Recent Publications

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, Szymańska 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).

Clerico 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).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

All Publications