Zobrazeno 1 - 10
of 120
pro vyhledávání: '"Jolinda A Traugh"'
Autor:
Yuan-Hao Hsu, Jolinda A Traugh
Publikováno v:
PLoS ONE, Vol 5, Iss 3, p e9455 (2010)
Regulation of Pak2 activity involves at least two mechanisms: (i) phosphorylation of the conserved Thr(402) in the activation loop and (ii) interaction of the autoinhibitory domain (AID) with the catalytic domain. We collected 482 human protein kinas
Externí odkaz:
https://doaj.org/article/83bc3bb5ef79465cbee0bc7af33bd359
Publikováno v:
Biochimica et biophysica acta. Molecular cell research. 1867(4)
p21-activated protein kinase (PAK2) is a unique member of the PAK family kinases that plays important roles in stress signaling. It can be activated by binding to the small GTPase, Cdc42 and Rac1, or by caspase 3 cleavage. Cdc42-activated PAK2 mediat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcf7c0307f232b52a9b3994301428f20
https://pubmed.ncbi.nlm.nih.gov/31926209
https://pubmed.ncbi.nlm.nih.gov/31926209
Publikováno v:
Journal of Biological Chemistry. 283:36397-36405
During apoptotic stress, protein kinase Pak2 is cleaved by caspase 3 to form a heterotetramer that is constitutively activated following autophosphorylation. The active protein kinase migrates slightly slower than the inactive holoenzyme when analyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10e3d514fdbdd7a984e72c1a4aca2cfe
https://doi.org/10.1074/jbc.m805581200
https://doi.org/10.1074/jbc.m805581200
Autor:
Jolinda A. Traugh, Rolf Jakobi
Publikováno v:
European Journal of Biochemistry. 230:1111-1117
Casein kinase II exists in vivo as an active holoenzyme consisting of catalytic alpha and/or alpha' and regulatory beta subunits, which form a tetrameric structure of alpha 2 beta 2. Unlike most other protein kinases, casein kinase II uses both ATP a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85b129a65fa590a2fe58982f96b38aaf
https://doi.org/10.1111/j.1432-1033.1995.1111g.x
https://doi.org/10.1111/j.1432-1033.1995.1111g.x
Publikováno v:
Biochemistry & Analytical Biochemistry. 5
p21-activated kinase-2 (PAK2) is ubiquitously expressed in all mammalian cells and tissues tested so far. It is a unique member of PAK family kinases that can be activated by various stress conditions to induce apoptosis or cytostasis. Although many
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ace7b8bd9efaf4e7e8ec997cd5f21d5
https://doi.org/10.4172/2161-1009.1000277
https://doi.org/10.4172/2161-1009.1000277
Publikováno v:
The EMBO Journal. 24:4094-4105
Translation is downregulated in response to a variety of moderate stresses, including serum deprivation, hyperosmolarity and ionizing radiation. The cytostatic p21-activated protein kinase 2 (Pak2)/γ-PAK is activated under the same stress conditions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c21539df6f8fcf974191a60736ee217
https://doi.org/10.1038/sj.emboj.7600868
https://doi.org/10.1038/sj.emboj.7600868
Publikováno v:
Molecular and Cellular Biology. 24:1582-1594
Pak2 is a serine/threonine kinase that participates in the cellular response to stress. Among the potential substrates for Pak2 is the protein Myc, encoded by the proto-oncogene MYC. Here we demonstrate that Pak2 phosphorylates Myc at three sites (T3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcbcfb05c4f7632dba2fc9bbb8867e19
https://doi.org/10.1128/mcb.24.4.1582-1594.2004
https://doi.org/10.1128/mcb.24.4.1582-1594.2004
Autor:
Polygena T. Tuazon, Shinkou Kyo, Yumi Tohyama, Xiujuan Qu, S. M. Shahjahan Miah, Koichiro Maeno, Jun Ling, Hirohei Yamamura, Kiyonao Sada, Jolinda A. Traugh
Publikováno v:
Molecular and Cellular Biology. 24:71-83
The p21-activated serine/threonine protein kinase Pak2/gamma-PAK and the nonreceptor type of protein tyrosine kinase Syk are known to be activated when the cells are exposed to osmotic stress. The purpose of the present study was to examine whether P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8df1cc1df51209c3482fdd26a9b0f494
https://doi.org/10.1128/mcb.24.1.71-83.2004
https://doi.org/10.1128/mcb.24.1.71-83.2004
Publikováno v:
Journal of Biological Chemistry. 278:13101-13109
The intracellular localization and physiological functions of the p21-activated protein kinase gamma-PAK have been examined in human embryonic kidney 293T and COS-7 cells. At 1-4 days post-transfection, cell division is inhibited by the expression of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e04831f44beaa4639ee23122f5c41731
https://doi.org/10.1074/jbc.m212557200
https://doi.org/10.1074/jbc.m212557200
Publikováno v:
FEBS Letters. 507:195-199
Autophosphorylation of p21-activated protein kinase gamma-PAK is stimulated at 10 microM sphingosine in vitro and is maximal at 100 microM. Sites autophosphorylated on gamma-PAK in response to sphingosine are identical to those obtained with Cdc42(GT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5ce3272e5f51c4c05d32f1ba1396bac
https://doi.org/10.1016/s0014-5793(01)02965-9
https://doi.org/10.1016/s0014-5793(01)02965-9