science
plus
.abes.fr
|
explorer
À propos de :
Jeltsch Albert
Goto
Sponge
NotDistinct
Permalink
An Entity of Type :
foaf:Person
, within Data Space :
scienceplus.abes.fr
associated with source
document(s)
Type:
Person
New Facet based on Instances of this Class
Attributs
Valeurs
type
Person
name
Jeltsch Albert
personal mailbox
a.jeltsch@iu-bremen.de
a.jeltsch@jacobs-university.de
familyName
Jeltsch
Given name
Albert
is
relates
of
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_48/101021bi025979a/authorship/2
http://hub.abes.fr/oup/periodical/nar/2001/volume_29/issue_18/101093nar29183705/authorship/2
http://hub.abes.fr/oup/periodical/nar/2008/volume_36/issue_21/101093nargkn747/authorship/8
http://hub.abes.fr/oup/periodical/nar/2005/volume_33/issue_22/101093nargki1009/authorship/4
http://hub.abes.fr/oup/periodical/nar/2008/volume_36/issue_5/101093nargkn083/authorship/6
http://hub.abes.fr/oup/periodical/proeng/1996/volume_9/issue_5/101093protein95413/authorship/1
http://hub.abes.fr/oup/periodical/nar/2003/volume_31/issue_7/101093nargkg274/authorship/19
http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_1/101093nargkl1035/authorship/7
http://hub.abes.fr/oup/periodical/hmg/2006/volume_15/issue_9/101093hmgddl059/authorship/7
http://hub.abes.fr/oup/periodical/proeng/2000/volume_13/issue_4/101093protein134275/authorship/2
http://hub.abes.fr/oup/periodical/nar/2001/volume_29/issue_15/101093nar29153137/authorship/2
http://hub.abes.fr/oup/periodical/nar/2006/volume_34/issue_4/101093nargkl002/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1998/volume_37/issue_16/101021bi973025s/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1997/volume_36/issue_38/101021bi9705826/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_37/101021bi0155450/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_29/101021bi047634t/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1998/volume_37/issue_8/101021bi9719206/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1999/volume_38/issue_13/101021bi982456n/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_18/101021bi00018a028/authorship/1
http://hub.abes.fr/springer/periodical/239/1996/volume_42/issue_2/B937E6A462D962A2E053120B220A02BD/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_34/101021bi00200a001/authorship/1
is
Author
of
DNA Binding Specificity of the EcoRV Restriction Endonuclease Is Increased by Mg2+ Binding to a Metal Ion Binding Site Distinct from the Catalytic Center of the Enzyme
Structure and function of type II restriction endonucleases
Accuracy of DNA methylation pattern preservation by the Dnmt1 methyltransferase
Chimeric DNA methyltransferases target DNA methylation to specific DNA sequences and repress expression of target genes
Formation of nucleoprotein filaments by mammalian DNA methyltransferase Dnmt3a in complex with regulator Dnmt3L
Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutants
On the possibilities and limitations of rational protein design to expand the specificity of restriction enzymes: a case study employing EcoRV as the target
Does the Restriction Endonuclease EcoRV Employ a Two-Metal-Ion Mechanismfor DNA Cleavage?
Intra- vs Intersubunit Communication in the Homodimeric Restriction EnzymeEcoRV: Thr 37 and Lys 38 Involved in Indirect Readout Are Only Important forthe Catalytic Activity of Their Own Subunit
Probing the DNA Interface of the EcoRV DNA-(Adenine-N6)-methyltransferase bySite-Directed Mutagenesis, Fluorescence Spectroscopy, and UV Cross-Linking
Developing a programmed restriction endonuclease for highly specific DNA cleavage
Mutations in DNA methyltransferase DNMT3B in ICF syndrome affect its regulation by DNMT3L
Changing the target base specificity of the EcoRV DNA methyltransferase by rational de novo protein-design
Bisulfite sequencing Data Presentation and Compilation (BDPC) web server—a useful tool for DNA methylation analysis
How Does a DNA Interacting Enzyme Change Its Specificity during MolecularEvolution? A Site-Directed Mutagenesis Study at the DNA Binding Site of theDNA-(Adenine-N6)-methyltransferase EcoRV
De Novo Methylation of Nucleosomal DNA by the Mammalian Dnmt1 andDnmt3A DNA Methyltransferases
A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes
Kinetic Characterization of Linear Diffusion of the Restriction EndonucleaseEcoRV on DNA
Plasmid DNA Cleavage by MunI Restriction Enzyme: Single-Turnover andSteady-State Kinetic Analysis
Horizontal gene transfer contributes to the wide distribution and evolution of type II restriction-modification systems
Pausing of the Restriction Endonuclease EcoRI during Linear Diffusion on DNA
Alternative Linked Data Documents:
ODE
Content Formats:
RDF
ODATA
Microdata
