M.HhaI binds tightly to substrates containing mismatches at the target base.
about
2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferasesDnmt2 is not required for de novo and maintenance methylation of viral DNA in embryonic stem cellsType I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)Probing a rate-limiting step by mutational perturbation of AdoMet binding in the HhaI methyltransferaseZebularine: A Novel DNA Methylation Inhibitor that Forms a Covalent Complex with DNA MethyltransferasesThe SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helixA dual flip-out mechanism for 5mC recognition by the Arabidopsis SUVH5 SRA domain and its impact on DNA methylation and H3K9 dimethylation in vivoDNA containing 4'-thio-2'-deoxycytidine inhibits methylation by HhaI methyltransferaseStructures of HhaI methyltransferase complexed with substrates containing mismatches at the target baseRecognition of nonhybridizing base pairs during nucleotide excision repair of DNAProbing the MVAI methyltransferase region that interacts with DNA: affinity labeling with the dialdehyde-containing DNA duplexes.Examination of the DNA substrate selectivity of DNA cytosine methyltransferases using mass tagging.A higher degree of expression of DNA methyl transferase 1 in cervical cancer is associated with poor survival outcome.AdoMet-dependent methylation, DNA methyltransferases and base flipping.Molecular and enzymatic profiles of mammalian DNA methyltransferases: structures and targets for drugs.Folate deficiency exacerbates apoptosis by inducing hypomethylation and resultant overexpression of DR4 together with altering DNMTs in Alzheimer's disease.Protein-facilitated base flipping in DNA by cytosine-5-methyltransferase.Inhibition of (cytosine C5)-methyltransferase by oligonucleotides containing flexible (cyclopentane) and conformationally constrained (bicyclo[3.1.0]hexane) abasic sites.Binding of nucleoid-associated protein fis to DNA is regulated by DNA breathing dynamics.Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA methyltransferases.Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites.A prediction of the amino acids and structures involved in DNA recognition by type I DNA restriction and modification enzymes.Interaction of the phage T4 Dam DNA-[N6-adenine] methyltransferase with oligonucleotides containing native or modified (defective) recognition sites.HhaI and HpaII DNA methyltransferases bind DNA mismatches, methylate uracil and block DNA repair.Chemical mapping of cytosines enzymatically flipped out of the DNA helix.A mutant HpaII methyltransferase functions as a mutator enzyme.Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression.The Vsr endonuclease of Escherichia coli: an efficient DNA repair enzyme and a potent mutagen.Relationships between p14ARF Gene Methylation and Clinicopathological Features of Colorectal Cancer: A Meta-Analysis.Transducing methyltransferase activity into electrical signals in a carbon nanotube-DNA device().Mandatory fortification with folic acid in the United States is associated with increased expression of DNA methyltransferase-1 in the cervixSelective recognition of pyrimidine-pyrimidine DNA mismatches by distance-constrained macrocyclic bis-intercalatorsROS1 5-methylcytosine DNA glycosylase is a slow-turnover catalyst that initiates DNA demethylation in a distributive fashion.Caught in the act: visualization of an intermediate in the DNA base-flipping pathway induced by HhaI methyltransferaseSymmetry elements in DNA structure important for recognition/methylation by DNA [amino]-methyltransferases.DNA methyltransferases: mechanistic models derived from kinetic analysis.The mechanism of DNA cytosine-5 methylation. Kinetic and mutational dissection of Hhai methyltransferase.Probing murine methyltransfease Dnmt3a interactions with benzo[a]pyrene-modified DNA by fluorescence methodsIdentification of the binding site for the extrahelical target base in N6-adenine DNA methyltransferases by photo-cross-linking with duplex oligodeoxyribonucleotides containing 5-iodouracil at the target position.Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of dam methyltransferase.
P2860
Q24546328-3EB8CA5B-694F-4505-9557-021934FCB019Q24548031-955581FB-0413-49C1-8D9A-C8578F7CA7FAQ24548508-4BFA04D1-1701-4EA8-93CD-9CD1FA75A50CQ24794135-9E978544-8742-49F0-B647-6583C30E7E8FQ27639568-F76C64D3-BF73-4387-9A0E-507CB4A1978FQ27651993-79112471-7816-45BB-9DA0-28A3126E6263Q27666611-C70A916E-C895-4D21-9C40-97AF71B0FDFEQ27739981-7170DF4F-CEA2-458D-BDF6-CCA649E246FFQ27765722-0F965DDD-F3F0-4F35-91DB-34674AF271CDQ30639682-D1179C80-2C2C-473E-B0C0-E0E3873CE430Q31996897-5648CB5A-3430-428B-8DDE-7F6C057ADAD2Q33786726-35858BB2-AFB2-40C9-A0EF-48EE0E34A0F0Q33812527-36878B7A-9187-473B-AB3A-544656AE5B56Q33941847-E1A87A9B-7788-4009-A8AA-AC0D4D6C6C01Q34143019-CAC9B584-074C-4C12-8240-34F76273893CQ34166998-FA6D5234-53BD-470C-BCD7-874E1C5A8E63Q34167650-883C4562-CE89-474B-AD9B-FEBA9F7654BBQ34373551-F3545816-5577-4826-894B-34A9BC64F5D9Q34558005-6A0DAF5E-9D3E-4917-9835-1EA54ECC2C52Q34587622-9B1D0397-4B18-412A-A958-9BD43CE3B1FCQ34626537-F8722780-F9D7-4583-ADAE-BBA235D38865Q34634843-A261E6EC-0CF3-41C0-9D7F-CBE4A7290010Q34641294-55CEE077-A539-4731-AEA3-3A1B4794AAF0Q34746885-D71B83C1-41DD-43DE-8441-896C5A2E1D5FQ34775305-44ABDE70-E92A-4740-A9E9-5505D699D856Q34778092-B87FC8B7-D477-41E6-A89F-9A3E1E7693FAQ35562083-E4F43AC6-2FB9-46CB-8EE9-A0FFB6152918Q35630875-A770680C-9BD2-4F7C-A6B2-D4EECB88AF72Q35964783-FAF94B9D-099C-45C2-AAAA-F25F13B7B9F3Q36101705-01ECD049-CB16-47E9-B403-41F29268206BQ36408244-00F3CD54-0054-4035-AB2C-C7260D653467Q36859253-0365C3EB-27A4-409A-BBD8-A32729B5DEC7Q37273644-D8B2AA50-6607-41D8-A421-DF87199193F8Q37346182-CAF9934E-E83F-443F-A4FE-65E649511A2BQ37346268-5214BA5F-63BE-446C-8CB3-C4FBB9192556Q37977119-6478C0C7-6F13-47AD-A3D3-6D207B178E2CQ38302392-3CC9A520-AACF-46E4-81BC-F36CDED6A145Q38322396-47C06D86-E795-4C78-AA24-245CED0194D3Q38324707-4B095391-FEFF-4D5C-AF66-61C6CB0E205BQ38326532-5999505D-EF2A-43AF-8D26-27313DD8F02B
P2860
M.HhaI binds tightly to substrates containing mismatches at the target base.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
M.HhaI binds tightly to substrates containing mismatches at the target base.
@en
type
label
M.HhaI binds tightly to substrates containing mismatches at the target base.
@en
prefLabel
M.HhaI binds tightly to substrates containing mismatches at the target base.
@en
P2860
P356
P1476
M.HhaI binds tightly to substrates containing mismatches at the target base.
@en
P2860
P304
P356
10.1093/NAR/23.8.1388
P577
1995-04-01T00:00:00Z