pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA. - Wikidata - awgldk - TriplyDB

pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA.

pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA.

http://www.wikidata.org/entity/Q34471932

about

Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome Mechanism of Elongation Factor-G-mediated Fusidic Acid Resistance and Fitness Compensation in Staphylococcus aureus The Impact of Aminoglycosides on the Dynamics of Translation Elongation Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases Loss of a conserved tRNA anticodon modification perturbs cellular signaling Evolutionary optimization of speed and accuracy of decoding on the ribosome Synthetic biology challenges long-held hypotheses in translation, codon bias and transcription.The divergence, actions, roles, and relatives of sodium-coupled bicarbonate transporters Accounting for biases in riboprofiling data indicates a major role for proline in stalling translation.Spatial Distribution and Ribosome-Binding Dynamics of EF-P in Live Escherichia coli.Intrinsic pKa values of 3'-N-α-l-aminoacyl-3'-aminodeoxyadenosines determined by pH dependent 1H NMR in H2O.eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G.The bacterial translation stress response.N(6)-methyladenosine in mRNA disrupts tRNA selection and translation-elongation dynamics Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding Mutations of highly conserved bases in the peptidyltransferase center induce compensatory rearrangements in yeast ribosomes.Two proofreading steps amplify the accuracy of genetic code translation A recent intermezzo at the Ribosome Club.Distinct XPPX sequence motifs induce ribosome stalling, which is rescued by the translation elongation factor EF-P Binding of Macrolide Antibiotics Leads to Ribosomal Selection against Specific Substrates Based on Their Charge and Size.Synonymous codons, ribosome speed, and eukaryotic gene expression regulation.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acids The ribosome in action: Tuning of translational efficiency and protein folding.Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids.Proofreading neutralizes potential error hotspots in genetic code translation by transfer RNAs.A comparative genomics study on the effect of individual amino acids on ribosome stalling.Maintenance of protein synthesis reading frame by EF-P and m(1)G37-tRNA.Trade-offs between tRNA abundance and mRNA secondary structure support smoothing of translation elongation rate.Measurement of average decoding rates of the 61 sense codons in vivo.Translational stalling at polyproline stretches is modulated by the sequence context upstream of the stall site.Selective desulfurization significantly expands sequence variety of 3'-peptidyl-tRNA mimics obtained by native chemical ligation.The 150 most important questions in cancer research and clinical oncology series: questions 57-66 : Edited by Chinese Journal of Cancer.Activities of the peptidyl transferase center of ribosomes lacking protein L27.Molecular insights into protein synthesis with proline residues.EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.Elongation factor P: Function and effects on bacterial fitness.Logical engineering of D-arm and T-stem of tRNA that enhances d-amino acid incorporation.RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.

P2860

Q27324728-FEDA360E-F871-443F-951A-8E9D5EF6910C Q27670650-67C8B885-04E7-4BC1-93AC-341F7D0ED49D Q27676402-CF28357D-606D-48CD-AD0D-71EBDFE38B38 Q27695680-0CE7A345-5CA3-40CB-B118-CDDB62F62921 Q28535022-2DB5E54F-CDF4-4342-86BE-8EAC21581773 Q28741198-32C7ADDD-F10D-4961-A949-568D861AEE31 Q30418054-45F1D280-C02F-4BE7-BA58-F56617D8A8B9 Q30440948-4D446014-5348-4325-A8E0-8446A4CA28D4 Q30858065-79640C69-296F-4EE7-8D43-C79D5D926428 Q33770615-B8B2EDF8-61BB-4DF6-A0E3-0E9DAB2BC710 Q33810255-D1A1A02F-F7DB-4D3D-BA7A-3ABA3E2B8DEB Q33878081-ADFC3AC6-8CB0-4A9E-BF7D-80769199281A Q34079096-E7173C93-4D1B-4FC6-82B5-D2D0C5507F23 Q34490409-A28FD579-35F3-4DDA-AFEF-93E08174B287 Q34508439-9D38DE51-EB2D-4956-A8D0-890A7DC81860 Q34750390-E64D29C8-71B2-452C-93C7-95D2397A1613 Q34807889-3806E816-5569-4222-81FE-E7FEBAEA07C4 Q36190559-19DA5689-907B-4BC7-98AF-1032AA3FF15B Q36264326-D00EA8A6-C929-4C56-A146-D75D52C79C45 Q37191901-EBC2FE0E-F894-468B-A8FA-ED4E0E50D4BF Q37428512-DD177A17-4962-4E9A-A66B-FB3F3537F91C Q38231225-1A61391B-493F-428D-9188-B62FDDEFA25F Q38594900-F86F4D57-A3D9-40CC-B831-65F4EC5B869B Q38782146-780353B4-6FE7-4BF3-8562-A540A3FF39E2 Q38838979-F0351743-1D8E-4B66-9C35-5A1C339A6097 Q39159551-A8AEEB89-C993-4804-BF24-608D9F3B32E7 Q39842250-46CBB9F1-D310-438E-B3CF-3F299BD89611 Q40451655-3284B9E5-2DD2-462A-9DC4-8A7A1B9CDF73 Q41144712-D42E5093-EDD2-431E-9602-CF4D2AF0997E Q41234550-B4EF2BAE-DF34-4E60-A550-AE658C50AE8D Q41788002-9C73D5C3-2A6D-4332-8645-46804E1E386F Q41851942-10034478-E8C4-4584-8B1B-1A90DB0CE659 Q42155357-79B00204-7897-41C6-BBF2-B42D09AFE6E7 Q42370046-F500FAAB-82B6-4B7D-A2A6-02BB2E0826A2 Q42578776-3458B0A5-6347-439A-9E1B-AE7C9B07463C Q45160993-8DA4E186-6CD4-409A-A1E0-40CE4B3A567B Q45223328-5271F466-C4E8-481C-807C-28FDB7B7C669 Q45335200-20FECC48-55C6-4729-B08E-2089D5A815FD Q47137027-A7BF0978-F8BC-4163-AC3D-BF9FCCD00A6F Q47235409-B104C524-1293-44B6-ABA9-C0E6AAEE56B0

