LILA GIERASCH

Summary

Affiliation: University of Massachusetts
Country: USA

Publications

  1. pmc Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization
    Beena Krishnan
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, Massachusetts, USA
    Nat Struct Mol Biol 18:222-6. 2011
  2. pmc How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity
    Lila M Gierasch
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Mol Cell 41:129-31. 2011
  3. pmc A career pathway in protein folding: from model peptides to postreductionist protein science
    Lila M Gierasch
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
    Protein Sci 20:783-90. 2011
  4. pmc Protein folding in the cell: challenges and progress
    Anne Gershenson
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA
    Curr Opin Struct Biol 21:32-41. 2011
  5. pmc Sending signals dynamically
    Robert G Smock
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA
    Science 324:198-203. 2009
  6. ncbi request reprint The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA
    Yi Te Chou
    Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003 04510, USA
    J Biol Chem 280:32753-60. 2005
  7. pmc Unique physical properties and interactions of the domains of methylated DNA binding protein 2
    Rajarshi P Ghosh
    Department of Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
    Biochemistry 49:4395-410. 2010
  8. pmc Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein
    Beena Krishnan
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Chem Biol 15:1104-15. 2008
  9. pmc Rett syndrome-causing mutations in human MeCP2 result in diverse structural changes that impact folding and DNA interactions
    Rajarshi P Ghosh
    Department of Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA 01003, USA
    J Biol Chem 283:20523-34. 2008
  10. pmc Use of synthetic signal sequences to explore the protein export machinery
    Eugenia M Clerico
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Biopolymers 90:307-19. 2008

Research Grants

  1. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2000
  2. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2002
  3. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2003
  4. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2003
  5. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2004
  6. Conference Proposal: Protein Folding in the Cell
    LILA GIERASCH; Fiscal Year: 2004
  7. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2004
  8. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2005
  9. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2005
  10. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2006

