Követés
Saulius Klimašauskas
Saulius Klimašauskas
Institute of Biotechnology, Life Sciences Center, Vilnius University
E-mail megerősítve itt: ibt.lt - Kezdőlap
Cím
Hivatkozott rá
Hivatkozott rá
Év
Hhal methyltransferase flips its target base out of the DNA helix
S Klimasauskas, S Kumar, RJ Roberts, X Cheng
Cell 76 (2), 357-369, 1994
12911994
The DNA (cytosine-5) methyltransferases
S Kumar, X Cheng, S Klimasauskas, S Mi, J Posfai, RJ Roberts, ...
Nucleic acids research 22 (1), 1, 1994
5761994
5-hmC in the brain is abundant in synaptic genes and shows differences at the exon-intron boundary
T Khare, S Pai, K Koncevicius, M Pal, E Kriukiene, Z Liutkeviciute, M Irimia, ...
Nature structural & molecular biology 19 (10), 1037-1043, 2012
3082012
2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases
B Holz, E Weinhold, S Klimasauskas, S Serva
Nucleic acids research 26 (4), 1076-1083, 1998
2851998
Direct transfer of extended groups from synthetic cofactors by DNA methyltransferases
C Dalhoff, G Lukinavičius, S Klimas̆auskas, E Weinhold
Nature chemical biology 2 (1), 31-32, 2006
2652006
Processive methylation of hemimethylated CpG sites by mouse Dnmt1 DNA methyltransferase
G Vilkaitis, I Suetake, S Klimašauskas, S Tajima
Journal of Biological Chemistry 280 (1), 64-72, 2005
2532005
Enzymatic C5-cytosine methylation of DNA: mechanistic implications of new crystal structures forHhaI methyltransferase-DNA-AdoHcy complexes
M O'Gara, S Klimaŝauskas, RJ Roberts, X Cheng
Journal of molecular biology 261 (5), 634-645, 1996
2211996
A new tool for biotechnology: AdoMet-dependent methyltransferases
S Klimašauskas, E Weinhold
Trends in biotechnology 25 (3), 99-104, 2007
1942007
MHhal binds tightly to substrates containing mismatches at the target base
S Klimašauskas, RJ Roberts
Nucleic acids research 23 (8), 1388-1395, 1995
1931995
Sequence motifs characteristic of DNA [cytosine-N4] methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases
S Klimasauskas, A Timinskas, M Saulius, D Butkiene, V Butkus, ...
Nucleic acids research 17 (23), 9823-9832, 1989
1851989
Cytosine-5-methyltransferases add aldehydes to DNA
Z Liutkevičiūtė, G Lukinavičius, V Masevičius, D Daujotytė, ...
Nature chemical biology 5 (6), 400-402, 2009
1822009
Targeted labeling of DNA by methyltransferase-directed transfer of activated groups (mTAG)
G Lukinavičius, V Lapienė, Z Staševskij, C Dalhoff, E Weinhold, ...
Journal of the American Chemical Society 129 (10), 2758-2759, 2007
1622007
An adversarial DNA N6-methyladenine-sensor network preserves polycomb silencing
SM Kweon, Y Chen, E Moon, K Kvederaviciutė, S Klimasauskas, ...
Molecular cell 74 (6), 1138-1147. e6, 2019
1482019
Dynamic modes of the flipped‐out cytosine during HhaI methyltransferase–DNA interactions in solution
S Klimašauskas, T Szyperski, S Serva, K Wüthrich
The EMBO journal, 1998
1441998
The mechanism of DNA cytosine-5 methylation: Kinetic and mutational dissection of HhaI methyltransferase
G Vilkaitis, S Serva, E Weinhold, S Klimašauskas
Journal of Biological Chemistry 276 (24), 20924-20934, 2001
1412001
Cytosine modification in DNA by BcnI methylase yields N4-methylcytosine
A Janulaitis, S Klimasauskas, M Petrusyte, V Butkus
FEBS Lett 161 (1), 131-134, 1983
1401983
Enhanced chemical stability of AdoMet analogues for improved methyltransferase-directed labeling of DNA
G Lukinavičius, M Tomkuvienė, V Masevičius, S Klimašauskas
ACS chemical biology 8 (6), 1134-1139, 2013
1252013
DNA fluorocode: A single molecule, optical map of DNA with nanometre resolution
RK Neely, P Dedecker, J Hotta, G Urbanavičiūtė, S Klimašauskas, ...
Chemical science 1 (4), 453-460, 2010
1192010
Synthesis of S-adenosyl-L-methionine analogs and their use for sequence-specific transalkylation of DNA by methyltransferases
C Dalhoff, G Lukinavičius, S Klimašauskas, E Weinhold
Nature protocols 1 (4), 1879-1886, 2006
1152006
Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in M. HhaI–DNA complexes
RK Neely, D Daujotyte, S Grazulis, SW Magennis, DTF Dryden, ...
Nucleic Acids Research 33 (22), 6953-6960, 2005
1132005
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