FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1983952649> ?p ?o ?g. }

• W1983952649 endingPage "1782" @default.
• W1983952649 startingPage "1778" @default.
• W1983952649 abstract "Structural maintenance of chromosome (SMC) proteins play a central role in higher-order chromosome structure in all kingdoms of life [1Haering C.H. Nasmyth K. Building and breaking bridges between sister chromatids.Bioessays. 2003; 25: 1178-1191Crossref PubMed Scopus (143) Google Scholar, 2Gruber S. Haering C.H. Nasmyth K. Chromosomal cohesin forms a ring.Cell. 2003; 112: 765-777Abstract Full Text Full Text PDF PubMed Scopus (426) Google Scholar, 3Swedlow J.R. Hirano T. The making of the mitotic chromosome Modern insights into classical questions.Mol. Cell. 2003; 11: 557-569Abstract Full Text Full Text PDF PubMed Scopus (224) Google Scholar, 4Morrison C. Vagnarelli P. Sonoda E. Takeda S. Earnshaw W.C. Sister chromatid cohesion and genome stability in vertebrate cells.Biochem. Soc. Trans. 2003; 31: 263-265Crossref PubMed Google Scholar, 5Jessberger R. The many functions of SMC proteins in chromosome dynamics.Nat. Rev. Mol. Cell Biol. 2002; 3: 767-778Crossref PubMed Scopus (126) Google Scholar]. SMC proteins consist of a long coiled-coil domain that joins an ATP binding cassette (ABC) ATPase domain on one side and a dimerization domain on the other side [6Melby T.E. Ciampaglio C.N. Briscoe G. Erickson H.P. The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins Long, antiparallel coiled coils, folded at a flexible hinge.J. Cell Biol. 1998; 142: 1595-1604Crossref PubMed Scopus (324) Google Scholar]. SMC proteins require ATP binding or hydrolysis to promote cohesion and condensation, which is suggested to proceed via formation of SMC rings or assemblies [7Case R.B. Chang Y.P. Smith S.B. Gore J. Cozzarelli N.R. Bustamante C. The bacterial condensin MukBEF compacts DNA into a repetitive, stable structure.Science. 2004; 305: 222-227Crossref PubMed Scopus (41) Google Scholar, 8Bazett-Jones D.P. Kimura K. Hirano T. Efficient supercoiling of DNA by a single condensin complex as revealed by electron spectroscopic imaging.Mol. Cell. 2002; 9: 1183-1190Abstract Full Text Full Text PDF PubMed Scopus (93) Google Scholar, 9Arumugam P. Gruber S. Tanaka K. Haering C.H. Mechtler K. Nasmyth K. ATP hydrolysis is required for cohesin's association with chromosomes.Curr. Biol. 2003; 13: 1941-1953Abstract Full Text Full Text PDF PubMed Scopus (202) Google Scholar, 10Kimura K. Rybenkov V.V. Crisona N.J. Hirano T. Cozzarelli N.R. 13S condensin actively reconfigures DNA by introducing global positive writhe Implications for chromosome condensation.Cell. 1999; 98: 239-248Abstract Full Text Full Text PDF PubMed Scopus (260) Google Scholar, 11Weitzer S. Lehane C. Uhlmann F. A model for ATP hydrolysis-dependent binding of cohesin to DNA.Curr. Biol. 2003; 13: 1930-1940Abstract Full Text Full Text PDF PubMed Scopus (162) Google Scholar]. To learn more about the role of ATP in the architecture of SMC proteins, we report crystal structures of nucleotide-free and ATP bound P. furiosus SMC ATPase domains. ATP dimerizes two SMC ATPase domains by binding to opposing Walker A and signature motifs, indicating that ATP binding can directly assemble SMC proteins. DNA stimulates ATP hydrolysis in the engaged SMC ABC domains, suggesting that ATP hydrolysis can be allosterically regulated. Structural and mutagenesis data identify an SMC protein conserved-arginine finger that is required for DNA stimulation of the ATPase activity and directly connects a putative DNA interaction site to ATP. Our results suggest that stimulation of the SMC ATPase activity may be a specific feature to regulate the ATP-driven assembly and disassembly of SMC proteins." @default.
• W1983952649 created "2016-06-24" @default.
• W1983952649 creator A5041686856 @default.
• W1983952649 creator A5063163809 @default.
• W1983952649 creator A5064495138 @default.
• W1983952649 date "2004-10-01" @default.
• W1983952649 modified "2023-10-14" @default.
• W1983952649 title "Structural Biochemistry of ATP-Driven Dimerization and DNA-Stimulated Activation of SMC ATPases" @default.
• W1983952649 cites W1969008019 @default.
• W1983952649 cites W1972307085 @default.
• W1983952649 cites W1976758542 @default.
• W1983952649 cites W1977817512 @default.