Collaborators

Detail Information

Publications22

  1. pmc Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization
    Beena Krishnan
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, Massachusetts, USA
    Nat Struct Mol Biol 18:222-6. 2011
    ..Mutations in α₁AT that cause polymerization-induced serpinopathies map to the labile region, suggesting that the evolution of serpin function required sampling of high risk conformations on a dynamic energy landscape...
  2. pmc How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity
    Lila M Gierasch
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Mol Cell 41:129-31. 2011
    ....
  3. pmc A career pathway in protein folding: from model peptides to postreductionist protein science
    Lila M Gierasch
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
    Protein Sci 20:783-90. 2011
    ..In my own case, this has been an epoch of great discovery in protein folding and I feel very fortunate to have participated in it...
  4. pmc Protein folding in the cell: challenges and progress
    Anne Gershenson
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA
    Curr Opin Struct Biol 21:32-41. 2011
    ....
  5. pmc Sending signals dynamically
    Robert G Smock
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA
    Science 324:198-203. 2009
    ..The next stages in the signaling hierarchy-how multiple signals are integrated and how cellular signaling pathways are organized in space and time-present exciting challenges for the future, requiring bold multidisciplinary approaches...
  6. ncbi request reprint The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA
    Yi Te Chou
    Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003 04510, USA
    J Biol Chem 280:32753-60. 2005
    ....
  7. pmc Unique physical properties and interactions of the domains of methylated DNA binding protein 2
    Rajarshi P Ghosh
    Department of Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
    Biochemistry 49:4395-410. 2010
    ..These findings led to new mechanistic and biochemical insights regarding the conformational modulations of this intrinsically disordered protein, and its context-dependent in vivo roles...
  8. pmc Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein
    Beena Krishnan
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Chem Biol 15:1104-15. 2008
    ..This latter design exemplifies the potential of split motifs as structure sensors...
  9. pmc Rett syndrome-causing mutations in human MeCP2 result in diverse structural changes that impact folding and DNA interactions
    Rajarshi P Ghosh
    Department of Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA 01003, USA
    J Biol Chem 283:20523-34. 2008
    ..For each mutation, we examined the extent to which the magnitude of these differences correlated with the severity of RTT patient symptoms...
  10. pmc Use of synthetic signal sequences to explore the protein export machinery
    Eugenia M Clerico
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Biopolymers 90:307-19. 2008
    ..While progress has been made, the absence of atomic resolution structures for complexes of signal peptides and their receptors has definitely left many questions to be answered in the future...
  11. pmc Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    Joanna F Swain
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Amherst, MA 01003, USA
    Mol Cell 26:27-39. 2007
    ..Thus, the energy of ATP binding is used to form a stable interface between the nucleotide- and substrate-binding domains, which results in destabilization of regions of the latter domain and consequent weaker substrate binding...
  12. ncbi request reprint Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family
    Anna Marie C Marcelino
    Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA
    Proteins 63:373-84. 2006
    ..We conclude that an essential and structurally apparent separation of local and global sequence information is conserved throughout the iLBP family...
  13. ncbi request reprint Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions
    Kannan Gunasekaran
    Department of Biochemistry, University of Massachusetts, Amherst 01003, USA
    Proteins 54:179-94. 2004
    ..The analysis also shows the usefulness of considering pair-wise conservation based on a simple classification of amino acids, in analyzing sequences and structures to find common core regions among homologues...
  14. pmc Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine
    Beena Krishnan
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, 710 N Pleasant St, Amherst, MA 01003 9305, USA
    Chem Biol Drug Des 69:31-40. 2007
    ..NTA(2)-BM is a potential fluorophore for selective tagging of proteins in vivo...
  15. ncbi request reprint Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain
    Robert M Cleverley
    Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA
    J Biol Chem 277:46763-8. 2002
    ..Our results suggest that the NG domain forms a substantial part of the binding site for the signal sequence...
  16. ncbi request reprint 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
    Kenneth S Rotondi
    Department of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Biophys Chem 100:421-36. 2003
    ....
  17. pmc Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state
    Jiang Hong
    Department of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA
    J Am Chem Soc 132:10445-52. 2010
    ..Our results demonstrate how macromolecular crowding may influence protein folding by effects on both the unfolded state ensemble and unfolding kinetics...
  18. ncbi request reprint A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution
    Kenneth S Rotondi
    Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Biopolymers 80:374-85. 2005
    ..11, pp. 949-957) or is suggested to populate an alternate conformation (L.-J. Ball, C. M. Goult, J. A. Donarski, J. Micklefield, and V. Ramesh, Organic & Biomolecular Chemistry, 2004, Vol. 2, pp. 1872-1878)...
  19. ncbi request reprint Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states
    Joanna F Swain
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
    J Biol Chem 281:1605-11. 2006
    ..coli DnaK do not interact. We conclude that the isolated substrate-binding domain exists in a stable high affinity state in the absence of influence from a nucleotide-bound ATPase domain...
  20. ncbi request reprint Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein
    Zoya Ignatova
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA
    J Biol Chem 281:12959-67. 2006
    ....
  21. pmc Roles of beta-turns in protein folding: from peptide models to protein engineering
    Anna Marie C Marcelino
    Department of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003, USA
    Biopolymers 89:380-91. 2008
    ..Factors that correlate with the importance of turns in folding indeed include their intrinsic stability, as well as their topological context and their participation in hydrophobic networks within the protein's structure...
  22. ncbi request reprint Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine
    Lila M Gierasch
    Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA
    Mol Cell 9:3-5. 2002
    ..Mechanistically crucial allosteric effects of ATP binding arise from rearrangement of interdomain electrostatic contacts...

