Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Kurt J. Amann"'
Autor:
Joshua A. Mayer, Kurt J. Amann
Publikováno v:
Cell Motility and the Cytoskeleton. 66:109-118
The bacterial actin MreB has been implicated in a variety of cellular roles including cell shape determination, cell wall synthesis, chromosome condensation and segregation, and the establishment and maintenance of cell polarity. Toward elucidating a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7a6e4c2c6f100ef13048aff281ccea2
https://doi.org/10.1002/cm.20332
https://doi.org/10.1002/cm.20332
Autor:
Greg J. Bean, Kurt J. Amann
Publikováno v:
Biochemistry. 47:826-835
The untested assumption that bacteria lack a cytoskeleton (1) was overturned by the discoveries of prokaryotic orthologs (2, 3) of tubulin (4), actin (5, 6), and even intermediate filament proteins (7). The tubulin ortholog FtsZ drives contraction of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::890b828c0d3d1c03d2a5eb3bab9ea644
https://doi.org/10.1021/bi701538e
https://doi.org/10.1021/bi701538e
Publikováno v:
Molecular Biology of the Cell. 17:239-250
Calpain 2 regulates membrane protrusion during cell migration. However, relevant substrates that mediate the effects of calpain on protrusion have not been identified. One potential candidate substrate is the actin binding protein cortactin. Cortacti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dcd0f968e0f141c48223029eff4a0e3
https://doi.org/10.1091/mbc.e05-06-0488
https://doi.org/10.1091/mbc.e05-06-0488
Autor:
Yuhong Song, Sachi C. Gerbin, David D. Chang, Raymond S. Maul, Kurt J. Amann, Thomas D. Pollard
Publikováno v:
The Journal of Cell Biology
Epithelial protein lost in neoplasm (EPLIN) is a cytoskeleton-associated protein encoded by a gene that is down-regulated in transformed cells. EPLIN increases the number and size of actin stress fibers and inhibits membrane ruffling induced by Rac.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0308280a08f1f2222b5bd7e0d59780e
https://doi.org/10.1083/jcb.200212057
https://doi.org/10.1083/jcb.200212057
Autor:
John E. Heuser, Coumaran Egile, Svetla Stoilova-McPhie, Kurt J. Amann, Larnele Hazelwood, Niels Volkmann, Rong Li, Thomas D. Pollard, Dorit Hanein, Dirk C. Winter
Publikováno v:
Science. 293:2456-2459
The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a06384a04aee9b49624b2091edb879c3
https://doi.org/10.1126/science.1063025
https://doi.org/10.1126/science.1063025
Autor:
Kurt J. Amann, Thomas D. Pollard
Publikováno v:
Nature Cell Biology. 3:306-310
Regulated assembly of actin-filament networks provides the mechanical force that pushes forward the leading edge of motile eukaryotic cells and intracellular pathogenic bacteria and viruses. When activated by binding to actin filaments and to the WA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7efd922705cf796885c213a9d0d82e59
https://doi.org/10.1038/35060104
https://doi.org/10.1038/35060104
Publikováno v:
Journal of Biological Chemistry. 274:35375-35380
We previously identified a cluster of basic spectrin-like repeats in the dystrophin rod domain that binds F-actin through electrostatic interactions (Amann, K. J., Renley, B. A., and Ervasti, J. M. (1998) J. Biol. Chem. 273, 28419-28423). Because of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a743cb8b89a2f765322844fa5b2822f
https://doi.org/10.1074/jbc.274.50.35375
https://doi.org/10.1074/jbc.274.50.35375
Publikováno v:
Cell Motility and the Cytoskeleton. 41:264-270
We purified actin from bovine brain by DNase I affinity chromatography in order to compare the binding of dystrophin to muscle actin with its binding to nonmuscle actin. While both beta- and gamma-nonmuscle actins are expressed in brain, Western blot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3026e1e98d55a35fdde28886bee45ef1
https://doi.org/10.1002/(sici)1097-0169(1998)41:3<264::aid-cm7>3.0.co
https://doi.org/10.1002/(sici)1097-0169(1998)41:3<264::aid-cm7>3.0.co
Publikováno v:
The Journal of Cell Biology
The F-actin binding and cross-linking properties of skeletal muscle dystrophin-glycoprotein complex were examined using high and low speed cosedimentation assays, microcapillary falling ball viscometry, and electron microscopy. Dystrophin-glycoprotei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5013d11ff610f00293ab3ff88cc4d209
https://doi.org/10.1083/jcb.135.3.661
https://doi.org/10.1083/jcb.135.3.661
Autor:
Xiao-Ping Xu, Isabelle Rouiller, Coumaran Egile, Thomas D. Pollard, Kurt J. Amann, Rong Li, Stephan Nickell, Dorit Hanein, Niels Volkmann, Daniela Nicastro
Publikováno v:
The Journal of Cell Biology
The actin-related protein 2/3 (Arp2/3) complex mediates the formation of branched actin filaments at the leading edge of motile cells and in the comet tails moving certain intracellular pathogens. Crystal structures of the Arp2/3 complex are availabl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e1abe4faaed6d5656aafdd3e78f0c65
https://pubmed.ncbi.nlm.nih.gov/18316411
https://pubmed.ncbi.nlm.nih.gov/18316411