Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step. - Wikidata - wikimedia - TriplyDB

Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step.

Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step.

http://www.wikidata.org/entity/Q27936414

about

Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2-7 Helicase to Reveal Essential Features of Structure and Function Mechanisms for initiating cellular DNA replication The Mcm2-7 replicative helicase: a promising chemotherapeutic target MCM ring hexamerization is a prerequisite for DNA-binding.Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain A conserved MCM single-stranded DNA binding element is essential for replication initiation An Mcm10 Mutant Defective in ssDNA Binding Shows Defects in DNA Replication Initiation Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex.The structural basis for MCM2-7 helicase activation by GINS and Cdc45.The Dbf4-Cdc7 kinase promotes Mcm2-7 ring opening to allow for single-stranded DNA extrusion and helicase assembly.ATP-dependent conformational dynamics underlie the functional asymmetry of the replicative helicase from a minimalist eukaryote Mutation of the zebrafish nucleoporin elys sensitizes tissue progenitors to replication stress.The effects of oligomerization on Saccharomyces cerevisiae Mcm4/6/7 function Phosphorylation of Mcm2 modulates Mcm2-7 activity and affects the cell's response to DNA damage A unique DNA entry gate serves for regulated loading of the eukaryotic replicative helicase MCM2-7 onto DNA The Saccharomyces cerevisiae Mcm6/2 and Mcm5/3 ATPase active sites contribute to the function of the putative Mcm2-7 'gate'.Geminin inhibits a late step in the formation of human pre-replicative complexes.The mini-chromosome maintenance (Mcm) complexes interact with DNA polymerase α-primase and stimulate its ability to synthesize RNA primers Cdc45 (cell division cycle protein 45) guards the gate of the Eukaryote Replisome helicase stabilizing leading strand engagement.DNA binding polarity, dimerization, and ATPase ring remodeling in the CMG helicase of the eukaryotic replisome.Analysis of the crystal structure of an active MCM hexamer A Checkpoint-Related Function of the MCM Replicative Helicase Is Required to Avert Accumulation of RNA:DNA Hybrids during S-phase and Ensuing DSBs during G2/M The Sulfolobus solfataricus GINS Complex Stimulates DNA Binding and Processive DNA Unwinding by Minichromosome Maintenance Helicase Immunoexpression of Ki-67, MCM2, and MCM3 in Ameloblastoma and Ameloblastic Carcinoma and Their Correlations with Clinical and Histopathological Patterns Functional conservation of beta-hairpin DNA binding domains in the Mcm protein of Methanobacterium thermoautotrophicum and the Mcm5 protein of Saccharomyces cerevisiae.Cryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA.On helicases and other motor proteins.Ciprofloxacin is an inhibitor of the Mcm2-7 replicative helicase.Molecular architecture of the recombinant human MCM2-7 helicase in complex with nucleotides and DNA.The Mcm complex: unwinding the mechanism of a replicative helicase.ATP binding and hydrolysis by Mcm2 regulate DNA binding by Mcm complexes.Hrq1, a homolog of the human RecQ4 helicase, acts catalytically and structurally to promote genome integrity.Structural biology of MCM helicases.G364R mutation of MCM4 detected in human skin cancer cells affects DNA helicase activity of MCM4/6/7 complex.From structure to mechanism-understanding initiation of DNA replication.Subunit organization of Mcm2-7 and the unequal role of active sites in ATP hydrolysis and viability.Functional conservation of the pre-sensor one beta-finger hairpin (PS1-hp) structures in mini-chromosome maintenance proteins of Saccharomyces cerevisiae and archaea Opening the gate to DNA replication MCM2-regulated functional networks in lung cancer by multi-dimensional proteomic approach.Mcm subunits can assemble into two different active unwinding complexes.

