Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B - Wikidata - wikimedia - TriplyDB

Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B

Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B

http://www.wikidata.org/entity/Q35218972

about

Human Cytomegalovirus Strategies to Maintain and Promote mRNA Translation Structural Analysis of the DAP5 MIF4G Domain and Its Interaction with eIF4A Investigation of the conserved glutamate immediately following the DEAD box in eukaryotic translation initiation factor 4AI.Yeast eukaryotic initiation factor 4B (eIF4B) enhances complex assembly between eIF4A and eIF4G in vivo Cofactor-dependent specificity of a DEAD-box protein.Yeast eIF4B binds to the head of the 40S ribosomal subunit and promotes mRNA recruitment through its N-terminal and internal repeat domains Human eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosome Quantitative studies of mRNA recruitment to the eukaryotic ribosome eIF4F: a retrospective A mechanistic overview of translation initiation in eukaryotes Neuronal BC RNAs cooperate with eIF4B to mediate activity-dependent translational control Real-time fluorescence assays to monitor duplex unwinding and ATPase activities of helicases.DEAD box unwinding caught in the act Phosphorylation stoichiometries of human eukaryotic initiation factors The mechanism of eukaryotic translation initiation: new insights and challenges Transcriptome-wide characterization of the eIF4A signature highlights plasticity in translation regulation.The eIF4F and eIFiso4F Complexes of Plants: An Evolutionary Perspective Evidence That Base-pairing Interaction between Intron and mRNA Leader Sequences Inhibits Initiation of HAC1 mRNA Translation in Yeast.The eukaryotic initiation factor eIF4H facilitates loop-binding, repetitive RNA unwinding by the eIF4A DEAD-box helicase.RNA BIOCHEMISTRY. Factor-dependent processivity in human eIF4A DEAD-box helicase.The role of the poly(A) binding protein in the assembly of the Cap-binding complex during translation initiation in plants.Role of p70S6K1-mediated phosphorylation of eIF4B and PDCD4 proteins in the regulation of protein synthesis.The current status of vertebrate cellular mRNA IRESs The DEAD-box helicase eIF4A: paradigm or the odd one out?Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members.Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity eIF4B stimulates translation of long mRNAs with structured 5' UTRs and low closed-loop potential but weak dependence on eIF4G.Identification and characterization of functionally critical, conserved motifs in the internal repeats and N-terminal domain of yeast translation initiation factor 4B (yeIF4B)Toward a molecular understanding of RNA remodeling by DEAD-box proteins.The diverse roles of the eIF4A family: you are the company you keep.Cellular cap-binding protein, eIF4E, promotes picornavirus genome restructuring and translation.The molecular choreography of protein synthesis: translational control, regulation, and pathways.Eukaryotic translation initiation factors and cancer.eIF4B, eIF4G and RNA regulate eIF4A activity in translation initiation by modulating the eIF4A conformational cycle.eIF4B stimulates eIF4A ATPase and unwinding activities by direct interaction through its 7-repeats region.Functional 5' UTR mRNA structures in eukaryotic translation regulation and how to find them.USP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1.Structure of a human cap-dependent 48S translation pre-initiation complex.

P2860

Q26752742-32C644AE-534E-43F3-864D-434904D9AC33 Q27676748-400B64F2-5E22-4B41-BB55-3A102CAEA1DC Q27932083-8D184998-E631-41C9-B904-3B06A476A4A7 Q27935513-33EC2D7D-67CB-420E-9958-26B7699A8232 Q27936164-6DF32479-07A2-4872-853F-41142220C5FB Q27936401-6243E8F7-AAB6-40ED-820E-A58C6D2A0DC2 Q28117731-BCB80BE3-9C3C-4124-8481-A48E14BE5D23 Q28258346-6D690410-5399-4A36-9BCE-FA22FA5301D4 Q28266825-8DC02E1A-122E-417C-9231-F01806A89B08 Q28268066-8041D59C-7EC7-47C2-9297-AF9F0A364E66 Q28570179-2F9EC608-5787-4959-A71F-925ACE6F0DB0 Q33925519-D2BF66F5-6B1B-43EE-8DA1-41E5A824E7C7 Q34003693-D9577FFF-58BD-42D6-82A3-A2ADCAAA83CC Q34072222-445D88F5-7490-4E17-BA8D-F78FD9110B74 Q34289214-4E4F4CAD-D635-4A48-90C0-9E2B8823038C Q34375074-B7A08F93-1F28-47B2-A259-98EAAEA06CE9 Q35960491-4883757B-AA3D-4B13-B5D4-83B7F868C52B Q36065191-7DFB3EC8-50C8-4341-BB63-085FC7C9D877 Q36106977-267B7C83-0393-4693-9BD4-723F669FF920 Q36161368-7610E527-3A12-4B1C-BFF8-2143A7E343F3 Q36417593-36F164E4-E5FE-4DF0-94BC-E22972E19560 Q36466762-F5919941-14C6-44F6-A9BD-A2D369AC17ED Q36555207-6485B756-E79B-4DB7-AAC9-B04FD6AD38BE Q36662305-399D060B-125E-42E0-AE4B-417C8D6FE665 Q37032965-1066F095-540F-46F6-943B-FDF584671760 Q37104055-26382F8A-3AF5-4BFB-B66C-CE17391C36D3 Q37281478-F94352E2-656E-445B-BF06-0DD7E3072D00 Q37488544-DAC68DA2-A739-42B3-AB05-D545CAB2A56B Q38045141-66B0B343-9F19-4C09-A8E9-23F230741851 Q38180774-EF2FA038-33AE-40BB-B76C-3474910A1C3C Q38615488-E1D62D21-EAE9-479B-9100-2616D3B5D5F0 Q38961838-577AEA4C-B106-47F4-9148-66FAD35C5703 Q39400409-482DCB41-6FF5-43E0-B864-DB86B301472F Q42719837-38B55E11-EF28-43F3-AF1D-F6654039F689 Q45765174-201CFF2B-456B-4087-B5D7-582B4D165D8E Q46856027-2B89B1E6-A175-4D1D-AB6B-ABB00C1666A9 Q47307244-1210F3B2-5B94-4716-8182-B277F2007206 Q52385046-C0E3BA53-A68B-41D3-82E8-237D1DC7055C

