Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Dawn Z. Herrick"'
Publikováno v:
Journal of Analytical & Pharmaceutical Research. 7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a664fd865b16227bcc60e64ed3637665
https://doi.org/10.15406/japlr.2018.07.00299
https://doi.org/10.15406/japlr.2018.07.00299
Publikováno v:
ACS Symposium Series ISBN: 9780841233096
ACS Symposium Series
ACS Symposium Series
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec58cc6f84a11a3836eb2bf62516e4c5
https://doi.org/10.1021/bk-2018-1281.ch004
https://doi.org/10.1021/bk-2018-1281.ch004
Autor:
Yongmei Wang, Wei Gao, Sara Orski, X. Michael Liu, Taihyun Chang, Junwon Han, Chang Y. Ryu, Benjamin Crawshaw, Dawn Z. Herrick, E. Peter Maziarz, Tianlan Zhang, Bryan McCulloch, Ralph Even, David M. Meunier, Yongfu Li, Jamie Cohen, Francis Acholla, Wenyu Su, Krishna Kuppannan, Albena Lederer, Susanne Boye, Dietmar Appelhans
'This book is about Recent Progress in Separation of Macromolecules and Particulates'--
Publikováno v:
Biochemistry
OxlT, the oxalate/formate exchanger of Oxalobacter formigenes, is a member of the major facilitator superfamily of transporters. In the present work, substrate (oxalate) was found to enhance the reactivity of the cysteine mutant S336C on the cytoplas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b1dd3553f7550eb92e2796b4a4ec4de
https://doi.org/10.1021/bi5012173
https://doi.org/10.1021/bi5012173
Publikováno v:
Journal of Molecular Biology. 423:818-830
Outer-membrane TonB-dependent transporters, such as the Escherichia coli ferric citrate transporter FecA, interact with the inner-membrane protein TonB through an energy-coupling segment termed the Ton box. In FecA, which regulates its own transcript
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09a1a0bf55c4d1aab8e59227c6a86baa
https://doi.org/10.1016/j.jmb.2012.09.003
https://doi.org/10.1016/j.jmb.2012.09.003
Publikováno v:
Biochemistry. 50:2633-2641
Synaptotagmin 1 (syt1) is a synaptic vesicle-anchored membrane protein that acts as the calcium sensor for the synchronous component of neuronal exocytosis. Using site-directed spin labeling, the position and membrane interactions of a fragment of sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a25ffc22a81640c78993665d0b03c1f
https://doi.org/10.1021/bi200049c
https://doi.org/10.1021/bi200049c
Publikováno v:
Journal of Molecular Biology. 405:696-706
Synaptotagmin 1 (syt1) functions as a Ca(2+)-sensor for neuronal exocytosis. Here, site-directed spin labeling was used to examine the complex formed between a soluble fragment of syt1, which contains its two C2 domains, and the neuronal core soluble
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9f0570dd2f21b0c6ef0cd8068eb9cfd
https://doi.org/10.1016/j.jmb.2010.11.015
https://doi.org/10.1016/j.jmb.2010.11.015
Autor:
Hao Huang, Dawn Z. Herrick, David S. Cafiso, Jeffrey F. Ellena, Charles D. Schwieters, Weiwei Kuo
Publikováno v:
Journal of Molecular Biology. 390:913-923
Synaptotagmin 1 (syt1) is a synaptic vesicle membrane protein that functions as the Ca(2)(+) sensor in neuronal exocytosis. Here, site-directed spin labeling was used to generate models for the solution and membrane-bound structures of a soluble frag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1778285a6797130e13019e940dd93a89
https://doi.org/10.1016/j.jmb.2009.06.007
https://doi.org/10.1016/j.jmb.2009.06.007
Position of Synaptotagmin I at the Membrane Interface: Cooperative Interactions of Tandem C2 Domains
Publikováno v:
Biochemistry. 45:9668-9674
Synaptotagmin I is a synaptic vesicle associated membrane protein that appears to regulate Ca(2+)-mediated exocytosis. Here, the Ca(2+)-dependent membrane interactions of a water soluble fragment of synaptotagmin I (C2AB) that contains its two C2 dom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cf5dab6903ef2001b743dbf1107cded
https://doi.org/10.1021/bi060874j
https://doi.org/10.1021/bi060874j
Autor:
James H. Hurley, Evzen Boura, Dawn Z. Herrick, Hoi Sung Chung, William A. Eaton, Bartosz Różycki, David S. Cafiso, Jaroslav Vecer, Gerhard Hummer
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 108(23)
ESCRT-I is required for the sorting of integral membrane proteins to the lysosome, or vacuole in yeast, for cytokinesis in animal cells, and for the budding of HIV-1 from human macrophages and T lymphocytes. ESCRT-I is a heterotetramer of Vps23, Vps2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea6309d407a5454e883e8c629a9c965b
https://pubmed.ncbi.nlm.nih.gov/21596998
https://pubmed.ncbi.nlm.nih.gov/21596998