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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im Februar 1990 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в лютому 1990 (uk)
publication date	wds:Q59051365-EC301806-6E8C-47E0-8AD5-DF622E121C75
publication date	1990-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59051365-DE4F045E-D18F-4CEC-A4E0-023D5A46B19A
language of work or name	English
exact match	wds:Q59051365-D8F6059F-7097-453D-8055-293B8763CDA5
exact match	https://scigraph.springernature.com/pub.10.1038/343687a0
cites work	wds:Q59051365-13D06555-9F24-46DB-8ABA-4A1D78529FB9 wds:Q59051365-141090F3-DE98-41DD-B7E7-AFA4D6E06BB2 wds:Q59051365-1F4B921C-789F-4BB7-91E8-80714AE91444 wds:Q59051365-2B95CC31-3012-46D8-9724-9C96EE59044A wds:Q59051365-41E186D9-DBB3-4AE6-92D5-40E9E9E66333 wds:Q59051365-486ADA84-465B-4295-AD7D-DBC9CBF4A345 wds:Q59051365-54C9559E-4414-4CBB-A1A7-1F568564D5DD wds:Q59051365-56D6D3F4-982F-4349-ACB5-917E735D3951 wds:Q59051365-64E13090-4FA0-4393-90F2-2526420F17AE wds:Q59051365-79D76E58-A5BB-43F5-8BB2-8A67E054B4B9 wds:Q59051365-88DC2597-0D52-405C-BB28-1F65A424ABD6 wds:Q59051365-94D0666F-09A8-495E-8097-1C0412CB204F wds:Q59051365-A66D24EC-8F86-4F75-80C5-420AE99106D9 wds:Q59051365-B207ACB9-00EE-4130-8062-31D00AC732F0 wds:Q59051365-BD737605-0A8E-466E-9303-7F29EB7883AE wds:Q59051365-C8A073EC-DCE0-4217-8EFE-5A8467D6C90C wds:Q59051365-D544552E-39B9-496D-8DA8-D23A698CFE91 wds:Q59051365-DE4127E2-5F8E-40A1-8D98-57B5EC6344DD wds:Q59051365-F327F87C-B290-4386-8CEE-B62FF2527F39
cites work	Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Stereochemically restrained refinement of macromolecular structures Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1 Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2 . 8 A resolution A graphics model building and refinement system for macromolecules Structure of ras proteins Reexamination of the Three-Dimensional Structure of the Small Subunit of RuBisCo from Higher Plants Three-dimensional pattern recognition: An approach to automated interpretation of electron density maps of proteins Tertiary structure of plant RuBisCO: domains and their contacts Crystallographic R factor refinement by molecular dynamics Structure of ferredoxin I from Azotobacter vinelandii Structure of satellite tobacco necrosis virus at 3.0 A resolution Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor Iron-sulfur clusters and protein structure of Azotobacter ferredoxin at 2.0 A resolution The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-phosphogluconic aldolase at 3.5-A resolution The singly-wound parallel β barrel: A proposed structure for 2-keto-3-deoxy-6-phosphogluconate aldolase
author name string	wds:Q59051365-6AD4EE26-A76B-4191-A08E-D75E1DA0D487 wds:Q59051365-89331486-4F8B-44EE-A0CD-69D302B988D5
author name string	T. Alwyn Jones Carl-Ivar Bränd´en
rdfs:label	Between objectivity and subjectivity (en) Between objectivity and subjectivity (nl)
skos:prefLabel	Between objectivity and subjectivity (en) Between objectivity and subjectivity (nl)
name	Between objectivity and subjectivity (en) Between objectivity and subjectivity (nl)
title	wds:Q59051365-9C9EF60D-F5FE-4535-86D6-9E2E36F34AD8
title	Between objectivity and subjectivity (en)
page(s)	wds:Q59051365-9638965A-CA78-4411-AB58-F7CA56AFF53B
page(s)	687-689
instance of	wds:Q59051365-B85F28A3-7B4B-496B-B7D2-4C5E9FEEF427
instance of	scholarly article
published in	wds:Q59051365-B26E1EF0-48A6-4A46-9622-C7D73D4C2837
published in	Nature
issue	wds:Q59051365-EEDE76F2-422F-469C-B573-DF3440A2537F
volume	wds:Q59051365-05C9F1F7-A6FC-4AA7-AD97-953D12F04007
issue	6260
volume	343
DOI	wds:Q59051365-84E67088-47BD-4CFE-8C38-BE8929DC4D18
DOI	http://dx.doi.org/10.1038/343687A0
DOI	10.1038/343687A0
Dimensions Publication ID	wds:Q59051365-034F7A8C-A3A4-4367-91B7-F792B0E304DA
Dimensions Publication ID	1035234503
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59051365
is cites work of	Determining relevant features to recognize electron density patterns in x-ray protein crystallography. A proteomic Ramachandran plot (PRplot). Avoidable errors in deposited macromolecular structures: an impediment to efficient data mining A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases Knowledge-based model building of proteins: concepts and examples Where freedom is given, liberties are taken Homo crystallographicus--quo vadis? Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Checking your imagination: applications of the free R value VERIFY3D: assessment of protein models with three-dimensional profiles Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution Interaction with type IV pili induces structural changes in the bacterial outer membrane secretin PilQ. New Biological Insights from Better Structure Models Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server. The PDB_REDO server for macromolecular structure model optimization A decade of progress in understanding the structural basis of protein synthesis. Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles. Outcome of the first electron microscopy validation task force meeting Activation of dimeric ABA receptors elicits guard cell closure, ABA-regulated gene expression, and drought tolerance

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