Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor
about
Initiation of mRNA translation in bacteria: structural and dynamic aspectsInitiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPasesThe molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomesX-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational flexibility of eIF5B is restricted on the ribosome by interaction with eIF1AA model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunitThe integrative role of cryo electron microscopy in molecular and cellular structural biology.Initiation factor 2 stabilizes the ribosome in a semirotated conformationTranslation initiation factor 3 regulates switching between different modes of ribosomal subunit joining.Structures of the orthosomycin antibiotics avilamycin and evernimicin in complex with the bacterial 70S ribosome.eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling.Essential functions linked with structural disorder in organisms of minimal genomeRepurposing drugs for treatment of tuberculosis: a role for non-steroidal anti-inflammatory drugs.Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association.Bacterial Protein Synthesis as a Target for Antibiotic Inhibition.Non-Steroidal Anti-inflammatory Drugs As Host-Directed Therapy for Tuberculosis: A Systematic Review.IBiSS, a versatile and interactive tool for integrated sequence and 3D structure analysis of large macromolecular complexes.Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation.Ribosomal protein L7/L12 is required for GTPase translation factors EF-G, RF3, and IF2 to bind in their GTP state to 70S ribosomes.Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathwaysDirectional transition from initiation to elongation in bacterial translation.A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association.E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form
P2860
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P2860
Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Involvement of protein IF2 N d ...... full-length initiation factor
@ast
Involvement of protein IF2 N d ...... full-length initiation factor
@en
Involvement of protein IF2 N d ...... full-length initiation factor
@nl
type
label
Involvement of protein IF2 N d ...... full-length initiation factor
@ast
Involvement of protein IF2 N d ...... full-length initiation factor
@en
Involvement of protein IF2 N d ...... full-length initiation factor
@nl
prefLabel
Involvement of protein IF2 N d ...... full-length initiation factor
@ast
Involvement of protein IF2 N d ...... full-length initiation factor
@en
Involvement of protein IF2 N d ...... full-length initiation factor
@nl
P2093
P2860
P50
P3181
P356
P1476
Involvement of protein IF2 N d ...... full-length initiation factor
@en
P2093
Alexander G Myasnikov
Angelita Simonetti
Bruno P Klaholz
Claudio O Gualerzi
Daniel Eiler
Isabelle Hazemann
Isabelle M L Billas
Joseph D Puglisi
Pierre Roblin
Thomas A Steitz
P2860
P304
P3181
P356
10.1073/PNAS.1309578110
P407
P577
2013-09-24T00:00:00Z