Recent Publications

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

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

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

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

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

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

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

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

Clerico EM, Jansen R, Pozhidaeva A, Ozden C, Tilitsky JM, and Gierasch LM, Selective promiscuity in binding of the E. coli Hsp70 chaperone to an unfolded protein. Proc. Natl. Acad. Sci. U.S.A. , Proc Natl Acad Sci U S A118(41):e2016962118 (2021).

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

Gierasch LM and Berman HR, How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 2.  J. Biol. Chem. 296: 100608 (2021).

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

Gierasch LM, Albericio F, and Toniolo C editors, Special Issue: Tribute to Louis A. Carpino. Peptide Science, 112 (2020).

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

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

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

Mayer MP and Gierasch LM. Hsp70 Molecular Chaperones: Emerging Concepts. JBC, 294(6):2085-2097 REV118.002810 (2018).

Meng W, Clerico W, McArthur N, and Gierasch LM. The allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proc Natl Acad Sci U S A 115(47):11970-11975 (2018).

Thakur AK, Meng W, Gierasch LM. Local and non-local topological information in the denatured state ensemble of a ß-barrel protein. Protein Sci. 27(12):2062-2072 (2018).

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

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

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

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

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

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

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

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

Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proc Natl Acad Sci U S A. 112:E2865-73 (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 Rep. 11:321-33 (2015).

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

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

Gershenson A, Gierasch LM, Pastore A, Radford S. Energy landscapes of functional proteins are inherently risky. Nat Chem Biol. 10:884-91 (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). Chem Rev. 114:6661-714 (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 Comput Biol. 10:e1003624. (2014).

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

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

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 (2013).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Krishnan B, Gierasch LM. Cross-Strand Split Tetra-Cys Motifs as Structure Sensors in a β-Sheet Protein. Chem Biol 15, 1104-15 (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. JBC 283, 20523-34 (2008).

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

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

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

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

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

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

Ignatova Z, Gierasch LM. Effects of osmolytes on protein folding and aggregation in cells. Methods Enzymol 428, 355-72 (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. Mol Cell 26, 27-39 (2007).

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

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

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

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