Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Joanna F Swain"'
Autor:
Robert G Smock, Olivier Rivoire, William P Russ, Joanna F Swain, Stanislas Leibler, Rama Ranganathan, Lila M Gierasch
Publikováno v:
Molecular Systems Biology, Vol 6, Iss 1, Pp 1-10 (2010)
Abstract Allosteric coupling between protein domains is fundamental to many cellular processes. For example, Hsp70 molecular chaperones use ATP binding by their actin‐like N‐terminal ATPase domain to control substrate interactions in their C‐te
Externí odkaz:
https://doaj.org/article/b2ba0e6b5cfe4e2a91bd8ce9f67a48bb
Autor:
Dasa Lipovsek, Andrew E Douglas, Mary J. Harner, Michael A. Poss, Fei Yu, Chi-Wang Lin, Joanna F. Swain, Ving G. Lee, Virginie Lafont, Martin C. Wright
Publikováno v:
Angewandte Chemie (International Ed. in English)
Recent improvements in mRNA display have enabled the selection of peptides that incorporate non‐natural amino acids, thus expanding the chemical diversity of macrocycles beyond what is accessible in nature. Such libraries have incorporated non‐na
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97126c94a9dc825fc77df895df68ae30
https://doi.org/10.1002/ange.202103043
https://doi.org/10.1002/ange.202103043
Autor:
Chi‐Wang Lin, Mary J. Harner, Andrew E. Douglas, Virginie Lafont, Fei Yu, Ving G. Lee, Michael A. Poss, Joanna F. Swain, Martin Wright, Daša Lipovšek
Publikováno v:
Angewandte Chemie. 133
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7f0efca19135f96e10da0950ba97ef2
https://doi.org/10.1002/ange.202184261
https://doi.org/10.1002/ange.202184261
Publikováno v:
Journal of Biological Chemistry. 281:1605-1611
The Hsp70 family of molecular chaperones acts to prevent protein misfolding, import proteins into organelles, unravel protein aggregates, and enhance cell survival under stress conditions. These activities are all mediated by recognition of diverse h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d8747b8798357d30797b2b996146127
https://doi.org/10.1074/jbc.m509356200
https://doi.org/10.1074/jbc.m509356200
Autor:
Aaron P. Yamniuk, Joanna F. Swain, D. Kukral, H. Malone, Alexander T. Kozhich, Anjaneya Chimalakonda, Michael K. Ahlijanian, Y. Xiling, Malavi Madireddi
Publikováno v:
Neuromuscular Disorders. 26:S94-S95
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a7d786e6b65fe3530e91eacbce12db7
https://doi.org/10.1016/j.nmd.2016.06.036
https://doi.org/10.1016/j.nmd.2016.06.036
Publikováno v:
Journal of Biological Chemistry. 277:50985-50990
SecA, a 204-kDa homodimeric protein, is a major component of the cellular machinery that mediates the translocation of proteins across the Escherichia coli plasma membrane. SecA promotes translocation by nucleotide-modulated insertion and deinsertion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9328fa798487104e7575905dfabdbaa8
https://doi.org/10.1074/jbc.m209237200
https://doi.org/10.1074/jbc.m209237200
Publikováno v:
Biochemical Society Symposia. 68:69-82
Members of the Hsp70 (heat-shock protein of 70 kDa) family of molecular chaperones bind to exposed hydrophobic stretches on substrate proteins in order to dissociate molecular complexes and prevent aggregation in the cell. Substrate affinity for the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::647414f75c45c730be513741beed34f1
https://doi.org/10.1042/bss0680069
https://doi.org/10.1042/bss0680069
Autor:
Joanna F. Swain, Lila M. Gierasch
Publikováno v:
Journal of Biological Chemistry. 276:12222-12227
N-terminal signal sequences can direct nascent protein chains to the inner membrane of prokaryotes and the endoplasmic reticulum of eukaryotes by interacting with the signal recognition particle. In this study, we show that isolated peptides correspo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9b3cbba02d418b1882f4480e2c2b0cf3
https://doi.org/10.1074/jbc.m011128200
https://doi.org/10.1074/jbc.m011128200
Autor:
Lila M. Gierasch, Joanna F. Swain
Publikováno v:
Nature Structural Biology. 9:406-408
A new study has demonstrated that the E. coli Hsp70, DnaK, can catalyze cis-trans isomerization of non-prolyl peptide bonds.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4488a11e015a45a5382be3db41014f0f
https://doi.org/10.1038/nsb0602-406
https://doi.org/10.1038/nsb0602-406
Autor:
Stanislas Leibler, William P. Russ, Robert G. Smock, Lila M. Gierasch, Joanna F. Swain, Rama Ranganathan, Olivier Rivoire
Publikováno v:
Molecular Systems Biology
The Hsp70 family of molecular chaperones provides a well defined and experimentally powerful model system for understanding allosteric coupling between different protein domains. New extensions to the statistical coupling analysis (SCA) method permit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e96fa13cf997935b1844e52031ed2f6b
https://pubmed.ncbi.nlm.nih.gov/20865007
https://pubmed.ncbi.nlm.nih.gov/20865007