Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex. - Wikidata - awgldk - TriplyDB

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

http://www.wikidata.org/entity/Q45195721

about

Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for proteolysis.Mechanisms for initiating cellular DNA replication A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin A Structural Basis for the Regulatory Inactivation of DnaA Structural Synergy and Molecular Crosstalk between Bacterial Helicase Loaders and Replication Initiators The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria The G157C mutation in the Escherichia coli sliding clamp specifically affects initiation of replication DnaAcos hyperinitiates by circumventing regulatory pathways that control the frequency of initiation in Escherichia coli.Rapid exchange of bound ADP on the Staphylococcus aureus replication initiation protein DnaA.Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing.The Role of the N-Terminal Domains of Bacterial Initiator DnaA in the Assembly and Regulation of the Bacterial Replication Initiation Complex Regulation of the activity of the dual-function DnaA protein in Caulobacter crescentus.A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli.Functional dissection of YabA, a negative regulator of DNA replication initiation in Bacillus subtilis Hda-mediated inactivation of the DnaA protein and dnaA gene autoregulation act in concert to ensure homeostatic maintenance of the Escherichia coli chromosome.Specific genomic sequences of E. coli promote replicational initiation by directly reactivating ADP-DnaA.Cdt1 revisited: complex and tight regulation during the cell cycle and consequences of deregulation in mammalian cells.Modularity of the bacterial cell cycle enables independent spatial and temporal control of DNA replication Mechanism for the TtDnaA-Tt-oriC cooperative interaction at high temperature and duplex opening at an unusual AT-rich region in Thermoanaerobacter tengcongensis.The rcbA gene product reduces spontaneous and induced chromosome breaks in Escherichia coli.Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA.Regulatory network of the initiation of chromosomal replication in Escherichia coli.Bacteriophage replication modules.Substitutions of Conserved Residues in the C-terminal Region of DnaC Cause Thermolability in Helicase Loading.Reduced lipopolysaccharide phosphorylation in Escherichia coli lowers the elevated ori/ter ratio in seqA mutants The β-sliding clamp directs the localization of HdaA to the replisome in Caulobacter crescentus.Feedback control of DnaA-mediated replication initiation by replisome-associated HdaA protein in Caulobacter.Mutant DnaAs of Escherichia coli that are refractory to negative control.DnaA, ORC, and Cdc6: similarity beyond the domains of life and diversity.Regulating DNA replication in bacteria.DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA.Control of Initiation of DNA Replication in Bacillus subtilis and Escherichia coli.Modes of overinitiation, dnaA gene expression, and inhibition of cell division in a novel cold-sensitive hda mutant of Escherichia coli.Replication Initiation in Bacteria.Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling.Mutations at several loci cause increased expression of ribonucleotide reductase in Escherichia coli Slow unloading leads to DNA-bound β2-sliding clamp accumulation in live Escherichia coli cells The sporulation protein SirA inhibits the binding of DnaA to the origin of replication by contacting a patch of clustered amino acids The primosomal protein DnaD inhibits cooperative DNA binding by the replication initiator DnaA in Bacillus subtilis.DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading.

