Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Douglas A. Hattendorf"'
Autor:
John R Glover, Susan Lindquist, Douglas A. Hattendorf, Danielle M. Ware, Eric C. Schirmer, Melarkode S Ramakrishnan, Anil G. Cashikar
Publikováno v:
Molecular Cell. 9:751-760
AAA proteins remodel other proteins to affect a multitude of biological processes. Their power to remodel substrates must lie in their capacity to couple substrate binding to conformational changes via cycles of nucleotide binding and hydrolysis, but
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9559cb242a5029ae77835944b7de826c
https://doi.org/10.1016/s1097-2765(02)00499-9
https://doi.org/10.1016/s1097-2765(02)00499-9
Autor:
Thomas M. Weiss, William I. Weis, Karen N. Colbert, Pawel Burkhardt, Douglas A. Hattendorf, Dirk Fasshauer
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 31, pp. 12637-12642
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America
In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08fd071dcaca846a7e4796c9f9ed1d33
https://serval.unil.ch/resource/serval:BIB_0C4B820E84E4.P001/REF.pdf
https://serval.unil.ch/resource/serval:BIB_0C4B820E84E4.P001/REF.pdf
Publikováno v:
The EMBO Journal
Sec1/Munc18-like (SM) proteins functionally interact with SNARE proteins in vesicular fusion. Despite their high sequence conservation, structurally disparate binding modes for SM proteins with syntaxins have been observed. Several SM proteins appear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3e3477ca16aa6e770c4a9814071f324
https://pubmed.ncbi.nlm.nih.gov/18337752
https://pubmed.ncbi.nlm.nih.gov/18337752
Publikováno v:
Nature. 446(7135)
The crystal structure of Sro7 and its interaction with the SNARE Sec9p is described. The structure reveals two WD40 β-propeller domains followed by a 60-residue tail. A mutant lacking the tail binds to the SNARE domain of Sec9 and inhibits assembly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bcc9a88e34705b2f33d243465d31058
https://pubmed.ncbi.nlm.nih.gov/17392788
https://pubmed.ncbi.nlm.nih.gov/17392788
Autor:
Susan Lindquist, Douglas A. Hattendorf
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 99(5)
Hsp104 from Saccharomyces cerevisiae is a hexameric protein with two AAA ATPase domains (N- and C-terminal nucleotide-binding domains NBD1 and NBD2, respectively) per monomer. Our previous analysis of the Hsp104 ATP hydrolysis cycle revealed that NBD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d48e2bd4ae3678512cc7994765f902e3
https://pubmed.ncbi.nlm.nih.gov/11867765
https://pubmed.ncbi.nlm.nih.gov/11867765
Autor:
Douglas A. Hattendorf, Susan Lindquist
AAA proteins share a conserved active site for ATP hydrolysis and regulate many cellular processes. AAA proteins are oligomeric and often have multiple ATPase domains per monomer, which is suggestive of complex allosteric kinetics of ATP hydrolysis.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55285d1b75bbeda16118cad0f4bb6337
https://europepmc.org/articles/PMC125804/
https://europepmc.org/articles/PMC125804/