Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM034962-13
Application #
2177674
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1988-01-01
Project End
1998-11-30
Budget Start
1996-09-01
Budget End
1998-11-30
Support Year
13
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Massachusetts Amherst
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
153223151
City
Amherst
State
MA
Country
United States
Zip Code
01003
Maki, Jenny L; Krishnan, Beena; Gierasch, Lila M (2012) Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry 51:1369-79
Clerico, Eugenia M; Szymanska, Aneta; Gierasch, Lila M (2009) Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers 92:201-11
Clerico, Eugenia M; Maki, Jenny L; Gierasch, Lila M (2008) Use of synthetic signal sequences to explore the protein export machinery. Biopolymers 90:307-19
Krishnan, Beena; Gierasch, Lila M (2008) Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein. Chem Biol 15:1104-15
Krishnan, Beena; Szymanska, Aneta; Gierasch, Lila M (2007) Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des 69:31-40
Mainprize, Iain L; Beniac, Daniel R; Falkovskaia, Elena et al. (2006) The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy. Mol Biol Cell 17:5063-74
Lin, Bor-Ruei; Gierasch, Lila M; Jiang, Chun et al. (2006) Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels. J Membr Biol 214:103-13
Chou, Yi-Te; Gierasch, Lila M (2005) The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J Biol Chem 280:32753-60
Swain, Joanna F; Gierasch, Lila M (2005) First glimpses of a chaperonin-bound folding intermediate. Proc Natl Acad Sci U S A 102:13715-6
Fak, John J; Itkin, Anna; Ciobanu, Daita D et al. (2004) 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

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