P2860

0c1c88f755b8d49d7563e3325fc1f913e3dc3989 28f61fd46e44df36cf7bf717ff1c4777cbae700f 5a77af434652e50ce051d50672ff898495b166b4 5b3e109ecd34954bda5f94d87561df9880b92734 a37783f5f273b8d7f23b7d5ad6ad178568a2b118 a758970e7dc84f07d536464fef0083b71bfecd3c d4d915e7798ed391481d139942ad89af10cfdba4 dd892b3e2e96deac5bbb2fbf6721e53f0b3c8155

P248

Q26779724-EFE5238F-3D43-4D9C-8804-7E41A0223593 Q26827264-668EE657-CE11-4E05-8FA5-FBC46A92822C Q26861045-5B3A3428-EF2C-4142-B3B9-95BB6FA70A78 Q27324366-744F1C25-9435-41C4-A239-897A83D50C03 Q27650348-A1CD64AE-56B1-4508-977E-72BA70FD229A Q27682741-FF018785-1652-4686-B0C6-8A75A30909CA Q28114327-03D5D55C-6BFE-4189-BF59-7D0105B8F31F Q28281309-89439742-B6F7-4F77-B205-72A31D2AE808 Q28306649-DA4CCE49-62DA-457A-9595-4E185B39F53A Q29976890-AED2559D-25CD-44D4-9C74-9C9C4724D870 Q30523929-8A7E526F-25EA-40B8-B433-AF6FA58C9048 Q33381633-C5A80EEC-B44F-4823-A4B6-A96C69520740 Q33699332-6CDA77F1-6A80-4D94-8BF1-0D7755DC53FB Q33906513-3DFCFB27-F0CB-49A4-A9A4-8A67DFA91C55 Q33984498-11D58821-E453-4944-A16D-DBCF7DDDBE6C Q34189297-7C464573-8984-4F3E-A10C-75CBDFAAEC29 Q34431115-CCE0828F-9410-4F69-9412-6486D3E6D356 Q34973846-F2CDF9A7-E787-4467-97A7-5E9BC16807CF Q35031537-7DC5CC00-48A8-49AE-9C6E-69145FB8C922 Q35176517-4D1D858A-51A9-4A54-93B8-34ADE7188454 Q35176524-31E9CF31-CAFD-47BC-89FF-C78D2527E3B6 Q36111269-7DB8E7F7-8F5F-42F8-A7E0-2B65693BBB9A Q36207981-854CE6A2-4080-4929-9715-6F2465D8AEFF Q36448578-D821B652-22C5-427C-85E7-F2ACF755435F Q36836963-4DE34860-AAE4-4F09-AA46-AFBEB8A0CF6B Q37076181-2F2D6095-FEA2-40F7-9D23-EA5D65B835A2 Q37105913-BC202FFF-A108-4280-ABCE-57773DBF92AF Q37218789-376CAF17-0411-4D60-BE0F-CD27D0066BE8 Q37262903-CB491BCC-616A-428D-82B5-E57186C6ACAD Q37451513-E68D5723-7512-4F5B-886A-7BA2AE5AC422 Q37500135-D8473E86-3ECD-4CB0-A348-25725CF28774 Q37600384-8CA6B773-3137-448A-BF65-3E9C166BA823 Q37603329-C56A2A94-C76F-42EA-BD73-D51ABC2AF8C5 Q38911821-BF7C27FB-0B63-49DE-B8E3-FEB83EA77C85 Q39440326-7F3F0773-05BF-4633-AC91-622BE6E09F68 Q41881445-A8A1EE13-D905-415B-9973-36E5FB51F508 Q42150265-DB3930A8-A43A-4AA6-B10A-69470BE116B3 Q42272850-9E2DF512-001E-49CF-83E0-6FF43B9E80AD Q42378823-1F6BF6F8-B1C1-40A1-9911-1AAE7CAEA092 Q43154731-C32FCA75-6223-4F46-BB37-53B86C3B1601

P2860

Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step.

http://www.wikidata.org/entity/Q27936414

description

2007 nî lūn-bûn

@nan

2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

Differences in the single-stra ...... ine a slow ATP-dependent step.

