Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
about
Reconstitution and subunit geometry of human condensin complexesCondensins: universal organizers of chromosomes with diverse functionsBacillus subtilis RecN binds and protects 3'-single-stranded DNA extensions in the presence of ATP.Dynamic assembly, localization and proteolysis of the Bacillus subtilis SMC complex.Multistep assembly of DNA condensation clusters by SMC.Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteinsThe Role of MukE in Assembling a Functional MukBEF ComplexAn asymmetric SMC-kleisin bridge in prokaryotic condensinRAD50, an SMC family member with multiple roles in DNA break repair: how does ATP affect function?The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins.In vivo architecture and action of bacterial structural maintenance of chromosome proteins.Organization and segregation of bacterial chromosomes.RecN is a cohesin-like protein that stimulates intermolecular DNA interactions in vitro.Recruitment of SMC by ParB-parS organizes the origin region and promotes efficient chromosome segregation.A new family of bacterial condensinsMaintenance of chromosome structure in Pseudomonas aeruginosaUsing DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.SCFSlimb ubiquitin ligase suppresses condensin II-mediated nuclear reorganization by degrading Cap-H2.Crystal structure of the Mre11-Rad50-ATPγS complex: understanding the interplay between Mre11 and Rad50SMC proteins and chromosome mechanics: from bacteria to humans.DNA reshaping by MukB. Right-handed knotting, left-handed supercoiling.Three-dimensional topology of the SMC2/SMC4 subcomplex from chicken condensin I revealed by cross-linking and molecular modelling.SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis.An SMC ATPase mutant disrupts chromosome segregation in Caulobacter.SMC complexes in bacterial chromosome condensation and segregation.A mycobacterial smc null mutant is proficient in DNA repair and long-term survival.Resolving chromosome segregation in bacteria.ATP hydrolysis is required for relocating cohesin from sites occupied by its Scc2/4 loading complex.SMC condensation centers in Bacillus subtilis are dynamic structuresPseudomonas aeruginosa Condensins Support Opposite Differentiation States.The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes.ATP-induced shrinkage of DNA with MukB protein and the MukBEF complex of Escherichia coli.Control of Smc Coiled Coil Architecture by the ATPase Heads Facilitates Targeting to Chromosomal ParB/parS and Release onto Flanking DNA.Antagonistic interactions of kleisins and DNA with bacterial Condensin MukB.Molecular and genetic analysis of condensin function in vertebrate cells.Mechanics of DNA bridging by bacterial condensin MukBEF in vitro and in singulo.Chromosome condensation in the absence of the non-SMC subunits of MukBEF.MatP regulates the coordinated action of topoisomerase IV and MukBEF in chromosome segregation.Mechanism of cohesin loading onto chromosomes: a conformational dynamics study.Tuned SMC Arms Drive Chromosomal Loading of Prokaryotic Condensin.
P2860
Q24294996-5C570850-F215-46F3-87A8-54BA2071FDA6Q24617958-32F8D679-0AC8-4AB8-8649-BEB273014146Q24791049-E3FC6312-035F-47C3-8C6F-3842BB05BAFEQ24814394-58B4C4EE-F0AA-4DE3-B33C-6A187036BEC2Q27339091-239E928F-281D-4568-AB70-E86CC42394C9Q27659630-D3B4CDE7-ECD0-478C-9406-4E09F9F8554BQ27671838-64E14285-7DBE-44CB-9E30-640D8F4035C8Q27683835-9ECB8AFD-2A29-4645-941F-F852156E0057Q28239071-E40BFF1D-974B-4914-8485-7F2EEF409865Q28769655-E8FF63AA-3865-441D-97C3-E8764E55FB7FQ30554323-9CC5D33B-9FC7-4C40-A4E4-09B3002BB109Q33355284-F8BE80D1-E773-4B1A-AA53-4049504AC0DFQ33883179-7EA36ED0-2294-4A6D-AEBC-9C407C1F989EQ33943503-DDCA8E1F-21BE-4488-8795-FCC59D3B991CQ33959790-66720279-4FB1-459F-991C-A268DC9B5B8CQ33991987-A28C2F43-FE8B-4AE4-AAE2-D50B9F6DFCB3Q34183337-87D1AD7C-F2EF-47F4-B179-4145E737EE79Q34636206-466477F0-7C3C-4DE5-9222-4663A74A2F12Q34976674-8415CC45-FFB8-45F2-8A5B-FE3EB45E38F0Q35037951-1B26A77E-2801-4D91-84E9-F09CC0E99835Q35124756-2202D10C-3D54-41E3-932B-FE34BBB26813Q35133867-5A20E491-FC0E-4529-ADC0-78586BCAF936Q35640052-0FD10970-79B3-4D4E-B239-97088034863AQ35739317-45E3A913-A3BE-4950-AE6C-CD49A0D24D90Q36288410-DCA85377-ADFD-45F3-81A5-D7D4DB6D1818Q36422288-F3E8432F-1942-4EBA-971C-E6621738B79DQ36597246-A9EE172B-0F60-435D-98E1-6FA5339BFB14Q36606820-5DDFEE73-84BF-4B26-8686-90CD8A0723EEQ36833104-248705E8-1044-47AF-8E3C-042EC00BB315Q37321989-864F66F9-16DA-4825-A488-2DCA7C63C2D4Q38151884-A2C3C0F5-494D-46E3-8FA2-BDDA7DADF7B8Q38608524-600BEC24-37F6-4626-BD84-40482A99D28EQ38899514-058DB8CC-7010-447A-A132-C74EA3601098Q39066500-6BB1A722-5F62-4391-995A-CDAE75AC7BB9Q39631412-A84E09EB-87BF-4605-8203-B11BF9EAD1FDQ39790323-43294864-9922-4FF8-8786-0EFEABC18B5FQ41669863-9596ED87-1108-45E4-8A66-DCBF0AB19B86Q41890134-DFF5A76F-474A-4961-944A-A8B33DABC5ECQ42093999-03B4B868-06D8-447D-A7D3-CCB29B8EF925Q42183879-BCA0CE7B-755A-4D31-BD1B-E9AD5C15A7E7
P2860
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@ast
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@en
type
label
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@ast
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@en
prefLabel
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@ast
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@en
P2860
P356
P1433
P1476
Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins.
@en
P2093
Michiko Hirano
Tatsuya Hirano
P2860
P304
P356
10.1038/SJ.EMBOJ.7600264
P407
P577
2004-06-03T00:00:00Z