P2860

Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B

http://www.wikidata.org/entity/Q35218972

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@ast

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@en

type

label

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@ast

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@en

prefLabel

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@ast

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@en

P1433

Q35218972-4B32F65D-8DD3-4FCD-B2AD-C8E920302BD9

P1476

Q35218972-940A7EAE-7C0E-4A05-8EC6-1FD14381FBD7

P2093

Q35218972-6591DB7F-97C2-4D76-B3F9-4BBED70BC1DE

Q35218972-781943FA-1E40-4979-8A21-64CFA4A06423

Q35218972-8E6D8D62-66A1-4AD8-820F-46504D188534

Q35218972-949CD16C-9869-4A58-9F67-3D3EA8984D3F

P2860

Q35218972-0750AAD1-AAF7-47A8-A5AB-38A54B0266AA

Q35218972-086C05CE-3807-4965-A25B-EA0D3EB39F04

Q35218972-19AC6257-BAEA-45F0-AFD1-898644F10685

Q35218972-2103FEA9-1F12-46F3-9E2E-224D161C0DB4

Q35218972-321EA6AA-89CD-469E-AB62-3EB20CE23E0C

Q35218972-32AC79ED-6AA5-4772-AE73-19B3C5FA55C0

Q35218972-338570DF-1B32-4D7D-8A56-98381B19253B

Q35218972-35734DE4-9B59-4651-A1D4-92B77B77DF25

Q35218972-374F96D1-F4B3-4F4E-B665-0A318D651973

Q35218972-47AE77A3-4130-47CB-AB4E-85A8EC119692

P304

Q35218972-FA33197E-DC75-4510-BF7D-352D3E55DF24

P31

Q35218972-3A42D5D8-AB63-4677-A429-B582C4EEEA6B

P356

Q35218972-7755B5B0-225A-4241-AB7F-ED6742714632

P407

Q35218972-83ED9AF2-0509-4114-81A3-8A04A605F63F

P433

Q35218972-5BD631F7-1E41-4928-983D-D1970AE0B08F

P478

Q35218972-7A559153-D3B5-4FCF-B1DD-5FB3EF39C63F

P577

Q35218972-6C7381E3-172D-4844-8514-67722D5A295F

P5875

Q35218972-463678DC-E67D-40FF-B4ED-8AE20A880F7C

P698

Q35218972-D90E74F7-1341-4022-8DF7-F6C08FD3EF77

P932

Q35218972-696490C3-116B-417F-A542-A22CD6013D46

P356

J.JMB.2011.08.004

P1433

Journal of Molecular Biology

P1476

Duplex unwinding and ATPase ac ...... are coupled by eIF4G and eIF4B

@en

P2093

Ali R Özeş

http://www.w3.org/2001/XMLSchema#string

Brian C Avanzino

http://www.w3.org/2001/XMLSchema#string

Christopher S Fraser

http://www.w3.org/2001/XMLSchema#string

Kateryna Feoktistova

http://www.w3.org/2001/XMLSchema#string

P2860

Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation

Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif

Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H

Mfold web server for nucleic acid folding and hybridization prediction

Control of mammalian translation by mRNA structure near caps.

The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence

Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase

ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding

A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3

Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions

P304

674-687

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.JMB.2011.08.004

http://www.w3.org/2001/XMLSchema#string

P407

P433

4

http://www.w3.org/2001/XMLSchema#string

P478

412

http://www.w3.org/2001/XMLSchema#string

P577

2011-08-05T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51570222

http://www.w3.org/2001/XMLSchema#string

P698

21840318

http://www.w3.org/2001/XMLSchema#string

P932

3175293

http://www.w3.org/2001/XMLSchema#string