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MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNALesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNACHARMM: the biomolecular simulation programUracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanismsDNA lesion recognition by the bacterial repair enzyme MutMCrystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognitionAtomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylaseStructure of uracil-DNAN-glycosylase (UNG) fromVibrio cholerae: mapping temperature adaptation through structural and mutational analysisAn unprecedented nucleic acid capture mechanism for excision of DNA damageCrystal Structure of Human Methyl-Binding Domain IV Glycosylase Bound to Abasic DNAMolecular dynamics and protein function.Dependence of substrate binding and catalysis on pH, ionic strength, and temperature for thymine DNA glycosylase: Insights into recognition and processing of G·T mispairsClosing the circle: replicating RNA with RNACorrelated Mutation in the Evolution of Catalysis in Uracil DNA Glycosylase SuperfamilyMutational analysis of arginine 276 in the leucine-loop of human uracil-DNA glycosylase.Thymine DNA glycosylase exhibits negligible affinity for nucleobases that it removes from DNAUracil DNA glycosylase: revisiting substrate-assisted catalysis by DNA phosphate anions.Analysis of ice-binding sites in fish type II antifreeze protein by quantum mechanics.Internal proton transfer in the external pyridoxal 5'-phosphate Schiff base in dopa decarboxylase.The substrate binding interface of alkylpurine DNA glycosylase AlkDUnraveling the differences of the hydrolytic activity of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase: a quantum mechanics-molecular mechanics modeling study.Dependence of DNA polymerase replication rate on external forces: a model based on molecular dynamics simulationsRecent advances in the structural mechanisms of DNA glycosylasesThe missing link between thermodynamics and structure in F1-ATPase.Proton transfer facilitated by ligand binding. An energetic analysis of the catalytic mechanism of Trypanosoma cruzi trans-sialidase.Mutations at Arginine 276 transform human uracil-DNA glycosylase into a single-stranded DNA-specific uracil-DNA glycosylase.An oxocarbenium-ion intermediate of a ribozyme reaction indicated by kinetic isotope effectsQM/MM molecular dynamics study of the galactopyranose → galactofuranose reaction catalysed by Trypanosoma cruzi UDP-galactopyranose mutase.Cellular response to DNA damage.Probing enzyme phosphoester interactions by combining mutagenesis and chemical modification of phosphate ester oxygens.Molecular dynamics simulations of the catalytic pathway of a cysteine protease: a combined QM/MM study of human cathepsin K.The DNA glycosylase AlkD uses a non-base-flipping mechanism to excise bulky lesions.Nanorod-Shaped Basic Al2O3 Catalyzed N,N-Diformylation of Bisuracil Derivatives: A Greener "NOSE" Approach.Free energy study of the catalytic mechanism of Trypanosoma cruzi trans-sialidase. From the Michaelis complex to the covalent intermediate.DNA conformations in mismatch repair probed in solution by X-ray scattering from gold nanocrystals.A Catalytic Role for C-H/π Interactions in Base Excision Repair by Bacillus cereus DNA Glycosylase AlkD.Depurination of N7-methylguanine by DNA glycosylase AlkD is dependent on the DNA backbone.Role of two strictly conserved residues in nucleotide flipping and N-glycosylic bond cleavage by human thymine DNA glycosylase.Divergent mechanisms for enzymatic excision of 5-formylcytosine and 5-carboxylcytosine from DNA.Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes.
P2860
Q21131242-DD228116-FDB3-4E9A-85C4-5D1481A180E5Q24319667-FE6AB0B9-58DD-4A7B-8E5E-0FA50C4DB7FAQ24658108-686E9AF0-8091-4A1D-9221-EC5EE8428DB0Q24672089-C8F04F45-AE90-4FE8-BFBE-AB5C8EE3DCC5Q27642268-8167FB99-DEAB-4DAF-B2D9-148958811D3EQ27650995-745BFC37-D0AD-4FDD-968B-8FA785818685Q27657850-89A7379F-0802-4915-9627-1CD4B8802544Q27659441-63315490-A189-4827-A3B7-7DB374997D6AQ27664934-F88458E2-7A1A-43E5-B971-E168AD943C8DQ27678915-FB572A23-EF8B-4CA3-9E69-AC24DADB670BQ28248486-2170F27B-7FE7-4F4C-AD76-F03BE5E1046AQ28740645-1967F008-7802-4672-8B89-F8D14416E314Q28749191-C7C564F3-3789-4516-AD4E-AE00E0170AEBQ30400981-343E4775-B562-414D-BF68-40BE6E850A60Q30840154-FB9668B5-5F10-4863-94FA-D52FF68454D8Q30992958-0D23A96F-C3B3-4BD3-953D-1E4C0A497BA6Q31164951-AE755D44-A5A6-4204-97B2-633D34E94219Q33184654-9F4DE266-8364-40C6-8704-8EBB72AB758EQ33685234-62543D2F-1602-4F17-86B1-14357615C1EBQ33688806-D16462EF-97FE-4E39-BB7F-2431FA2A22B8Q33732570-ED952351-952E-42B2-B268-05A454D8E44DQ34186979-DBBA6F3E-34C5-423B-B435-2F239B87A34CQ34306735-17B361FE-0119-48D8-AC4D-A738023CCCB4Q34327927-B32B9A13-BE49-42FB-BBB6-C5D8795362A0Q34550867-E42FE4EA-67A3-4D9A-AA39-F8A5FBFDBE11Q34577780-243F4BB1-0CDC-4712-9E07-DB9EC3BC6458Q34787673-CCAE25FD-431F-4203-87CD-4B8F08D83D8AQ35315473-6DB69190-1B91-4519-A2DB-C8E1C460367CQ36420091-58017AFE-D918-4DE8-98A7-73B3F1B39BACQ36559673-E8730AAD-49C3-458C-A568-A6EF20668461Q36915183-F7021A1A-2DAB-4401-BAC4-826DF2827774Q36977957-0F89FB42-8792-4D09-9E42-3CC5C4787F84Q37156839-55BC1308-6860-4E0D-AAD9-26A9FA8E2F23Q37189253-CF76DA4C-4D70-428F-B401-472A882DDC4EQ37256043-4CE20C3B-F16F-4FB7-84E7-B760BF410C35Q37279194-FBC37900-127A-4632-A18A-A17CB9B7979CQ37367743-B562A73D-E66B-4F5E-A924-A1B5F7E6F3F6Q37479458-221A3C25-046B-4CB1-996B-4BAE3F65112DQ37595036-2D50C4DF-3102-4E39-AF31-FC1D1FB22FBDQ37876374-40899B47-37C5-421E-AE3A-CC620E1840A0
P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին 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
Uracil-DNA glycosylase acts by substrate autocatalysis
@ast
Uracil-DNA glycosylase acts by substrate autocatalysis
@en
Uracil-DNA glycosylase acts by substrate autocatalysis
@nl
type
label
Uracil-DNA glycosylase acts by substrate autocatalysis
@ast
Uracil-DNA glycosylase acts by substrate autocatalysis
@en
Uracil-DNA glycosylase acts by substrate autocatalysis
@nl
prefLabel
Uracil-DNA glycosylase acts by substrate autocatalysis
@ast
Uracil-DNA glycosylase acts by substrate autocatalysis
@en
Uracil-DNA glycosylase acts by substrate autocatalysis
@nl
P2860
P356
P1433
P1476
Uracil-DNA glycosylase acts by substrate autocatalysis
@en
P2093
A R Dinner
G M Blackburn
P2860
P2888
P356
10.1038/35099587
P407
P577
2001-10-18T00:00:00Z
P5875
P6179
1052212789