About: Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction

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About: Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction Goto Sponge NotDistinct Permalink

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scientific article published on 01 June 1981

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 1981 (uk) article scientifique publié en 1981 (fr) im Juni 1981 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunu de 1981 (ast) scientific article published on 01 June 1981 (en)
publication date	wds:Q70175772-35C4BCD7-FE5E-4B1F-BDF0-83CF841F5CA6
publication date	1981-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70175772-1CF9E858-ABD3-43E8-B9E9-450FC31F6604
language of work or name	English
cites work	wds:Q70175772-14AE8A2B-07E2-4470-B749-2E2C990BC292 wds:Q70175772-32E0E464-AE85-4284-8B1F-28A160679DD9 wds:Q70175772-7576A270-1ECC-4042-950C-B1CB8306E968 wds:Q70175772-79884818-B0AB-4590-B815-A2A7EC37CB9D wds:Q70175772-82C6ECE1-7BAD-4AA4-8E4E-BFD4F441B267 wds:Q70175772-86F06CFB-B3A1-4056-8454-ED4AB2587414
cites work	X-ray determination of the GDP-binding site of Escherichia coli elongation factor Tu by substitution with ppGpp Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution The complete amino-acid sequence of elongation factor Tu from Escherichia coli Relation between structure and function of alpha/beta-proteins High resolution X-ray crystallographic analysis of a modified form of the elongation factor Tu:Guanosine diphosphate complex Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-Tu, from Escherichia coli
author name string	wds:Q70175772-20C0FC47-E201-435E-9611-6F6DA561C375 wds:Q70175772-2B058B63-10CE-4004-8ABD-405D3B4BFFE6 wds:Q70175772-2CB1F2FF-BFC5-461E-8213-2C823B109062 wds:Q70175772-61915CC3-E8C3-459B-8DC0-90AFCEA95F87 wds:Q70175772-C44E3951-2650-49FB-97BA-97203E2EB9E8 wds:Q70175772-C86B8ABE-3F09-44C5-A7D5-0D688C883986
author name string	Morikawa K Nyborg J Miller DL Clark BF Rubin JR la Cour TF
rdfs:label	Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (en) Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (nl)
skos:prefLabel	Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (en) Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (nl)
name	Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (en) Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (nl)
title	wds:Q70175772-AD500B50-4ECA-4090-82E4-A36FEE4F3B30
title	Structural features of the GDP binding site of elongation factor Tu from Escherichia coli as determined by x-ray diffraction (en)
page(s)	wds:Q70175772-2BD2541B-2642-4DAC-BE14-CE6AC96DA434
page(s)	177-179
instance of	wds:Q70175772-C8861592-2221-4590-9F29-C1504A1D5478
instance of	scholarly article
main subject	wds:Q70175772-63DDA8AF-C28C-43FC-926C-AAF610E9508C wds:Q70175772-7464858D-E5B8-4960-AEEA-28905A6A5524
main subject	X-ray diffraction Escherichia coli
PubMed ID	wds:Q70175772-F29470B3-9213-4615-8CF4-3B9CF02CA68C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7023989
PubMed ID	7023989
published in	wds:Q70175772-0908DC62-C6AE-4B42-9430-B7E753A6DAFB
published in	FEBS Letters
issue	wds:Q70175772-7049C0E9-55D7-4E22-83E0-F63E48B99404
volume	wds:Q70175772-1BE59613-981A-4CA0-92A6-8D58FCEA3EB4
issue	1
volume	129
DOI	wds:Q70175772-E8906E59-FDBA-453F-A74F-0F4C0B721C39
DOI	http://dx.doi.org/10.1016/0014-5793(81)80784-3
DOI	10.1016/0014-5793(81)80784-3
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70175772
is cites work of	Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors. Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure Antibodies specific for amino acid 12 of the ras oncogene product inhibit GTP binding Isolation of tef1 encoding translation elongation factor EF1α from the homobasidiomycete Schizophyllum commune A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome Sequence homology between EF‐1α, the α‐chain of elongation factor 1 from Artemia salina and elongation factor EF‐TU from Escherichia coli Elongation factor Tu is methylated in response to nutrient deprivation in Escherichia coli Cross-linking of tRNA at two different sites of the elongation factor Tu. The Elongation Factor EF-Tu and Its Two Encoding Genes Structural studies of ribosomes Formation and properties of a covalent complex between elongation factor Tu and Phe-tRNA bearing a photoaffinity probe on its 3-(3-amino-3-carboxypropyl)uridine residue Mutants of the elongation factor EF-Tu, a new class of nonsense suppressors Unusually strong immunological cross-reaction between elongation factor Tu of Escherichia coli and Bacillus subtilis
is cites work of	wds:Q36263941-54F16C1A-6FD7-4038-AF5B-ABDB6ECAF81B wds:Q37527421-AC8EF8D0-5527-4EFF-AD75-3DCB0DAD41BD wds:Q40169029-BD9F868C-B23B-4398-A9C1-57AEB86556A1 wds:Q37687967-BC8AC518-FBC4-4FCB-8ACB-A05C0F815FC6 wds:Q27728967-D0A65C51-1DA7-48BE-8A24-23E3BB632685 wds:Q37580219-BA799CA8-34CC-4254-9FA9-20D499FA42A4 wds:Q41389897-456F75B8-28AA-417E-9D2A-73F3CE2A8022 wds:Q38345731-0F476FCD-2BCF-4185-A901-94ACBC0A783C wds:Q42243507-CA8DB2BB-FB39-4DA7-AF36-3FBFFC9745C8 wds:Q58852001-0F766BFD-AF52-48F5-A9CD-67E2F53AB2E5 wds:Q36146125-6B5F6F68-2F90-4920-989F-BD929C7E6D84 wds:Q40089160-BFE0B797-09CE-4D0E-99B3-C8ABEF6B6046 wds:Q41560594-C31370E0-C22A-4D52-8DDD-0363C631F73A wds:Q70241259-2E3579BB-1A23-4AB0-81A8-148AAF7C3866

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