Research Grants34

  1. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2000
    ....
  2. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2002
    ..abstract_text> ..
  3. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2003
    ..abstract_text> ..
  4. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2003
    ..Additionally, SecA is an ideal target for antibiotics, since it is uniquely present in bacteria. Enhanced understanding of its mode of recognition will provide a basis for development of new antibacterial agents. ..
  5. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2004
    ..Additionally, SecA is an ideal target for antibiotics, since it is uniquely present in bacteria. Enhanced understanding of its mode of recognition will provide a basis for development of new antibacterial agents. ..
  6. Conference Proposal: Protein Folding in the Cell
    LILA GIERASCH; Fiscal Year: 2004
    ..Poster sessions will allow all participants to interact scientifically with other investigators. Young investigators and women will be well-represented among speakers and encouraged to attend the conference. ..
  7. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2004
    ..g., p53-based cancers, Alzheimer's, Huntington's, Parkinson's, cystic fibrosis, BSE), and enhanced understanding of both will aid design of therapeutic strategies. ..
  8. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2005
    ..g., p53-based cancers, Alzheimer's, Huntington's, Parkinson's, cystic fibrosis, BSE), and enhanced understanding of both will aid design of therapeutic strategies. ..
  9. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2005
    ..Additionally, SecA is an ideal target for antibiotics, since it is uniquely present in bacteria. Enhanced understanding of its mode of recognition will provide a basis for development of new antibacterial agents. ..
  10. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2006
    ..g., p53-based cancers, Alzheimer's, Huntington's, Parkinson's, cystic fibrosis, BSE), and enhanced understanding of both will aid design of therapeutic strategies. ..
  11. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2007
    ..g., p53-based cancers, Alzheimer's, Huntington's, Parkinson's, cystic fibrosis, BSE), and enhanced understanding of both will aid design of therapeutic strategies. ..
  12. Allosteric Mechanism of Hsp70 Molecular Chaperones
    LILA GIERASCH; Fiscal Year: 2009
    ....
  13. Allosteric Mechanism of Hsp70 Molecular Chaperones
    Lila M Gierasch; Fiscal Year: 2010
    ....
  14. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2002
    ..abstract_text> ..
  15. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2001
    ..abstract_text> ..
  16. Allosteric Mechanism of Hsp70 Molecular Chaperones
    LILA GIERASCH; Fiscal Year: 2009
    ....
  17. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 2000
    ..abstract_text> ..
  18. SIGNAL SEQUENCES--CONFORMATION AND MEMBRANE BINDING
    LILA GIERASCH; Fiscal Year: 1999
    ..The bacterial secretory apparatus is also a target for new antibiotics, the design of which will be aided by detailed understanding of the key components. ..
  19. PEPTIDE AND PROTEIN CONFORMATIONS
    LILA GIERASCH; Fiscal Year: 1999
    ....
  20. SIGNAL SEQUENCES--CONFORMATION AND MEMBRANE BINDING
    LILA GIERASCH; Fiscal Year: 2000
    ..The bacterial secretory apparatus is also a target for new antibiotics, the design of which will be aided by detailed understanding of the key components. ..
  21. SIGNAL SEQUENCES--CONFORMATION AND MEMBRANE BINDING
    LILA GIERASCH; Fiscal Year: 2001
    ..The bacterial secretory apparatus is also a target for new antibiotics, the design of which will be aided by detailed understanding of the key components. ..
  22. Predicting Protein Structure with Guided Conformation Space Search
    Lila M Gierasch; Fiscal Year: 2010
    ..This research effort will develop of a novel, efficient, and biologically accurate computational approach to determine the three-dimensional structure of proteins. ..
  23. Signal Sequences -- Conformations and Membrane Binding
    LILA GIERASCH; Fiscal Year: 2006
    ..Additionally, SecA is an ideal target for antibiotics, since it is uniquely present in bacteria. Enhanced understanding of its mode of recognition will provide a basis for development of new antibacterial agents. ..
  24. SIGNAL SEQUENCES--CONFORMATION AND MEMBRANE BINDING
    LILA GIERASCH; Fiscal Year: 2002
    ..The bacterial secretory apparatus is also a target for new antibiotics, the design of which will be aided by detailed understanding of the key components. ..