about
The DNA (cytosine-5) methyltransferasesAlw26I, Eco31I and Esp3I--type IIs methyltransferases modifying cytosine and adenine in complementary strands of the target DNAProbing a rate-limiting step by mutational perturbation of AdoMet binding in the HhaI methyltransferaseTime-resolved fluorescence of 2-aminopurine as a probe of base flipping in M.HhaI-DNA complexesFunctional roles of the conserved threonine 250 in the target recognition domain of HhaI DNA methyltransferaseHhaI methyltransferase flips its target base out of the DNA helixEnzymatic C5-cytosine methylation of DNA: mechanistic implications of new crystal structures for HhaL methyltransferase-DNA-AdoHcy complexesSequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylasesCircular permutation of DNA cytosine-N4 methyltransferases: in vivo coexistence in the BcnI system and in vitro probing by hybrid formationKinetic and functional analysis of the small RNA methyltransferase HEN1: the catalytic domain is essential for preferential modification of duplex RNATandem virtual screening targeting the SRA domain of UHRF1 identifies a novel chemical tool modulating DNA methylation.5-hmC in the brain is abundant in synaptic genes and shows differences at the exon-intron boundary5-Hydroxymethylcytosine--the elusive epigenetic mark in mammalian DNA.Engineering the DNA cytosine-5 methyltransferase reaction for sequence-specific labeling of DNAApproaches for studying microRNA and small interfering RNA methylation in vitro and in vivo.Synthesis of S-Adenosyl-L-Methionine Analogs with Extended Transferable Groups for Methyltransferase-Directed Labeling of DNA and RNA.A basal promoter element recognized by free RNA polymerase sigma subunit determines promoter recognition by RNA polymerase holoenzyme.Lineage-specific variations in the trigger loop modulate RNA proofreading by bacterial RNA polymerases.DNA Labeling Using DNA Methyltransferases.Chemical display of thymine residues flipped out by DNA methyltransferasesArchaeal fibrillarin-Nop5 heterodimer 2'-O-methylates RNA independently of the C/D guide RNP particle.Cleavage of methylated CCCGGG sequences containing either N4-methylcytosine or 5-methylcytosine with MspI, HpaII, SmaI, XmaI and Cfr9I restriction endonucleases.Synthesis and physical characterization of DNA fragments containing N4-methylcytosine and 5-methylcytosineM.HhaI binds tightly to substrates containing mismatches at the target base.The sequence specificity domain of cytosine-C5 methylases.Functional mapping of the plant small RNA methyltransferase: HEN1 physically interacts with HYL1 and DICER-LIKE 1 proteins.A directed evolution design of a GCG-specific DNA hemimethylase.Direct observation of cytosine flipping and covalent catalysis in a DNA methyltransferase.Recognition of guanosine by dissimilar tRNA methyltransferases.Dynamic modes of the flipped-out cytosine during HhaI methyltransferase-DNA interactions in solution.Solubility engineering of the HhaI methyltransferase.Enhanced chemical stability of adomet analogues for improved methyltransferase-directed labeling of DNA.HhaI DNA methyltransferase uses the protruding Gln237 for active flipping of its target cytosine.Cytosine-5-methyltransferases add aldehydes to DNA.Analysis of products of DNA modification by methylases: a procedure for the determination of 5- and N4-methylcytosines in DNA.Tethered Oligonucleotide-Primed Sequencing, TOP-Seq: A High-Resolution Economical Approach for DNA Epigenome Profiling.Phenotyping cognitive impairment in dialysis patients: insights from experimental mouse models.Biosynthetic selenoproteins with genetically-encoded photocaged selenocysteines.Excision of the doubly methylated base N4,5-dimethylcytosine from DNA by Escherichia coli Nei and Fpg proteins.Direct decarboxylation of 5-carboxylcytosine by DNA C5-methyltransferases.
