Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Chavela M Carr"'
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0119563 (2015)
Vital cellular processes, from cell growth to synaptic transmission, rely on membrane-bounded carriers and vesicles to transport molecular cargo to and from specific intracellular compartments throughout the cell. Compartment-specific proteins are re
Externí odkaz:
https://doaj.org/article/891a11ace8564b36af6cce27ad6cb87f
Autor:
Lauren Kustigian, Xue Gong, Wei Gai, Jirapat Thongchol, Junjie Zhang, Jason Puchalla, Chavela M. Carr, Hays S. Rye
Publikováno v:
Traffic. 24:34-47
Membrane-enclosed transport carriers sort biological molecules between stations in the cell in a dynamic process that is fundamental to the physiology of eukaryotic organisms. While much is known about the formation and release of carriers from speci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ce6937ee935e34e766a1fde3bc1ef5f
https://doi.org/10.1111/tra.12875
https://doi.org/10.1111/tra.12875
Autor:
Kelly Krantz, M. E. Bisher, Rajan Thapa, Hays S. Rye, Callie Kobayashi, Chavela M. Carr, Julie Viehweg, Jason Puchalla
Publikováno v:
Journal of Biological Chemistry. 288:26721-26730
The role of clathrin-coated vesicles in receptor-mediated endocytosis is conserved among eukaryotes, and many of the proteins required for clathrin coat assembly and disassembly have orthologs in yeast and mammals. In yeast, dozens of proteins have b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::247d69ac7ef9ba492396c8f04cae16f0
https://doi.org/10.1074/jbc.m113.491753
https://doi.org/10.1074/jbc.m113.491753
Autor:
Daniel N. Brewer, Margaret R. Sallah, Francesca Morgera, Pallavi Gandhi, Mary Munson, Michelle L. Dubuke, Chavela M. Carr
Publikováno v:
Molecular Biology of the Cell
The Sec6 subunit of the multisubunit exocyst tethering complex interacts with the Sec1/Munc18 protein Sec1 and with the t-SNARE Sec9. Assembly of the exocyst upon vesicle arrival at sites of secretion is proposed to release Sec9 for SNARE complex ass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6818b4e064d3b504bbc69605b6af892f
https://doi.org/10.1091/mbc.e11-08-0670
https://doi.org/10.1091/mbc.e11-08-0670
Autor:
Josep Rizo, Chavela M. Carr
Publikováno v:
Current Opinion in Cell Biology. 22:488-495
Sec1/Munc18 (SM) proteins bind to and function with soluble N-ethylmaleimide–sensitive factor attachment protein receptors (SNAREs) at each vesicle fusion site in the cell. The purpose for these interactions is becoming clearer, as what had been in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e055a129fc6091b9cdf51256969acb83
https://doi.org/10.1016/j.ceb.2010.04.006
https://doi.org/10.1016/j.ceb.2010.04.006
Publikováno v:
Nature Cell Biology. 11:1399-1410
The RME1 ATPases are implicated in endocytic recycling. C. elegans RME1 interacts with Amphiphysin to regulate endocytic recycling in vivo and the two proteins cooperate in the generation of cargo carriers in vitro. The interaction is conserved in ot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c099d00e31f927fd4d0a3edfbeace91f
https://doi.org/10.1038/ncb1986
https://doi.org/10.1038/ncb1986
Autor:
Chavela M. Carr, Mary Munson
Publikováno v:
EMBO reports. 8:834-838
Communication between neurons relies on chemical synapses and the release of neurotransmitters into the synaptic cleft. Neurotransmitter release is an exquisitely regulated membrane fusion event that requires the linking of an electrical nerve stimul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6f6c9220d9dbdaab6b65c7d96cb0964
https://doi.org/10.1038/sj.embor.7401051
https://doi.org/10.1038/sj.embor.7401051
Publikováno v:
The Journal of Cell Biology
Proteins of the Sec1 family have been shown to interact with target-membrane t-SNAREs that are homologous to the neuronal protein syntaxin. We demonstrate that yeast Sec1p coprecipitates not only the syntaxin homologue Ssop, but also the other two ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78370f77ed82f81c366667e62114fe6e
https://doi.org/10.1083/jcb.146.2.333
https://doi.org/10.1083/jcb.146.2.333
Autor:
Y. Mao, P. Lyons, Shelly Stone, Anne Marie Quinn, Chavela M. Carr, Michael Sacher, Susan Ferro-Novick
Publikováno v:
Molecular Biology of the Cell. 8:1175-1181
Bet1p is a type II membrane protein that is required for vesicular transport between the endoplasmic reticulum and Golgi complex in the yeast Saccharomyces cerevisiae. A domain of Bet1p, that shows potential to be involved in a coiled-coil interactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4350d09db1d7feb61f136bbb15bd168e
https://doi.org/10.1091/mbc.8.7.1175
https://doi.org/10.1091/mbc.8.7.1175
Publikováno v:
Biochemistry. 33:7361-7367
One popular model for protein folding, the framework model, postulates initial formation of secondary structure elements, which then assemble into the native conformation. However, short peptides that correspond to secondary structure elements in pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::357bccc8080c0c6ab1ad4f451fe8d738
https://doi.org/10.1021/bi00189a042
https://doi.org/10.1021/bi00189a042