Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Katrina A. Evetts"'
Autor:
Darerca Owen, Daniel Nietlispach, Katrina A. Evetts, J. Camonis, Sunil Prasannan, R.B. Fenwick, Helen R. Mott, Louise J. Campbell
Publikováno v:
Biochemistry. 48:2192-2206
The small G proteins RalA/B have a crucial function in the regulatory network that couples extracellular signals with appropriate cellular responses. RalA/B are an important component of the Ras signaling pathway and, in addition to their role in mem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::449ce3a23d90772438df4af56425839c
https://doi.org/10.1021/bi802129d
https://doi.org/10.1021/bi802129d
Autor:
Darerca Owen, Helen R. Mott, Keily Littlefield, Katrina A. Evetts, Louise J. Campbell, Daniel Nietlispach, Eeson Rajendra, Laura K. Bailey
Publikováno v:
Journal of Biological Chemistry. 284:992-999
The ADP-ribosylation factor-like (Arl) family of small G proteins are involved in the regulation of diverse cellular processes. Arl2 does not appear to be membrane localized and has been implicated as a regulator of microtubule dynamics. The downstre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84c0f251045a293671485f9afbc0a8c6
https://doi.org/10.1074/jbc.m806167200
https://doi.org/10.1074/jbc.m806167200
Autor:
David B. Sacks, Darerca Owen, Katrina A. Evetts, Peter N. Lowe, Louise J. Campbell, Keily Littlefield, Helen R. Mott, Zhigang Li
Publikováno v:
Journal of Biological Chemistry. 283:1692-1704
IQGAP1 contains a domain related to the catalytic portion of the GTPase-activating proteins (GAPs) for the Ras small G proteins, yet it has no RasGAP activity and binds to the Rho family small G proteins Cdc42 and Rac1. It is thought that IQGAP1 is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c77fd7105e9e0be7c5074d4f99c2d61
https://doi.org/10.1074/jbc.m707257200
https://doi.org/10.1074/jbc.m707257200
Autor:
Katrina A. Evetts, Peter R. Nielsen, Helen R. Mott, Louise J. Hopkins, Daniel Nietlispach, Katherine Stott, Darerca Owen, Simon J. Grimshaw
Publikováno v:
Journal of Biological Chemistry. 279:2192-2201
The sterile alpha motif (SAM) is a 65-70-amino acid domain found in over 300 proteins that are involved in either signal transduction or transcriptional activation and repression. SAM domains have been shown to mediate both homodimerization and heter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c0e3fcd424850147a6394aae2a33440
https://doi.org/10.1074/jbc.m305605200
https://doi.org/10.1074/jbc.m305605200
Autor:
Laura K, Bailey, Louise J, Campbell, Katrina A, Evetts, Keily, Littlefield, Eeson, Rajendra, Daniel, Nietlispach, Darerca, Owen, Helen R, Mott
Publikováno v:
The Journal of biological chemistry. 284(2)
The ADP-ribosylation factor-like (Arl) family of small G proteins are involved in the regulation of diverse cellular processes. Arl2 does not appear to be membrane localized and has been implicated as a regulator of microtubule dynamics. The downstre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6ff0903db86a9e3a7ecef6f43e7cddcb
https://pubmed.ncbi.nlm.nih.gov/18981177
https://pubmed.ncbi.nlm.nih.gov/18981177
Autor:
Helen R. Mott, Laura K. Bailey, Eeson Rajendra, Keily Littlefield, Katrina A. Evetts, Daniel Nietlispach, Louise J. Campbell, Darerca Owen
Publikováno v:
Biomolecular NMR assignments. 3(1)
We report (1)H, (13)C and (15)N resonance assignments for Binder of Arl Two (BART), an effector of the small G protein Arl2. The BMRB accession code is 15914.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43a0f7fc644a1b51b58f3d8237faf1fb
https://pubmed.ncbi.nlm.nih.gov/19636941
https://pubmed.ncbi.nlm.nih.gov/19636941
Autor:
Darerca Owen, Daniel Nietlispach, R. Bryn Fenwick, Helen R. Mott, Sunil Prasannan, Katrina A. Evetts, Louise J. Campbell
Publikováno v:
Biomolecular NMR assignments. 2(2)
We report here the (1)H, (15)N and (13)C resonance assignments for the small G protein RalB bound to the GTP analogue, GMPPNP and complexed with the Ral binding domain of its downstream effector RLIP76. The BMRB accession code is 15525.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::650079150f5b94214c3ed85a0dee4f76
https://pubmed.ncbi.nlm.nih.gov/19636899
https://pubmed.ncbi.nlm.nih.gov/19636899
Autor:
R. Bryn Fenwick, Darerca Owen, Louise J. Campbell, Helen R. Mott, Sunil Prasannan, Daniel Nietlispach, Katrina A. Evetts
Publikováno v:
Biomolecular NMR assignments. 2(2)
We report (1)H and (15)N resonance assignments for the free Ral binding domain of RLIP76 (393-446) and the (1)H, (15)N and (13)C resonance assignments for the RLIP76 Ral binding domain in complex with the active conformation of RalB. The BMRB accessi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00d6e642b6c087e9c79ffda75f3e6ac2
https://pubmed.ncbi.nlm.nih.gov/19636902
https://pubmed.ncbi.nlm.nih.gov/19636902
Autor:
Darerca, Owen, Louise J, Campbell, Keily, Littlefield, Katrina A, Evetts, Zhigang, Li, David B, Sacks, Peter N, Lowe, Helen R, Mott
Publikováno v:
The Journal of biological chemistry. 283(3)
IQGAP1 contains a domain related to the catalytic portion of the GTPase-activating proteins (GAPs) for the Ras small G proteins, yet it has no RasGAP activity and binds to the Rho family small G proteins Cdc42 and Rac1. It is thought that IQGAP1 is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f77cad11494e0455ed46bc1f68a9608c
https://pubmed.ncbi.nlm.nih.gov/17984089
https://pubmed.ncbi.nlm.nih.gov/17984089
Autor:
Sunil Prasannan, Helen R. Mott, R. Bryn Fenwick, Darerca Owen, Daniel Nietlispach, Louise J. Campbell, Katrina A. Evetts
Publikováno v:
Biomolecular NMR assignments. 1(1)
We report 1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation. Backbone amide dynamics parameters for a majority of residues have also been obtained. The BMRB accession code is 15230 [corrected]
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72fa196bb3618bd3391f9fa98e92156a
https://pubmed.ncbi.nlm.nih.gov/19636851
https://pubmed.ncbi.nlm.nih.gov/19636851