Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Alan G. Weeds"'
Autor:
Abdulatif Al Haj, Ewald Hannappel, Unai Silvan, Sabine Buchmeier, Hans Georg Mannherz, Brigitte M. Jockusch, Alan G. Weeds, Christine App, Antonina Joanna Mazur, Carsten Theiss, Cora-Ann Schoenenberger
Publikováno v:
Cytoskeleton. 71:95-107
F-actin treadmilling plays a key part in cell locomotion. Because immunofluorescence showed colocalisation of thymosin beta4 (Tβ4) with cofilin-1 and Arp2/3 complex in lamellipodia, we analyzed combinations of these proteins on F-actin-adenosine tri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db0fe512207904676bd03b0e3df8077f
https://doi.org/10.1002/cm.21128
https://doi.org/10.1002/cm.21128
Autor:
Sutherland K. Maciver, Ellen G. Allwood, Andrei Smertenko, Alan G. Weeds, Patrick J. Hussey, Chang-Jie Jiang, Safina Khan
Publikováno v:
The Plant Journal. 25:203-212
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6896d6efe0684a587e037db25041f1b2
https://doi.org/10.1111/j.1365-313x.2001.00954.x
https://doi.org/10.1111/j.1365-313x.2001.00954.x
Publikováno v:
European Journal of Cell Biology. 84:503-515
Etoposide inhibits topoisomerase II and induces apoptosis in human epidermoid cancer cells (A431) and normal rat fibroblasts (NRK) as verified by apoptotic morphology and chromatin degradation. Here we examine changes in the localisation of actin, co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a1ad059d04cb8a917ddd863a1539e26
https://doi.org/10.1016/j.ejcb.2004.11.008
https://doi.org/10.1016/j.ejcb.2004.11.008
Publikováno v:
Journal of Biological Chemistry. 279:4840-4848
Human actin-depolymerizing factor (ADF) and cofilin are pH-sensitive, actin-depolymerizing proteins. Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8. To understand this, we solved the structure o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0dd72c7f86446d3c409af22da51ad927
https://doi.org/10.1074/jbc.m310148200
https://doi.org/10.1074/jbc.m310148200
Publikováno v:
Journal of Biological Chemistry. 278:14394-14400
Increasing cellular G-actin, using latrunculin B, in either intact or permeabilized rat peritoneal mast cells, caused translocation of both actin and an actin regulatory protein, cofilin, into the nuclei. The effect was not associated with an increas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdaabbab51fc0616be1689a9b3432336
https://doi.org/10.1074/jbc.m206393200
https://doi.org/10.1074/jbc.m206393200
Autor:
Richard G. Anthony, John H. Doonan, Alan G. Weeds, Patrick J. Hussey, Andrei Smertenko, Ellen G. Allwood, Bjørn K. Drøbak, Stefanie Reichelt
Publikováno v:
The Plant Cell. 14:2915-2927
Pollen tube growth is dependent on a dynamic actin cytoskeleton, suggesting that actin-regulating proteins are involved. We have examined the regulation of the lily pollen-specific actin-depolymerizing factor (ADF) LlADF1. Its actin binding and depol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ee96baffcdc121026f649b667959184
https://doi.org/10.1105/tpc.005363
https://doi.org/10.1105/tpc.005363
Publikováno v:
Journal of Molecular Biology. 315:911-925
The actin-depolymerizing factor (ADF)/cofilin family of proteins play an essential role in actin dynamics and cytoskeletal re-organization. Human tissues express two isoforms in the same cells, ADF and cofilin, and these two proteins are more than 70
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bcc7f392f0741ad9c08c26240df19a15
https://doi.org/10.1006/jmbi.2001.5280
https://doi.org/10.1006/jmbi.2001.5280
Publikováno v:
FEBS Letters. 508:131-135
Actin ADP-ribosylated at Arg177 was previously shown not to polymerise after increasing the ionic strength, but to cap the barbed ends of filaments. Here we confirm that the polymerisation of ADP-ribosylated actin is inhibited, however, under specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b77bfe8f0b7dbf2eb792380b03ebc4b
https://doi.org/10.1016/s0014-5793(01)03040-x
https://doi.org/10.1016/s0014-5793(01)03040-x
Autor:
Frédéric Godde, Jean-Jacques Toulmé, Alan G. Weeds, Serge Moreau, Michael J. Gait, Andrey A. Arzumanov
Publikováno v:
Helvetica Chimica Acta. 83:1424-1436
The Tat protein is an essential trans-activator of HIV gene expression. It interacts with its RNA recognition sequence, the trans-activation responsive region TAR, as well as cellular factors. These interactions are potential targets for drug discove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0daaea43fdc3a60d51dc00f1fcc4a5fd
https://doi.org/10.1002/1522-2675(20000705)83:7<1424::aid-hlca1424>3.0.co
https://doi.org/10.1002/1522-2675(20000705)83:7<1424::aid-hlca1424>3.0.co
Publikováno v:
Journal of Molecular Biology. 298:649-661
The actin depolymerizing factor (ADF)/cofilin family of proteins interact with actin monomers and filaments in a pH-sensitive manner. When ADF/cofilin binds F-actin it induces a change in the helical twist and fragmentation; it also accelerates the d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0306e9e15629ed05558a43d1fd515313
https://doi.org/10.1006/jmbi.2000.3688
https://doi.org/10.1006/jmbi.2000.3688