• W1983952649 cites W1978696228 @default.
• W1983952649 cites W1992864103 @default.
• W1983952649 cites W2010233450 @default.
• W1983952649 cites W2013035015 @default.
• W1983952649 cites W2013190249 @default.
• W1983952649 cites W2022616695 @default.
• W1983952649 cites W2031077971 @default.
• W1983952649 cites W2034217568 @default.
• W1983952649 cites W2042339569 @default.
• W1983952649 cites W2059634393 @default.
• W1983952649 cites W2063450668 @default.
• W1983952649 cites W2072135452 @default.
• W1983952649 cites W2075250295 @default.
• W1983952649 cites W2080113789 @default.
• W1983952649 cites W2083817316 @default.
• W1983952649 cites W2090385798 @default.
• W1983952649 cites W2107554748 @default.
• W1983952649 cites W2120588322 @default.
• W1983952649 cites W2143644703 @default.
• W1983952649 cites W2170122994 @default.
• W1983952649 doi "https://doi.org/10.1016/j.cub.2004.09.044" @default.
• W1983952649 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15458651" @default.
• W1983952649 hasPublicationYear "2004" @default.
• W1983952649 type Work @default.
• W1983952649 sameAs 1983952649 @default.
• W1983952649 citedByCount "151" @default.
• W1983952649 countsByYear W19839526492012 @default.
• W1983952649 countsByYear W19839526492013 @default.
• W1983952649 countsByYear W19839526492014 @default.
• W1983952649 countsByYear W19839526492015 @default.
• W1983952649 countsByYear W19839526492016 @default.
• W1983952649 countsByYear W19839526492017 @default.
• W1983952649 countsByYear W19839526492018 @default.
• W1983952649 countsByYear W19839526492019 @default.
• W1983952649 countsByYear W19839526492020 @default.
• W1983952649 countsByYear W19839526492021 @default.
• W1983952649 countsByYear W19839526492022 @default.
• W1983952649 countsByYear W19839526492023 @default.
• W1983952649 crossrefType "journal-article" @default.
• W1983952649 hasAuthorship W1983952649A5041686856 @default.
• W1983952649 hasAuthorship W1983952649A5063163809 @default.
• W1983952649 hasAuthorship W1983952649A5064495138 @default.
• W1983952649 hasBestOaLocation W19839526491 @default.
• W1983952649 hasConcept C104317684 @default.
• W1983952649 hasConcept C115260700 @default.
• W1983952649 hasConcept C115821613 @default.
• W1983952649 hasConcept C121332964 @default.
• W1983952649 hasConcept C142089489 @default.
• W1983952649 hasConcept C152369539 @default.
• W1983952649 hasConcept C178108356 @default.
• W1983952649 hasConcept C30481170 @default.
• W1983952649 hasConcept C54355233 @default.
• W1983952649 hasConcept C62520636 @default.
• W1983952649 hasConcept C86803240 @default.
• W1983952649 hasConceptScore W1983952649C104317684 @default.
• W1983952649 hasConceptScore W1983952649C115260700 @default.
• W1983952649 hasConceptScore W1983952649C115821613 @default.
• W1983952649 hasConceptScore W1983952649C121332964 @default.
• W1983952649 hasConceptScore W1983952649C142089489 @default.
• W1983952649 hasConceptScore W1983952649C152369539 @default.
• W1983952649 hasConceptScore W1983952649C178108356 @default.
• W1983952649 hasConceptScore W1983952649C30481170 @default.
• W1983952649 hasConceptScore W1983952649C54355233 @default.
• W1983952649 hasConceptScore W1983952649C62520636 @default.
• W1983952649 hasConceptScore W1983952649C86803240 @default.
• W1983952649 hasIssue "19" @default.
• W1983952649 hasLocation W19839526491 @default.
• W1983952649 hasLocation W19839526492 @default.
• W1983952649 hasOpenAccess W1983952649 @default.
• W1983952649 hasPrimaryLocation W19839526491 @default.
• W1983952649 hasRelatedWork W1522520852 @default.
• W1983952649 hasRelatedWork W188370144 @default.
• W1983952649 hasRelatedWork W1928090971 @default.
• W1983952649 hasRelatedWork W1998346523 @default.
• W1983952649 hasRelatedWork W2027320544 @default.
• W1983952649 hasRelatedWork W2097201830 @default.
• W1983952649 hasRelatedWork W2138051350 @default.
• W1983952649 hasRelatedWork W2145020264 @default.
• W1983952649 hasRelatedWork W2278072455 @default.
• W1983952649 hasRelatedWork W2791426457 @default.
• W1983952649 hasVolume "14" @default.
• W1983952649 isParatext "false" @default.
• W1983952649 isRetracted "false" @default.
• W1983952649 magId "1983952649" @default.
• W1983952649 workType "article" @default.