Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Brenda Rener"'
Autor:
Shao-Xiong Wang, Virginia García-Cañas, Ronald B. Frazier, Angelia Reed-Bogan, Mohammad Saeed, Kevin D. Altria, Brenda Rener, Michel Girard, F. Moffatt, Serigne Thiam, Wendy Lau, Margaret Ruesch, Mingfang Hong, Oscar Salas-Solano, K. Michael Jessop, Ketaki Patel, Brian Nunnally, Heather Carnegie, Kshama Natarajan, Ming Zeng, Claudia Jochheim, Seth Madren, Xinfeng Zhang, SungAe Park, K. C. Cheng
Publikováno v:
Chromatographia. 66:955-961
An international project team (including members from US, Canada and UK) was formed from a number of interested biopharmaceutical companies and regulatory authorities to conduct a cross-organisation collaboration exercise. The results of the first co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d2be3e8dc223f2ed08d9b70a4999e19
https://doi.org/10.1365/s10337-007-0437-x
https://doi.org/10.1365/s10337-007-0437-x
Publikováno v:
Journal of Biological Chemistry. 271:9473-9482
We have examined the energetics of the interactions of two kinesin constructs with nucleotide and microtubules to develop a structural model of kinesin-dependent motility. Dimerization of the constructs was found to reduce the maximum rate of the mic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2cc0f3f72aa9904ff3ed4df1f65ec79
https://doi.org/10.1074/jbc.271.16.9473
https://doi.org/10.1074/jbc.271.16.9473
Autor:
Brenda Rener, Steven S. Rosenfeld, Herbert C. Cheung, Jacob Lebowitz, Sambit R. Kar, Jung Xing
Publikováno v:
Journal of Biological Chemistry. 269:30187-30194
The conformational transitions that smooth muscle myosin undergoes after nucleotide binding have been examined using fluorescently labeled nucleotides and regulatory light chain. The 10 S conformation of smooth muscle myosin could be induced by addit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::694ae4211d63c7e497adf38b075567df
https://doi.org/10.1016/s0021-9258(18)43795-7
https://doi.org/10.1016/s0021-9258(18)43795-7
Publikováno v:
Carbohydrate Research. 210:247-254
The structure of the type-specific polysaccharide antigen of Streptococcus rattus was determined by methylation analysis, periodate oxidation, and by 2D-1H- and 13C-n.m.r.-spectroscopy. The polysaccharide was found to possess the trisaccharide repeat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0366c4665fefb913e53d29c68565d2e
https://doi.org/10.1016/0008-6215(91)80126-8
https://doi.org/10.1016/0008-6215(91)80126-8
Publikováno v:
The Journal of biological chemistry. 271(47)
We have investigated the structural changes that occur in the molecular motor kinesin during its ATPase cycle, utilizing two bacterially expressed constructs. The structure of both constructs has been examined as a function of the nature of the nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec77179f567600c5161c10e0014fd393
https://pubmed.ncbi.nlm.nih.gov/8939973
https://pubmed.ncbi.nlm.nih.gov/8939973
Autor:
Steven S. Rosenfeld, Brenda Rener
Publikováno v:
Biochemistry. 33(8)
Myosin I has been implicated as the motor that drives protrusion of the leading edge of motile cells. This function requires a close association with the plasma membrane and the cytoskeleton. Association with the actin cytoskeleton is mediated by an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b45edee99a7108655835e3a1da117867
https://pubmed.ncbi.nlm.nih.gov/8117689
https://pubmed.ncbi.nlm.nih.gov/8117689
Publikováno v:
Carbohydrate research. 173(2)
The structure of the group-specific polysaccharide of group G Streptococcus was determined by means of methylation analysis and selective chemical degradations. The anomeric configurations and conformations of the sugar residues were studied by 1H- a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59349f6a009c5f01488cf5f5334c61e8
https://pubmed.ncbi.nlm.nih.gov/3359455
https://pubmed.ncbi.nlm.nih.gov/3359455