P2860

Q24304921-CFB351AA-FEF4-44C6-A92F-7B7F4ECBD49E Q26827264-8ACA6A6F-410C-4730-9FC1-35761B272B93 Q27649681-3451E66A-D1DE-4755-B591-2CAC645ECD3D Q27652854-1C446BB3-99CF-4B64-94A9-9D8D979F1405 Q27652911-89CEFD92-8106-4B54-A3EA-5A176BED4C4C Q27658335-D00D31A2-5560-4BDC-B82C-737D410F9410 Q27666492-111EE160-4E6F-441C-ACBB-8B931AADA760 Q33443424-66D40226-31D0-4E93-A84E-A06302B77527 Q33553501-92D9FBD1-83F0-48ED-860D-3D698535BF79 Q33580452-5490973E-8250-4AEE-83B2-76932673EE6B Q33737449-EC6AE096-07AB-465F-9E50-F2382A1085B3 Q34055908-59FB77C3-26BF-4FD5-A5A1-5823373AA72A Q34468299-D6D2528B-BBB3-459E-829B-2B6972982601 Q34478927-EB94DBEA-B53D-4822-AA71-D3A4D4B275DF Q34958905-A4F4DE74-EB0B-4683-A1E1-33D664AD4B13 Q34978255-1057976B-DBCD-48FE-B875-338A96DABD77 Q35107397-54CBE6BD-AEF6-466C-8C98-3D2D9917C6E9 Q35128076-64957902-DC89-4926-879E-C234015A6C80 Q35837356-20E2D95E-B2F1-42FD-949D-8F23A0BE6640 Q35942777-87AB4AF4-101D-4201-871B-673BBBB4BA19 Q36162251-E51C35FB-FE86-4B60-8975-A90A566F2A3F Q36336528-730939F5-7FB4-43DF-8D73-E3C936B9F650 Q36440552-B2E64174-AF41-4294-A440-8B229B0D2868 Q36744600-6DAD8109-710A-4923-8008-273972CE9C18 Q37214505-04525BB2-D9E0-4942-B954-CC3773F32058 Q37332247-6C9A26B9-F0CA-41BC-8DDD-39E2E221E511 Q37333324-6D3593EC-7CF9-4076-A8CA-98E055E54552 Q37528728-AD207EC7-0A71-4FF1-888C-4D168499FD5B Q37687102-3EB2577D-38FD-4DD4-AA7B-5754047FBA40 Q38087526-02297DCC-DF07-4AED-8AED-966D36F25050 Q38673352-DAD7F407-7FD3-4F1C-BA44-29D22D7053F0 Q39079493-B9E97F06-F9F7-40E4-9052-8CD5C5E6B638 Q41340163-6A86AB59-4242-4B7F-B64A-C08E39267837 Q41343446-0A0C616C-9873-4483-8ADE-39CBE3AED94A Q41791841-41D3EFAE-D511-42F2-B866-2E1ECA0EDE71 Q42017043-0C36DFB9-09C2-4605-9DBA-944882A16410 Q42064896-BBA7CBDC-1B4F-49CC-B128-A5812B416E84 Q42091460-90C5F617-2146-416C-B603-C38D00D53688 Q42321823-E70A8D56-B448-48AC-8FA5-099AACF07880 Q42576825-D0A67DDB-0CD9-4311-9C2A-7C6D29623F3E

P2860

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

http://www.wikidata.org/entity/Q45195721

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

name

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@en

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@nl

type

label

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@en

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@nl

prefLabel

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@en

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@nl

P1433

Q45195721-32F5C466-9841-4291-AB98-4F00458D8EB3

P1476

Q45195721-B00A572E-D28D-4E4E-946F-A6B7C8B097ED

P2093

Q45195721-2A4556F0-5159-423B-82F7-D55044924A8F

Q45195721-3BF87F01-F17A-449D-84DC-0669908000F0

Q45195721-66BA0C11-B5F0-4708-83B4-C077F958C822

Q45195721-F28F39C8-A17C-4A51-9197-2978A9496AD8

Q45195721-F4B60C65-C029-4E1C-8146-3FB368FF5EFA

P2860

Q45195721-04EC9013-4864-4C5C-80CB-C00EEE219D9F

Q45195721-07E2C48A-928D-4DA0-8FCE-61E9E2F5B5C1

Q45195721-0940462D-099A-4738-95A6-D897FC2CEABE

Q45195721-0FA54841-ED23-47D1-A273-5E8B8CEA4732

Q45195721-1116E1CA-1ED4-4A82-9AC4-956D3FF74F6F

Q45195721-1D0117A0-EB65-4B56-A61F-528987DF4916

Q45195721-21AFDD78-A478-4B82-A2A1-9764FD90FD4B

Q45195721-22B22F30-B1BB-451E-A76E-CA8AA954D8BC

Q45195721-22E95360-81CD-48FF-866E-6619B8E63804

Q45195721-30BDA726-9712-424F-AB7F-1264CB70A705

P304

Q45195721-5DE57E09-04C7-41A5-9837-AEFF49AFEBA2

P31

Q45195721-C56E53D0-F411-46E8-A424-FFC5D00B224F

P356

Q45195721-0229B128-E246-4789-8E14-55D8D1884DED

P407

Q45195721-57454C67-EF96-4682-9D43-AE6B3D20A848

P433

Q45195721-6A896EDC-8439-4C87-92BB-D923292603EA

P478

Q45195721-B6467596-1FD2-4995-8A80-B5CD79BF3515

P577

Q45195721-10AE13E7-81CA-46CC-A92E-BD264B40009E

P698

Q45195721-ABE9ADCD-E06C-4E42-B18C-AE577FC92A50

P356

P1433

Journal of Biological Chemistry

P1476

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

@en

P2093

Hironori Kawakami

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

Masayuki Su'etsugu

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

Takuma Ishida

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

Toh-Ru Shimuta

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

Tsutomu Katayama

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

P2860

The structures of HsIU and the ATP-dependent protease HsIU-HsIV

Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control

Structure of the AAA ATPase p97

Structure and mechanism of the RuvB Holliday junction branch migration motor

Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III

Structural basis of replication origin recognition by the DnaA protein

Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the -clamp

Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

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

P304

6528-6536

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

P31

scholarly article

P356

10.1074/JBC.M412060200

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

P407

P433

8

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

P478

280

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

P577

2004-12-14T00:00:00Z

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

P698

15611053

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