cells
    183. Goldstein JL, Brown MS, Stradley SJ, Reiss Y, Gierasch LM. Nonfarnesylated tetrapeptide inhibitors of protein farnesyltransferase. J Biol Chem. 1991 Aug 25; 266(24):15575-8. PMID: 1874715.
      Citations: 27     Fields:    Translation:AnimalsCells
    184. 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. J Biol Chem. 1991 Aug 05; 266(22):14406-12. PMID: 1860847.
      Citations: 10     Fields:    Translation:Cells
    185. Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 1991 Jul 30; 30(30):7359-62. PMID: 1677268.
      Citations: 33     Fields:    Translation:Cells
    186. 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. Proc Natl Acad Sci U S A. 1991 Jul 01; 88(13):5799-803. PMID: 2062859.
      Citations: 12     Fields:    Translation:Cells
    187. McKnight CJ, Rafalski M, Gierasch LM. Fluorescence analysis of tryptophan-containing variants of the LamB signal sequence upon insertion into a lipid bilayer. Biochemistry. 1991 Jun 25; 30(25):6241-6. PMID: 2059631.
      Citations: 5     Fields:    Translation:Cells
    188. Landry SJ, Gierasch LM. Recognition of nascent polypeptides for targeting and folding. Trends Biochem Sci. 1991 Apr; 16(4):159-63. PMID: 1877092.
      Citations: 21     Fields:    Translation:Cells
    189. Reiss Y, Stradley SJ, Gierasch LM, Brown MS, Goldstein JL. Sequence requirement for peptide recognition by rat brain p21ras protein farnesyltransferase. Proc Natl Acad Sci U S A. 1991 Feb 01; 88(3):732-6. PMID: 1992464.
      Citations: 70     Fields:    Translation:HumansAnimalsCells
    190. 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. 1991; 10(2):130-9. PMID: 1896426.
      Citations: 39     Fields:    Translation:Cells
    191. 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-beta-cyano-L-alanine-L-Pro-OBzl. Int J Pept Protein Res. 1990 Dec; 36(6):531-7. PMID: 2090645.
      Citations:    Fields:    Translation:Cells
    192. Stroup AN, Gierasch LM. Reduced tendency to form a beta turn in peptides from the P22 tailspike protein correlates with a temperature-sensitive folding defect. Biochemistry. 1990 Oct 23; 29(42):9765-71. PMID: 2148688.
      Citations: 5     Fields:    Translation:Cells
    193. Jones JD, McKnight CJ, Gierasch LM. Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein export. J Bioenerg Biomembr. 1990 Jun; 22(3):213-32. PMID: 2202718.
      Citations: 17     Fields:    Translation:Cells
    194. Bruch MD, Gierasch LM. Comparison of helix stability in wild-type and mutant LamB signal sequences. J Biol Chem. 1990 Mar 05; 265(7):3851-8. PMID: 2406265.
      Citations: 10     Fields:    Translation:Cells
    195. 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 beta-turns. Biopolymers. 1990 Jan; 29(1):263-87. PMID: 2328290.
      Citations: 5     Fields:    Translation:Cells
    196. 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. 1990; 8(4):295-304. PMID: 2091022.
      Citations: 4     Fields:    Translation:AnimalsCells
    197. Bruch MD, McKnight CJ, Gierasch LM. Helix formation and stability in a signal sequence. Biochemistry. 1989 Oct 17; 28(21):8554-61. PMID: 2605206.
      Citations: 12     Fields:    Translation:Cells
    198. McKnight CJ, Briggs MS, Gierasch LM. Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties. J Biol Chem. 1989 Oct 15; 264(29):17293-7. PMID: 2677003.
      Citations: 22     Fields:    Translation:Cells
    199. Lark LR, Berzofsky JA, Gierasch LM. T-cell antigenic peptides from sperm whale myoglobin fold as amphipathic helices: a possible determinant for immunodominance? Pept Res. 1989 Sep-Oct; 2(5):314-21. PMID: 2520770.
