Directional transition from initiation to elongation in bacterial translation. - Wikidata - wikimedia - TriplyDB

Directional transition from initiation to elongation in bacterial translation.

Directional transition from initiation to elongation in bacterial translation.

http://www.wikidata.org/entity/Q41985630

about

Review: Translational GTPases Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding The ribosome in action: Tuning of translational efficiency and protein folding.Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways Effect of Fusidic Acid on the Kinetics of Molecular Motions During EF-G-Induced Translocation on the Ribosome.A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria.Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association.Translation initiation in bacterial polysomes through ribosome loading on a standby site on a highly translated mRNA.

P2860

Q28077489-0AABE90D-8A24-4B70-9F3A-519BAD42646B Q34543629-605D4227-A2D2-4045-B3DC-D25D361C1ECE Q38838979-2399828E-3B80-4831-A683-67B4F5AAAD57 Q41599605-DCC51E2D-C764-43B5-B2B4-320E2FA14D11 Q41620537-CE1C3C53-7D02-4861-8902-D862808ED1CD Q47131408-83B74238-4073-4026-91CD-76B2373FEB9F Q47299294-0DF0EE3C-2DE1-46BA-BBA8-A7209FEB2E62 Q50315933-136B4176-4669-4B71-AB86-9F3158733366 Q52312088-21E77D40-CF48-4C0F-908C-D09D25288901 Q52327539-FCADD576-CCF4-4EB1-A714-BE4E46290956

P2860

Directional transition from initiation to elongation in bacterial translation.

http://www.wikidata.org/entity/Q41985630

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Directional transition from initiation to elongation in bacterial translation.

@en

type

label

Directional transition from initiation to elongation in bacterial translation.

@en

prefLabel

Directional transition from initiation to elongation in bacterial translation.

@en

P1433

Q41985630-FF68BD16-EFDE-49D7-8B34-E662327A799B

P1476

Q41985630-03C56002-CBA1-422B-9F9C-187D76D225FE

P2093

Q41985630-97C7C9A1-0BA6-494D-B29A-2CF9D7620DEE

P2860

Q41985630-008202E5-A2FF-4CBE-B21B-A449F5DF0143

Q41985630-0AE1D556-B8D6-4704-8AB1-BA48C4C0AD8B

Q41985630-0B8263A3-CEC8-43E1-96A8-3B0A5BED2CA9

Q41985630-10DB0D5F-5784-41E0-BD4F-056161F586B6

Q41985630-13C64A41-386A-4180-9B45-3C132D6D06F1

Q41985630-16383040-AE2F-4BD7-A90A-D7F19519C88C

Q41985630-16B54988-32E3-489F-B7D6-834C657802C9

Q41985630-17F29B3A-577E-43B1-B0AD-3A7604BF52BA

Q41985630-1CF70093-6A2E-4713-A829-05F419D65C7E

Q41985630-298DA12D-4545-400B-9E97-510A001AD044

P304

Q41985630-49539D04-B8D0-4FBD-AB0B-01B92463A110

P31

Q41985630-EEE7B517-7435-489B-9E83-B54E37CF89A4

P356

Q41985630-63C71880-BF58-49D6-BEE1-6E26A8BFCCA7

P433

Q41985630-7720EE0F-9B86-48FC-8EB9-2290076B8647

P478

Q41985630-1643AE08-6B77-4530-A953-AB0F42B0B149

P50

Q41985630-7DDCD23C-8147-4CFC-847D-3E30609A9261

Q41985630-A8AF95A7-30CA-4A96-851D-944C8AA7AA9D

Q41985630-DA9FC373-5706-4F36-AD53-CECEC443C3B2

Q41985630-E400B145-20EE-423C-8726-73AEF85E1757

P577

Q41985630-70A85061-20BE-45A6-96BC-BAAACF5E7B4B

P5875

Q41985630-88A6AF82-F587-4CF5-BD11-6964382DF15A

P698

Q41985630-ED0B3629-1EA2-48C1-A983-C10B187760AA

P932

Q41985630-F4684CBD-5D8A-4EBE-85D4-B52E0FBF16F5

P356

P1433

Nucleic Acids Research

P1476

Directional transition from initiation to elongation in bacterial translation

@en

P2093

Akanksha Goyal

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

P2860

Ribosome formation from subunits studied by stopped-flow and rayleigh light scattering

Ribosomal initiation complex-driven changes in the stability and dynamics of initiation factor 2 regulate the fidelity of translation initiation

X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding

Structural Dynamics of Bacterial Translation Initiation Factor IF2

Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor

Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases

eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining

Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity.

Translation initiation factor IF2 interacts with the 30 S ribosomal subunit via two separate binding sites.

Mapping the fMet-tRNA(f)(Met) binding site of initiation factor IF2.

P304

10700-10712

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

P31

scholarly article

P356

10.1093/NAR/GKV869

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

P433

22

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

P478

43

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

P50

Riccardo Belardinelli

Cristina Maracci

P577

2015-09-03T00:00:00Z

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

P5875

281458440

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

P698

26338773

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

P932

4678851

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