About: Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization

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

About: Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization Goto Sponge NotDistinct Permalink

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

scientific journal article

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 2003 (ast) vědecký článek publikovaný v roce 2003 (cs) 2003 թուականի Յունիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в червні 2003 (uk) 2003 թվականի հունիսին հրատարակված գիտական հոդված (hy) im Juni 2003 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en 2003 (fr) scientific journal article (en) vedecký článok (publikovaný 2003/06/19) (sk) wetenschappelijk artikel (gepubliceerd op 2003/06/19) (nl) مقالة علمية (نشرت في 19-6-2003) (ar)
publication date	wds:Q28486771-5E33644F-74FA-4281-9EB7-71B4FB02BE84
publication date	2003-06-19 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28486771-834B9ADB-F20C-4F73-AFE6-763DBD1C54FF
language of work or name	English
cites work	wds:Q28486771-013E90FB-B9FD-4259-94C8-045530E602CF wds:Q28486771-09315643-61D4-4E5C-AFA8-8548D6BE2984 wds:Q28486771-0D47076A-976A-46B4-B8C3-D9B81A548E89 wds:Q28486771-11B3D2A5-177E-4A98-A8FA-DA3CBA502C8A wds:Q28486771-16811A2B-89DF-4F02-8373-CE3352AD2344 wds:Q28486771-2368CFBA-825A-4BBE-82D1-8DA6A8A0B2BD wds:Q28486771-31B12D6F-6846-442D-B25D-F599C4B600E9 wds:Q28486771-55E65013-4D5F-4C63-9D9D-AD93AAC58642 wds:Q28486771-59CA6D21-5FC9-461A-84E2-DF040D5865E2 wds:Q28486771-5AA907F8-D221-4BFB-AFAF-18AD1A171672 wds:Q28486771-6A743316-A720-4561-9332-2F5AE86D981E wds:Q28486771-6B42DC4B-6E07-4608-B288-C3EC32C335A9 wds:Q28486771-7B5F82E1-4FF8-4002-9C37-75271C671F7E wds:Q28486771-83921B16-70AC-4313-AA4D-8513D01175D6 wds:Q28486771-A2753E10-8CDF-4E5D-96DB-EC8635A7257B wds:Q28486771-AC3EBB83-E5E3-4E5E-A9C2-6D83CFE794DC wds:Q28486771-B77ADE42-4F98-435E-8090-6125BAC40353 wds:Q28486771-B7E9F1B8-D4A8-4C78-8E14-D7F992011497 wds:Q28486771-CB7FDAF2-DDDF-4B3B-828F-C65FAD525861 wds:Q28486771-CF52EF50-C1C0-417D-A1EA-1490D92FA909 wds:Q28486771-CF5EA028-09C2-4BCE-8CE2-47FF92EE7D53 wds:Q28486771-D0941A12-5E46-4EE2-B04C-7C048386E6A1 wds:Q28486771-DE11BC6F-B363-4A8F-9032-F472D316E04F wds:Q28486771-E8FE3FC4-A0D8-4CF0-8FA6-514B438C2342 wds:Q28486771-EC079798-655C-48D7-847B-3B21A24CA378 wds:Q28486771-F793BFAE-A14F-4DCE-9626-312C54BF9712 wds:Q28486771-F804124D-B4AA-4DE4-BC44-749C789E2AAC
cites work	SMART, a simple modular architecture research tool: identification of signaling domains Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence SETOR: hardware-lighted three-dimensional solid model representations of macromolecules A practical guide to the preparation of Ca2+ buffers Knowledge based modelling of homologous proteins, Part II: Rules for the conformations of substituted sidechains Knowledge based modelling of homologous proteins, Part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures Analysis and prediction of functional sub-types from protein sequence alignments. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Recent improvements to the SMART domain-based sequence annotation resource An evaluation of the performance of an automated procedure for comparative modelling of protein tertiary structure Structure of the adenylyl cyclase catalytic core Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: a progenitor of mammalian adenylyl cyclases Catalytic mechanism and regulation of mammalian adenylyl cyclases. Two amino acid substitutions convert a guanylyl cyclase, RetGC-1, into an adenylyl cyclase. Exchange of substrate and inhibitor specificities between adenylyl and guanylyl cyclases. The catalytic mechanism of mammalian adenylyl cyclase. Equilibrium binding and kinetic analysis of P-site inhibition Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis A guanylyl cyclase from Paramecium with 22 transmembrane spans. Expression of the catalytic domains and formation of chimeras with the catalytic domains of mammalian adenylyl cyclases Eukaryotic-like adenylyl cyclases in Mycobacterium tuberculosis H37Rv: cloning and characterization Adenylyl cyclase Rv1264 from Mycobacterium tuberculosis has an autoinhibitory N-terminal domain CyaG, a novel cyanobacterial adenylyl cyclase and a possible ancestor of mammalian guanylyl cyclases Biochemical characterization of the intracellular domain of the human guanylyl cyclase C receptor provides evidence for a catalytically active homotrimer GTPgammaS regulation of a 12-transmembrane guanylyl cyclase is retained after mutation to an adenylyl cyclase Functional Classification of cNMP-binding Proteins and Nucleotide Cyclases with Implications for Novel Regulatory Pathways in Mycobacterium tuberculosis
author name string	wds:Q28486771-D5427BF5-C863-42E2-8E2E-96B562293A51 wds:Q28486771-FBBEB63C-DF12-40B2-9CDA-2C024E80BB42
OpenCitations bibliographic resource ID	wds:Q28486771-E6090F3C-7969-41A3-836B-BD3E7E72AA99
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1165570
author name string	M. Subramaniam N. Srinivasan
OpenCitations bibliographic resource ID	1165570
rdfs:label	Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (en) Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (nl) Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (ast)
skos:prefLabel	Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (en) Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (nl) Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (ast)
name	Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (en) Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (nl) Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (ast)
author	wds:Q28486771-319964FB-D824-475F-B326-E3E87C80B43B wds:Q28486771-7247FB1D-0744-4417-AEB0-3B26B91426FC
author	Sandhya Srikant Visweswariah Avinash Shenoy
title	wds:Q28486771-6EB7F449-BC97-483C-BF68-DB2C74417AE3
title	Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization (en)
page(s)	wds:Q28486771-AB54ACE6-BE68-478D-9EBE-1D134291BC25
page(s)	253–259
instance of	wds:Q28486771-AA730314-F68A-4E12-9D42-259ABD420508
instance of	scholarly article
main subject	wds:Q28486771-25079C25-0D84-4001-9E1C-1DD8C990CDED wds:Q28486771-A259B150-9E36-4472-8AA6-BC78AD4A2F31 wds:Q28486771-C2121D07-327E-4FD8-B43B-494D3BBE5A9B
main subject	Mycobacterium tuberculosis

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, 180 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software