Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Angela A. Lilly"'
Publikováno v:
Protein Science. 18:1860-1868
SecB, a remarkable chaperone involved in protein export, binds diverse ligands rapidly with high affinity and low specificity. Site-directed spin labeling and electron paramagnetic resonance spectroscopy were used to investigate the surface of intera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60500a100d4f479c3352a821a9149d62
https://doi.org/10.1002/pro.197
https://doi.org/10.1002/pro.197
Autor:
Hilary C. Roth, Dylan B. Cooper, Angela A. Lilly, Jennine M. Crane, Linda L. Randall, Virginia F. Smith
Publikováno v:
Journal of Molecular Biology. 382:74-87
In all living cells regulated passage across membranes of specific proteins occurs through a universally conserved secretory channel. In bacteria and chloroplasts, the energy for the mechanical work of moving polypeptides through that channel is prov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a34310e42892fb3922ce8d76ee98048
https://doi.org/10.1016/j.jmb.2008.06.049
https://doi.org/10.1016/j.jmb.2008.06.049
Asymmetric Binding Between SecA and SecB Two Symmetric Proteins: Implications for Function in Export
Autor:
Chunfeng Mao, Jennine M. Crane, Angela A. Lilly, Gseping Liu, Patel Chetankumar Natvarlal, Linda L. Randall, Simon J. S. Hardy
Publikováno v:
Journal of Molecular Biology. 348:479-489
SecB, a small tetrameric chaperone in Escherichia coli, facilitates export of precursor polypeptides from the cytoplasm to the periplasmic space. During this process, SecB displays two modes of binding. As a chaperone, it binds promiscuously to precu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddd97996347167e4984e3897193d0bbb
https://doi.org/10.1016/j.jmb.2005.02.036
https://doi.org/10.1016/j.jmb.2005.02.036
Publikováno v:
Molecular Microbiology. 56:1078-1086
Summary Chemotaxis signalling complexes of Escherichia coli , composed of chemoreceptors, CheA and CheW, form clusters located predominately at cell poles. As the only kind of receptor in a cell, high-abundance recep- tors are polar and clustered whe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1a55b7404aa534a3c87840b6dc8f6c8
https://doi.org/10.1111/j.1365-2958.2005.04593.x
https://doi.org/10.1111/j.1365-2958.2005.04593.x
Autor:
Simon J. S. Hardy, Raghavendar Reddy Sanganna Gari, Carl E. Cheadle, Angela A. Lilly, Linda L. Randall, Yuying Suo, Gavin M. King, Chunfeng Mao
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 110(29)
We have established a reconstitution system for the translocon SecYEG in proteoliposomes in which 55% of the accessible translocons are active. This level corresponds to the fraction of translocons that are active in vitro when assessed in their nati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d015ce29fbaaf07fbc0d670ccea83b4
https://pubmed.ncbi.nlm.nih.gov/23818593
https://pubmed.ncbi.nlm.nih.gov/23818593
Publikováno v:
Proceedings of the National Academy of Sciences. 92:3391-3395
Transmembrane signaling by bacterial chemoreceptors is thought to involve conformational changes within a stable homodimer. We investigated the functional consequences of constraining movement between pairs of helices in the four-helix structure of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6ec0d3c01e7c0d162e442e2e2ebb50f
https://doi.org/10.1073/pnas.92.8.3391
https://doi.org/10.1073/pnas.92.8.3391
Publikováno v:
Methods in Molecular Biology ISBN: 9781603271677
Site-directed spin-labeling and the analysis of proteins by electron paramagnetic resonance spectroscopy provides a powerful tool for identifying sites of contact within protein complexes at the resolution of aminoacyl side chains. Here we describe t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3cb8c53c82b690a06d1f15a8b48b163
https://doi.org/10.1007/978-1-60327-412-8_11
https://doi.org/10.1007/978-1-60327-412-8_11
Autor:
Wayne L. Hubbell, Linda L. Randall, Jennine M. Crane, Angela A. Lilly, Yuying Suo, Chunfeng Mao
Publikováno v:
Journal of molecular biology. 363(1)
Export of protein into the periplasm of Escherichia coli via the general secretory system requires that the transported polypeptides be devoid of stably folded tertiary structure. Capture of the precursor polypeptides before they fold is achieved by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fa29aa2549e50a9ef0303d9e2518722
https://pubmed.ncbi.nlm.nih.gov/16962134
https://pubmed.ncbi.nlm.nih.gov/16962134
Autor:
Yuying Suo, Linda L. Randall, Virginia F. Smith, Wayne L. Hubbell, Chunfeng Mao, Angela A. Lilly, Jennine M. Crane
Publikováno v:
Journal of molecular biology. 353(2)
Export of protein into the periplasm of Escherichia coli via the general secretory system is achieved by action of a ternary complex comprising the polypeptide ligand, the chaperone SecB and SecA, a peripheral component of the membrane translocon, wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e757a144fe8a4e8fa281592642e661e7
https://pubmed.ncbi.nlm.nih.gov/16169560
https://pubmed.ncbi.nlm.nih.gov/16169560
Publikováno v:
Molecular microbiology. 56(4)
Chemotaxis signalling complexes of Escherichia coli, composed of chemoreceptors, CheA and CheW, form clusters located predominantly at cell poles. As the only kind of receptor in a cell, high-abundance receptors are polar and clustered whereas low-ab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d6d97cb7e48a157ddfe5cc9547577a04
https://pubmed.ncbi.nlm.nih.gov/15853891
https://pubmed.ncbi.nlm.nih.gov/15853891