P2860

pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA.

http://www.wikidata.org/entity/Q34471932

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@ast

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@en

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@nl

type

label

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@ast

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@en

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@nl

prefLabel

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@ast

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@en

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@nl

P1433

Q34471932-D86BFCAD-B13A-42E6-92B6-EF9633DA5682

P1476

Q34471932-AE6DB501-793E-4F6C-9E47-420B04A387AE

P2093

Q34471932-0125D6C5-6F99-4A73-BB5B-9CDD127F865B

Q34471932-10A1FDB1-68EF-41D9-941E-B13F72EADEF5

Q34471932-76A6E18C-C330-4B42-B12B-83D1D50C305D

Q34471932-CD8B3AAD-9E92-4440-972C-F7BF4A53257C

Q34471932-DFA7D05F-1BB3-41AB-AC4E-F6738EEE9A33

P2860

Q34471932-04634A74-9EFC-4B0B-B594-D6BB6506032C

Q34471932-06F6A4DB-B4FD-4962-912E-324C41F3D860

Q34471932-072A765E-0695-4913-BE24-65B3D48A818C

Q34471932-07CD4194-DD7C-4591-9E79-3F00F7877F1B

Q34471932-0B38C2C4-31D1-4AD1-9923-A106BF957F32

Q34471932-0B9979A3-C328-4307-98FF-A597835B4405

Q34471932-0EF75B0A-A94F-4E66-AE41-24B647CBF1D9

Q34471932-1A07A184-F602-4A41-B74E-DF0DDBB15A8D

Q34471932-1FC90C3A-1A83-4E3D-8F4E-C02CD5165B2F

Q34471932-2A64262E-FB26-41E8-AA35-099ECEEB276B

P304

Q34471932-0AAA163F-76B2-4497-B375-FC02DA659FEE

P31

Q34471932-1DA80087-FDF2-4E45-AE93-0F73158D6BF9

P356

Q34471932-D7647C8D-CD2C-4E69-9183-0E9228C2EDAC

P407

Q34471932-F25C4604-28D0-42BC-98C5-1C11749D558F

P433

Q34471932-FC8FE4D9-8EE4-4D40-98D2-D17978772BE3

P478

Q34471932-A8DA2D04-2A22-4501-B408-1488C53C38DB

P50

Q34471932-8A953843-40F8-4AE2-AE2C-BB85841457EC

Q34471932-B87DD1F8-0D98-493A-873B-DBF77C03CD0C

P577

Q34471932-F33D183D-D6AC-4E19-AFD2-F681FCC649C0

P5875

Q34471932-F18BCB4C-E489-43EA-9A70-AEB31ED2482A

P698

Q34471932-CFB3A8AB-C416-4CA3-9B33-0514E4D3BF43

P932

Q34471932-B7E721A4-6240-4421-8F4B-E4445B51C7F4

P356

PNAS.1012612107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

pH-sensitivity of the ribosoma ...... of the A-site aminoacyl-tRNA.

@en

P2093

Johan Åqvist

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

Ka-Weng Ieong

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

Michael Y Pavlov

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

Peter Strazewski

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

Stefan Trobro

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

P2860

Slow peptide bond formation by proline and other N-alkylamino acids in translation

The structural basis of ribosome activity in peptide bond synthesis

Structural insights into peptide bond formation.

The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA

The kinetics of ribosomal peptidyl transfer revisited.

Chemical models of peptide formation in translation.

Fast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3

Mechanism of peptide bond synthesis on the ribosome.

An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA.

The path to perdition is paved with protons.

P304

79-84

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

P31

scholarly article

P356

10.1073/PNAS.1012612107

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

P407

P433

1

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

P478

108

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

P50

Magnus Johansson

Måns Ehrenberg

P577

2010-12-17T00:00:00Z

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

P5875

49694188

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

P698

21169502

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

P932

3017169

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