Structure and hydration of the DNA-human topoisomerase I covalent complex.
about
Rotation of DNA around intact strand in human topoisomerase I implies distinct mechanisms for positive and negative supercoil relaxationReplacement of the human topoisomerase linker domain with the plasmodial counterpart renders the enzyme camptothecin resistantThe open state of human topoisomerase I as probed by molecular dynamics simulationRecovery of the poisoned topoisomerase II for DNA religation: coordinated motion of the cleavage core revealed with the microsecond atomistic simulation.Molecular dynamics simulation of the RNA complex of a double-stranded RNA-binding domain reveals dynamic features of the intermolecular interface and its hydration.The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant.Human topoisomerase I C-terminal domain fragment containing the active site tyrosine is a molten globule: implication for the formation of competent productive complex.Evidence of the crucial role of the linker domain on the catalytic activity of human topoisomerase I by experimental and simulative characterization of the Lys681Ala mutant.Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I.Protein concerted motions in the DNA-human topoisomerase I complex.Role of the linker domain and the 203-214 N-terminal residues in the human topoisomerase I DNA complex dynamics.Molecular dynamics studies on free and bound targets of the bovine papillomavirus type I e2 protein: the protein binding effect on DNA and the recognition mechanism
P2860
Q24814522-B244131D-50BD-4C11-B951-3C7969790C0CQ28534477-58EF2EFF-1B8C-4C0A-8A5C-7D24953C268EQ30361144-A2E99263-B94F-42D1-B51C-F3DDDD0D91E4Q30661486-CDDA5AE6-E720-4B82-823D-15DEBB01595EQ30757350-F98C1701-9B82-4CE4-9A32-C7F40DE50BA2Q35130480-8F7F4278-527F-42BC-A523-BC08AC0CA873Q36012501-3E679A69-E41C-4797-80BF-906B60AD9FDDQ37421089-813D6AD0-9CDF-4872-A93C-83FC4A1B8F3DQ38351710-53D601F0-9980-4EAD-9A7F-D6489FE3FC32Q39733795-C1B663D3-BDB9-4327-A3DA-00B9ECE2E35AQ40308617-2BEB91AE-B1C5-4B99-9C4C-1CD08AA1B83EQ41995001-298DF2E6-51D8-4625-9730-FB9446B25125
P2860
Structure and hydration of the DNA-human topoisomerase I covalent complex.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@ast
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@en
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@nl
type
label
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@ast
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@en
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@nl
prefLabel
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@ast
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@en
Structure and hydration of the DNA-human topoisomerase I covalent complex.
@nl
P2860
P1433
P1476
Structure and hydration of the DNA-human topoisomerase I covalent complex
@en
P2093
Castrignanò T
Desideri A
P2860
P304
P356
10.1016/S0006-3495(01)75716-5
P407
P577
2001-07-01T00:00:00Z