About: Structure of Ribonuclease

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Structure of Ribonuclease Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

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 1967 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в лютому 1967 (uk)
publication date	wds:Q58995270-34C4A3D0-0ECD-43B9-BB97-F4ACFD436870
publication date	1967-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58995270-9A96A533-DBC8-4195-8CAC-BBC9F45CCD8E
language of work or name	English
exact match	wds:Q58995270-FE9CEBAF-F0CF-4417-B6A3-D83A1940555D
exact match	https://scigraph.springernature.com/pub.10.1038/213557a0
cites work	wds:Q58995270-03B5F2D7-364D-4BA3-A499-26FB97814561 wds:Q58995270-22EEAA8F-BC98-4CEC-9065-EEBFD0D5B0D6 wds:Q58995270-3F071340-CE98-41D1-B168-0260E5258FE5 wds:Q58995270-8A0176FB-A408-4D4E-81F6-F9C9D3B326FA wds:Q58995270-97901F67-90E7-40C0-9BA2-7B18DF2D52F5 wds:Q58995270-A5F2F434-EC19-4203-AC1F-17E4DC39E6BB wds:Q58995270-B5DED886-DB7D-4C52-B1D0-471A698546BD
cites work	Structure of myoglobin: A three-dimensional Fourier synthesis at 2 A. resolution The amino-acid sequence x-ray methods, and its correlation with chemical data Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution The structure of carboxypeptidase A ON THE ENZYMIC ACTIVITY OF SUBTILISIN-MODIFIED RIBONUCLEASE Complex of Ribonuclease with a Substrate Analogue, Cytidine 2″-Phosphate
author name string	wds:Q58995270-11DA21D1-690E-4B94-A1E4-0B5E340DCBCE wds:Q58995270-3EBE995C-EEE7-44D6-9F88-DE8C13D07005 wds:Q58995270-54BA7AC0-3468-4FCF-BA0D-426FD7D9F828 wds:Q58995270-587C8F84-E3CB-4DA1-858A-088B3AA286C9 wds:Q58995270-935B1C08-63BC-4C1C-9463-AC1E9303A9B3 wds:Q58995270-9A4BDD84-5954-47D3-A330-CFE9B9D6ED59 wds:Q58995270-D2FE5098-62C8-48D3-B587-DA204983DFA7 wds:Q58995270-E71BC332-8A5C-470D-9025-EA3598E512B8
author name string	S Shall S J Morris R A Palmer B A Woolhouse C H Carlisle H P Avey M O Boles S A Evans
rdfs:label	Structure of Ribonuclease (en) Structure of Ribonuclease (nl)
skos:prefLabel	Structure of Ribonuclease (en) Structure of Ribonuclease (nl)
name	Structure of Ribonuclease (en) Structure of Ribonuclease (nl)
title	wds:Q58995270-4EDFD920-5CEF-4576-B2FD-21593529D917
title	Structure of ribonuclease (en)
page(s)	wds:Q58995270-B6F622CD-EFBA-49F1-9D26-507ADC53D5A2
page(s)	557-562
instance of	wds:Q58995270-59879423-2B4B-4CC3-BE5D-FBF2CAFACCDA
instance of	scholarly article
PubMed ID	wds:Q58995270-2FE7B520-9985-4986-9FC7-1F8BEB00C262
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6032249
PubMed ID	6032249
published in	wds:Q58995270-E0FFF463-6B77-4182-AA36-DF14EF17D4ED
published in	Nature
issue	wds:Q58995270-681A3278-A1C0-443A-BEB4-689313F5FCD7
volume	wds:Q58995270-2D672F25-29D1-4766-B194-2D432DC3931B
issue	5076
volume	213
DOI	wds:Q58995270-005175B3-B9DB-40E5-AF66-86F2E767C6FD
DOI	http://dx.doi.org/10.1038/213557A0
DOI	10.1038/213557A0
Fatcat ID	wds:Q58995270-4AB4CC96-CC99-499F-8329-65B7227838ED
Fatcat ID	release_q6wek2w7knbdvcf6ti5oiteeuy
corrigendum / erratum	wds:Q58995270-EF4A0F05-B43C-4ADC-8C66-264CDC1C7A50
corrigendum / erratum	Erratum: Corrigendum
Dimensions Publication ID	wds:Q58995270-4078EB82-1B82-4522-9F0B-21E5A9F12D8B
Dimensions Publication ID	1052932299
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58995270
is cites work of	Nucleases: diversity of structure, function and mechanism. Structural and functional importance of local and global conformational fluctuations in the RNase A superfamily Development of a lectin microarray based on an evanescent-field fluorescence principle A structural basis of the interactions between leucine-rich repeats and protein ligands Correlation of amino acid sequence and conformation in tobacco mosaic virus The refined crystal structure of ribonuclease A at 2.0 A resolution Tertiary Structure of Ribonuclease Conformational Adaptability in Enzymes A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits A Deuterium‐Hydrogen Exchange Study of Inhibitor‐Induced Conformational Changes in Ribonuclease A Value of general Acid-base catalysis to ribonuclease a. Nuclear magnetic resonance studies of the structure and binding sites of enzymes. I. Histidine residues The introduction of specific sites for heavy metal binding in a crystalline protein Crystallographic analysis of N-acetyl-dl-homocysteinyl ribonuclease derivatives The Structure of Ribonuclease-S at 6 A Resolution [48] thiolation ‘Crystal lattice engineering,’ an approach to engineer protein crystal contacts by creating intermolecular symmetry: Crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines Novel non-productively bound ribonuclease inhibitor complexes — high resolution X-ray refinement studies on the binding of RNase-A to cytidylyl-2′,5′-guanosine (2′,5′CpG) and deoxycytidylyl-3′,5′-guanosine (3′,5′dCpdG) Simultaneous estimation of the association constants of glycoprotein glycoforms to a common protein by capillary electrophoresis Protein Structure: Structure and Function of Proteins Molecular palaeogenetics: Amino acid sequence homology in ribonuclease and lysozyme The use of molecular models in evaluating protein and peptide conformations X-Ray Diffraction Studies of Crystalline Amino Acids, Peptides and Proteins Attempt to locate the α-Helical Segments of Ribonuclease
is cites work of	wds:Q30431892-39A05935-20CF-4BCA-937A-63046C4CFD14 wds:Q34661864-237A3C8E-AB43-4214-AA86-E6E6A31C5C05

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 183 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software