      Citations: 3     Fields:    Translation:AnimalsCells
    200. Cornell DG, Dluhy RA, Briggs MS, McKnight CJ, Gierasch LM. Conformations and orientations of a signal peptide interacting with phospholipid monolayers. Biochemistry. 1989 Apr 04; 28(7):2789-97. PMID: 2525918.
      Citations: 10     Fields:    Translation:Cells
    201. Gierasch LM. Signal sequences. Biochemistry. 1989 Feb 07; 28(3):923-30. PMID: 2653440.
      Citations: 115     Fields:    Translation:Cells
    202. 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. 1987 May 05; 26(9):2642-56. PMID: 3300777.
      Citations: 2     Fields:    Translation:Cells
    203. Chen L, Tai PC, Briggs MS, Gierasch LM. Protein translocation into Escherichia coli membrane vesicles is inhibited by functional synthetic signal peptides. J Biol Chem. 1987 Feb 05; 262(4):1427-9. PMID: 3543005.
      Citations: 19     Fields:    Translation:Cells
    204. Briggs MS, Cornell DG, Dluhy RA, Gierasch LM. Conformations of signal peptides induced by lipids suggest initial steps in protein export. Science. 1986 Jul 11; 233(4760):206-8. PMID: 2941862.
      Citations: 45     Fields:    Translation:Cells
    205. 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. 1986 Feb 11; 25(3):557-61. PMID: 3754152.
      Citations:    Fields:    Translation:Cells
    206. Bach AC, Gierasch LM. Dehydrophenylalanine can occur in various reverse-turn sites: conformational analysis of delta Phe-containing model peptides. Biopolymers. 1986; 25 Suppl:S175-91. PMID: 3779025.
      Citations: 3     Fields:    Translation:Cells
    207. Briggs MS, Gierasch LM. Molecular mechanisms of protein secretion: the role of the signal sequence. Adv Protein Chem. 1986; 38:109-80. PMID: 3541538.
      Citations: 43     Fields:    Translation:Cells
    208. Jain MK, Rogers J, Simpson L, Gierasch LM. Effect of tryptophan derivatives on the phase properties of bilayers. Biochim Biophys Acta. 1985 Jun 11; 816(1):153-62. PMID: 4005234.
      Citations: 5     Fields:    
    209. 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. 1985 May 31; 228(4703):1096-9. PMID: 3158076.
      Citations: 33     Fields:    Translation:Cells
    210. Gierasch LM, Rockwell AL, Thompson KF, Briggs MS. Conformation-function relationships in hydrophobic peptides: interior turns and signal sequences. Biopolymers. 1985 Jan; 24(1):117-35. PMID: 3886031.
      Citations: 1     Fields:    Translation:Cells
    211. Rose GD, Gierasch LM, Smith JA. Turns in peptides and proteins. Adv Protein Chem. 1985; 37:1-109. PMID: 2865874.
      Citations: 187     Fields:    Translation:Cells
    212. Briggs MS, Gierasch LM. Exploring the conformational roles of signal sequences: synthesis and conformational analysis of lambda receptor protein wild-type and mutant signal peptides. Biochemistry. 1984 Jul 03; 23(14):3111-4. PMID: 6380582.
      Citations: 17     Fields:    Translation:Cells
    213. Rose GD, Young WB, Gierasch LM. Interior turns in globular proteins. Nature. 1983 Aug 18-24; 304(5927):654-7. PMID: 6877386.
      Citations: 9     Fields:    Translation:Cells
    214. Gierasch LM, Lacy JE, Thompson KF, Rockwell AL, Watnick PI. Conformations of model peptides in membrane-mimetic environments. Biophys J. 1982 Jan; 37(1):275-84. PMID: 7055624.
      Citations: 6     Fields:    Translation:Cells
    215. Walter TH, McIntire GL, Bancroft EE, Davis ER, Gierasch LM, Blount HN. Interfacial spin trapping in model membrane systems. Biochem Biophys Res Commun. 1981 Oct 30; 102(4):1350-7. PMID: 6274337.
      Citations:    Fields:    
    216. 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. 1981 Aug 04; 20(16):4730-8. PMID: 7295645.
      Citations: 11     Fields:    Translation:Cells
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