Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Jared C. Cochran"'
Publikováno v:
Cytoskeleton (Hoboken, N.j.)
Myosin active site elements (i.e., switch‐1) bind both ATP and a divalent metal to coordinate ATP hydrolysis. ATP hydrolysis at the active site is linked via allosteric communication to the actin polymer binding site and lever arm movement, thus co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::700b7d24bfe3ad34028e246e06c44157
https://doi.org/10.1002/cm.21650
https://doi.org/10.1002/cm.21650
Publikováno v:
Biochemistry. 58:2326-2338
Chromokinesins NOD and KID have similar DNA binding domains and functions during cell division, while their motor domain sequences show significant variations. It has been unclear whether these motors have similar structure, chemistry, and microtubul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36f6c8b289e4ef4c1dbf78ec142966e3
https://doi.org/10.1021/acs.biochem.9b00011
https://doi.org/10.1021/acs.biochem.9b00011
Publikováno v:
eLife, Vol 3 (2014)
Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes. We obtained insight into this process by developing atomic models for no-nucleotide and ATP states of the mo
Externí odkaz:
https://doaj.org/article/bd812fc04f1d45f8a71622fceb5d5b18
Myosin active site elements (i.e. switch-1) bind both ATP and a divalent metal to coordinate ATP hydrolysis. ATP hydrolysis at the active site is linked via allosteric communication to the actin polymer binding site and lever arm movement, thus coupl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a70dedac651a4a9ddabf1da883a1392
https://doi.org/10.1101/2020.09.10.292169
https://doi.org/10.1101/2020.09.10.292169
Autor:
Barry J. Grant, T. Lynne Blasius, Yang Yue, Kristen J. Verhey, Shashank Jariwala, Stephanie Zhang, Jared C. Cochran, Benjamin C. Walker
Publikováno v:
The Journal of Cell Biology
The Journal of cell biology, vol 217, iss 4
The Journal of cell biology, vol 217, iss 4
Despite their shared ability to regulate microtubule polymerization dynamics, kinesin-4 motors display dramatically different motility properties ranging from fast processive motility to no movement. Yue et al. demonstrate that for KIF7 and KIF27, al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6db487852a2d33a90c0c2ccc031b4304
http://europepmc.org/articles/PMC5881503
http://europepmc.org/articles/PMC5881503
Autor:
Kayla M. Bell, Jared C. Cochran
Saccharomyces cerevisiae kinesin-5 Cin8 displays unconventional biochemical behavior including bidirectional motility and ability to bind multiple motor domains per αβ tubulin dimer in the microtubule lattice. Previous research suggested that a lar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d13c9f7fea575356ca7d6db7a3872f6f
https://doi.org/10.1101/525329
https://doi.org/10.1101/525329
Enzyme behavior has been described using the Michaelis-Menten mechanism. The analysis of extended time domains provides a means to extract the Michaelis-Menten constants through direct fitting of raw data. We have developed a scheme for determining M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0785ffdd049b1713f71f2a1a582544a6
Autor:
Hugo B. Brandão, Xindan Wang, David Z. Rudner, Jared C. Cochran, Anna C. Hughes, Martha G. Oakley, Benjamin C. Walker, Carrie Lierz, Andrew C. Kruse
Publikováno v:
Molecular cell. 71(5)
Summary Structural maintenance of chromosomes (SMC) complexes shape the genomes of virtually all organisms, but how they function remains incompletely understood. Recent studies in bacteria and eukaryotes have led to a unifying model in which these r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33dbaf73b274c86230f2c88485329e79
https://pubmed.ncbi.nlm.nih.gov/30100265
https://pubmed.ncbi.nlm.nih.gov/30100265
Publikováno v:
The Journal of Biological Chemistry
Kinesin motors play central roles in establishing and maintaining the mitotic spindle during cell division. Unlike most other kinesins, Cin8, a kinesin-5 motor in Saccharomyces cerevisiae, can move bidirectionally along microtubules, switching direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85e75c153f414365dd38dcd095344457
https://pubmed.ncbi.nlm.nih.gov/28701465
https://pubmed.ncbi.nlm.nih.gov/28701465
Publikováno v:
Biochemistry
NEMO is a scaffolding protein that, together with the catalytic subunits IKKα and IKKβ, plays an essential role in the formation of the IKK complex and in the activation of the canonical NF-κB pathway. Rational drug design targeting the IKK-bindin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d1186196ed7552be09b4ea18fc32548
https://doi.org/10.1021/bi500861x
https://doi.org/10.1021/bi500861x