(Q47892200)

English

Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase.

scientific article published in July 1998

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scholarly article

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase. (English)

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

4

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

author name string

Roth M

1

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

Helm-Kruse S

2

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

Friedrich T

3

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Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

language of work or name

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publication date

1 July 1998

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

Journal of Biological Chemistry

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Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

273

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Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

17333-17342

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Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

28

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Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

describes a project that uses

site-directed mutagenesis

1 reference

based on heuristic

inferred from title

Eukaryotic DNA methyltransferases--structure and function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Alterations in DNA methylation may play a variety of roles in carcinogenesis

1 reference

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Effects of DNA methylation on DNA-binding proteins and gene expression.

1 reference

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21 January 2018

DNA methylation and genomic imprinting

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Structure and function of DNA methyltransferases.

1 reference

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21 January 2018

Chemistry and biology of DNA methyltransferases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

The DNA (cytosine-5) methyltransferases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

HhaI methyltransferase flips its target base out of the DNA helix

1 reference

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21 January 2018

Enzymatic C5-cytosine methylation of DNA: mechanistic implications of new crystal structures for HhaL methyltransferase-DNA-AdoHcy complexes

1 reference

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21 January 2018

A structural basis for the preferential binding of hemimethylated DNA by HhaI DNA methyltransferase

1 reference

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21 January 2018

The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing

1 reference

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21 January 2018

The GATATC-modification enzyme EcoRV is closely related to the GATC-recognizing methyltransferases DpnII and dam from E. coli and phage T4.

1 reference

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21 January 2018

Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases

1 reference

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21 January 2018

Finding sequence motifs in groups of functionally related proteins

1 reference

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21 January 2018

Amino acid sequence arrangements of DNA-methyltransferases

1 reference

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21 January 2018

Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes.

1 reference

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21 January 2018

The role of the preserved sequences of Dam methylase

1 reference

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21 January 2018

Functional analysis of conserved motifs in EcoP15I DNA methyltransferase

1 reference

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21 January 2018

Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI.

1 reference

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21 January 2018

Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine

1 reference

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21 January 2018

Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Universal catalytic domain structure of AdoMet-dependent methyltransferases.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Targeted base stacking disruption by the EcoRI DNA methyltransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

DNA distortion and base flipping by the EcoRV DNA methyltransferase. A study using interference at dA and T bases and modified deoxynucleosides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Kinetics of methylation and binding of DNA by the EcoRV adenine-N6 methyltransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

The cloning, purification and characterization of the Eco RV modification methylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Incorporation of a complete set of deoxyadenosine and thymidine analogues suitable for the study of protein nucleic acid interactions into oligodeoxynucleotides. Application to the EcoRV restriction endonuclease and modification methylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Sequence-specific binding of DNA by the EcoRV restriction and modification enzymes with nucleic acid and cofactor analogues

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Probing the protein-DNA interface of the EcoRV modification methyltransferase bound to its recognition sequence, GATATC.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Functional mapping of the EcoRV DNA methyltransferase by random mutagenesis and screening for catalytically inactive mutants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Crystal structure of catechol O-methyltransferase

1 reference

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21 January 2018

The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends

1 reference

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21 January 2018

Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

1 reference

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21 January 2018

Sequence-specific DNA binding by the MspI DNA methyltransferase

1 reference

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21 January 2018

Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

A model for DNA binding and enzyme action derived from crystallographic studies of the TaqI N6-adenine-methyltransferase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

The EcoRV modification methylase causes considerable bending of DNA upon binding to its recognition sequence GATATC

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17333

21 January 2018

Identifiers

10.1074/JBC.273.28.17333

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

1 reference

Europe PubMed Central

6 February 2018

http://europepmc.org/abstract/MED/9651316

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