Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Sarah S Mohammad-Qureshi"'
Autor:
Lydia M Castelli, David Talavera, Christopher J Kershaw, Sarah S Mohammad-Qureshi, Joseph L Costello, William Rowe, Paul F G Sims, Christopher M Grant, Simon J Hubbard, Mark P Ashe, Graham D Pavitt
Publikováno v:
PLoS Genetics, Vol 11, Iss 5, p e1005233 (2015)
Translation initiation factor eIF4E mediates mRNA selection for protein synthesis via the mRNA 5'cap. A family of binding proteins, termed the 4E-BPs, interact with eIF4E to hinder ribosome recruitment. Mechanisms underlying mRNA specificity for 4E-B
Externí odkaz:
https://doaj.org/article/4442571fc9da4cb6b3f3487cf8c78944
Publikováno v:
The Journal of Biological Chemistry
Background: eIF2B is a critical translation factor and regulator of protein synthesis that is implicated in human disease. Results: Protein-protein interactions within the five-subunit eIF2B complex are identified. Conclusion: eIF2B complex formation
Publikováno v:
Biochemical Society Transactions. 36:658-664
A variety of cellular processes rely on G-proteins, which cycle through active GTP-bound and inactive GDP-bound forms. The switch between these states is commonly regulated by GEFs (guanine-nucleotide-exchange factors) and GAPs (GTPase-activating pro
Autor:
Sarah S. Mohammad-Qureshi, Raphaël Haddad, Jonathan P. Richardson, Graham D. Pavitt, Elizabeth J. Hemingway
Publikováno v:
Molecular and Cellular Biology. 27:5225-5234
The cap-dependent pathway for the initiation of translation requires the assembly of eukaryotic initiation factor (eIF) ribosomal subunits and a selected mRNA. Central to the initiation process is the GTP binding protein eIF2, which delivers aminoacy
Autor:
Bumjun Lee, Yasufumi Yamamoto, Tsuyoshi Udagawa, Graham D. Pavitt, Katsura Asano, Sarah S. Mohammad-Qureshi, Chingakham Ranjit Singh
Publikováno v:
The EMBO Journal. 25:4537-4546
In eukaryotic translation initiation, the eIF2.GTP/Met-tRNA(i)(Met) ternary complex (TC) binds the eIF3/eIF1/eIF5 complex to form the multifactor complex (MFC), whereas eIF2.GDP binds the pentameric factor eIF2B for guanine nucleotide exchange. eIF5
Autor:
Lydia M, Castelli, David, Talavera, Christopher J, Kershaw, Sarah S, Mohammad-Qureshi, Joseph L, Costello, William, Rowe, Paul F G, Sims, Christopher M, Grant, Simon J, Hubbard, Mark P, Ashe, Graham D, Pavitt
Publikováno v:
PLoS Genetics
Translation initiation factor eIF4E mediates mRNA selection for protein synthesis via the mRNA 5’cap. A family of binding proteins, termed the 4E-BPs, interact with eIF4E to hinder ribosome recruitment. Mechanisms underlying mRNA specificity for 4E
Autor:
Joseph, Costello, Lydia M, Castelli, William, Rowe, Christopher J, Kershaw, David, Talavera, Sarah S, Mohammad-Qureshi, Paul F G, Sims, Christopher M, Grant, Graham D, Pavitt, Simon J, Hubbard, Mark P, Ashe
Publikováno v:
Genome Biology
Background The selection and regulation of individual mRNAs for translation initiation from a competing pool of mRNA are poorly understood processes. The closed loop complex, comprising eIF4E, eIF4G and PABP, and its regulation by 4E-BPs are perceive
Publikováno v:
Genesdevelopment. 27(24)
Protein synthesis factor eIF2 delivers initiator tRNA to the ribosome. Two proteins regulate its G-protein cycle: eIF5 has both GTPase-accelerating protein (GAP) and GDP dissociation inhibitor (GDI) functions, and eIF2B is the guanine nucleotide exch
Autor:
Sarah S, Mohammad-Qureshi, Raphaël, Haddad, Karren S, Palmer, Jonathan P, Richardson, Edith, Gomez, Graham D, Pavitt
Publikováno v:
Methods in enzymology. 431
The eukaryotic initiation factor 2B (eIF2B) is a five-subunit guanine nucleotide exchange factor, that functions during translation initiation to catalyze the otherwise slow exchange of GDP for GTP on its substrate eIF2. Assays to measure substrate i
Autor:
Sarah S. Mohammad-Qureshi, Jonathan P. Richardson, Karren S. Palmer, Graham D. Pavitt, Edith Gomez, Raphaël Haddad
The eukaryotic initiation factor 2B (eIF2B) is a five-subunit guanine nucleotide exchange factor, that functions during translation initiation to catalyze the otherwise slow exchange of GDP for GTP on its substrate eIF2. Assays to measure substrate i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4aa48e4aa2b18398255936d735ea56c6
https://doi.org/10.1016/s0076-6879(07)31001-x
https://doi.org/10.1016/s0076-6879(07)31001-x