P50
Q24614934-84C8ECB7-6BC8-46C1-92EF-036C7578B5F9Q24629662-DD679659-6D70-41FD-BB6B-E60CFAFF86F7Q24794135-9401C78F-F4EF-40DD-8F23-13E1BC865485Q24810605-98CAB140-C37B-4E66-83E4-103BC30134DFQ27628771-8E732724-53C6-4FB5-AB79-EAAEB1AEC3A7Q27731553-FE5206C7-B376-4F06-826D-9467F7665A63Q27733356-E119EF8F-7A56-446D-AEE9-780E451665E0Q28273541-AA63DC0B-4306-47E5-BB99-34B63E856943Q33600868-AA8A4BD9-6E49-47E6-B1B4-DB078FA5EC81Q34135176-A1C2797E-D756-4773-A731-2A6D5B08217FQ35980762-6DC55B6E-A6DA-4AD0-9301-891C2C724538Q36300979-FF72CDC1-EAEC-49C0-971A-94D18E366C51Q36306335-597A444D-5075-45F0-937D-4F9F78BA3768Q36478079-3EA46B66-4165-4B27-A6C6-DCA7A4A58297Q36615909-16A7DCFD-17FF-4796-82CB-08AA2DFFD405Q36676947-73CD690E-B2E5-4EA5-AC59-4C5B6622C119Q38312071-A1F5C18B-E417-4DB8-BC4C-BD3B378D8B8AQ38530942-F3FEA022-992F-4494-A7D0-04F465EEFBC2Q39003564-5AAF97AD-D4CC-4EB1-9E11-76147A6A898DQ39724595-51D7C31F-EB01-47AA-ADB9-CA0B70AB40E7Q40174680-FBCA7A17-E649-4505-BC61-A2FB22358DEAQ40390163-FBE0FEF2-1669-4229-89F3-DC54AF38160CQ40391134-FE38E756-0749-4708-82C2-1EDED9B3CDC8Q40393755-D7385B66-09DC-4CC0-87DF-A1D7E3EEF409Q40508616-201ECAB9-4E18-44FA-ADC3-9635A09DA255Q41437610-569409CC-6209-4B22-9DB5-8880C04ACBB6Q41958418-B0AF5439-8547-4425-9FE4-BA8BFAC3A0DEQ42105782-123E6D4F-A465-4675-A194-67CEE37EE440Q42288537-EDBCFA8F-4FC1-432D-BAEC-316D786354F3Q42636190-CAEB7019-6E67-4D34-B5D4-07771B946809Q44433446-430593E0-86FD-4649-8FA0-E0D02035453DQ44796487-BA444BEE-073F-4D07-9AA3-BC61323FD1E1Q44993894-2666B750-1BCE-499F-ADB5-7221CC98096DQ46017177-1368AA1D-1005-45A4-811C-9191BCDBC534Q46384083-12D0BCE7-9C03-4F44-9EB0-E3097B20A832Q48002910-DBA38286-05A2-4E4D-BFE7-DD426C397C6FQ48148167-CDE616B3-1F2E-4C1F-A517-A11F66AD2985Q50439599-3B27DFBA-DE75-4C20-83EA-DD8D2E889BBDQ52568727-305F0169-1CA3-4A1F-A8BF-A2C18F31022CQ53058810-95C688EC-7776-4DA1-8827-629CD297D1C9
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Saulius Klimasauskas
@ast
Saulius Klimasauskas
@en
Saulius Klimasauskas
@es
Saulius Klimasauskas
@nl
Saulius Klimasauskas
@sl
type
label
Saulius Klimasauskas
@ast
Saulius Klimasauskas
@en
Saulius Klimasauskas
@es
Saulius Klimasauskas
@nl
Saulius Klimasauskas
@sl
altLabel
Klimasauskas
@en
Klimašauskas
@en
prefLabel
Saulius Klimasauskas
@ast
Saulius Klimasauskas
@en
Saulius Klimasauskas
@es
Saulius Klimasauskas
@nl
Saulius Klimasauskas
@sl
P1053
M-3053-2016
P106
P21
P31
P3829
P496
0000-0002-1395-2030
P569
2000-01-01T00:00:00Z