Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Jemima C. Thomas"'
Autor:
Catarina, Felisberto-Rodrigues, Jemima C, Thomas, Craig, McAndrew, Yann-Vaï, Le Bihan, Rosemary, Burke, Paul, Workman, Rob L M, van Montfort
Publikováno v:
The Biochemical journal. 476(18)
DHX8 is a crucial DEAH-box RNA helicase involved in splicing and required for the release of mature mRNA from the spliceosome. Here, we report the biochemical characterisation of full-length human DHX8 and the catalytically active helicase core DHX8
Publikováno v:
Biochemistry
Proteins of the ankyrin-repeat and SOCS-box (ASB) family act as the substrate-recognition subunits of ECS-type (ElonginBC-Cullin-SOCS-box) Cullin RING E3 ubiquitin ligase (CRL) complexes that catalyze the specific polyubiquitination of cellular prote
Autor:
Natasha S Clayton, Darerca Owen, Helen R. Mott, Chensu Wang, Michael A. White, Chris Abell, Jonathan M. Cooper, Jemima C. Thomas
Publikováno v:
Thomas, J C, Cooper, J M, Clayton, N S, Wang, C, White, M A, Abell, C, Owen, D & Mott, H R 2016, ' Inhibition of Ral GTPases Using a Stapled Peptide Approach ', Journal of Biological Chemistry, vol. 291, no. 35, pp. 18310-18325 . https://doi.org/10.1074/jbc.M116.720243
Aberrant Ras signaling drives numerous cancers, and drugs to inhibit this are urgently required. This compelling clinical need combined with recent innovations in drug discovery including the advent of biologic therapeutic agents, has propelled Ras b
Autor:
Jemima C. Thomas, Anthony A. Holder, Christopher H. Douse, Ernesto Cota, Edward W. Tate, Gordon Langsley, Paula S. Salgado, Peter Simpson, Judith L. Green
Publikováno v:
Journal of Biological Chemistry. 287:36968-36977
The interaction between the C-terminal tail of myosin A (MyoA) and its light chain, myosin A tail domain interacting protein (MTIP), is an essential feature of the conserved molecular machinery required for gliding motility and cell invasion by apico
Autor:
Christopher H, Douse, Sabrina J, Maas, Jemima C, Thomas, James A, Garnett, Yunyun, Sun, Ernesto, Cota, Edward W, Tate
Publikováno v:
ACS chemical biology. 9(10)
Constrained α-helical peptides are an exciting class of molecule designed to disrupt protein-protein interactions (PPIs) at a surface-exposed helix binding site. Complexes that engage more than one helical face account for over a third of structural
Autor:
Peter Simpson, Anthony A. Holder, Stephen R. Martin, Judith L. Green, Ronald I. Howson, Jemima C. Thomas, Edward W. Tate, D.K. Moss, Ernesto Cota
Publikováno v:
Molecular bioSystems. 6(3)
The myosin tail domain interacting protein-myosin A (MTIP-MyoA) protein complex is an essential element of the motor driving invasion of red blood cells by the Plasmodium species that cause malaria. Here we report the key determinants of binding at t