@ast

Differences in the single-stra ...... ine a slow ATP-dependent step.

@en

Differences in the single-stra ...... ine a slow ATP-dependent step.

@nl

type

label

Differences in the single-stra ...... ine a slow ATP-dependent step.

@ast

Differences in the single-stra ...... ine a slow ATP-dependent step.

@en

Differences in the single-stra ...... ine a slow ATP-dependent step.

@nl

prefLabel

Differences in the single-stra ...... ine a slow ATP-dependent step.

@ast

Differences in the single-stra ...... ine a slow ATP-dependent step.

@en

Differences in the single-stra ...... ine a slow ATP-dependent step.

@nl

P1433

Q27936414-9916E507-11AA-4A7C-A064-D0C194FF5485

P1476

Q27936414-4CC38579-0444-4904-AB3A-A511E1386802

P2093

Q27936414-994785F9-AAE0-4D3A-AD6F-B6A039FB9D07

P2860

Q27936414-05278126-50A0-40AC-A3B9-FCC836D9DF02

Q27936414-0F622FB2-0430-43F5-ABE9-F6AFD4347696

Q27936414-13C1DFF2-679D-411F-84EA-45407CD9CA40

Q27936414-18069CE2-28A6-4D33-BDEB-AE449FBA64B2

Q27936414-19126F45-951A-4837-B14B-03CCED8D4003

Q27936414-1B123E0E-1067-4742-908B-B57CEFECAFDC

Q27936414-1BB3CC8E-8912-40C2-8EA6-377FCD12E395

Q27936414-1CFA82E9-625D-4257-B093-1D891297BBE5

Q27936414-1DDF52E0-C462-40BB-BBD3-E033113DB65D

Q27936414-1F08CA34-AE39-4583-AC1C-5DA8D2EA52E0

P304

Q27936414-83AE6BD3-251A-43C9-97C3-3F8520DE2D9E

P31

Q27936414-C58FEEBB-C380-4D91-BE4D-5C5A366AA925

P3181

Q27936414-98058306-123C-462F-8EB6-0B44AC25CE33

P356

Q27936414-6F6E547D-7274-4E4A-BACD-5FF19B088097

P407

Q27936414-3014ACA3-BD75-43FA-B24A-05A9B7945787

P433

Q27936414-E60F8138-F80F-4E46-8DF0-4DDC8F6F85C9

P478

Q27936414-9CD4A83B-A25D-450E-99F5-94CF359ED998

P50

Q27936414-D73438E8-2489-40EA-8D66-24F61B6431AA

P577

Q27936414-ADD7CF5F-B0CA-44DD-ADE2-0A455A1FE07D

P5875

Q27936414-2CB1C4B7-DC27-484B-BE29-232B02F45DD5

P698

Q27936414-CE59ECEB-D4CD-4B26-8018-501A6FAE25D4

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Differences in the single-stra ...... fine a slow ATP-dependent step

@en

P2093

Anthony Schwacha

http://www.w3.org/2001/XMLSchema#string

P2860

A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex

Binding of human minichromosome maintenance proteins with histone H3

Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures

Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity

A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication

mcm5/cdc46-bob1 bypasses the requirement for the S phase activator Cdc7p

DNA binding and helicase actions of mouse MCM4/6/7 helicase.

The structure and function of MCM from archaeal M. Thermoautotrophicum

Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture.

Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex.

P304

33795-33804

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

3913942

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.M703824200

http://www.w3.org/2001/XMLSchema#string

P407

P433

46

http://www.w3.org/2001/XMLSchema#string

P478

282

http://www.w3.org/2001/XMLSchema#string

P50

Matthew L Bochman

P577

2007-09-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

5949899

http://www.w3.org/2001/XMLSchema#string

P698

17895243

http://www.w3.org/2001/XMLSchema#string