Determination of the orientation of a DNA binding motif in a protein-DNA complex by photocrosslinking. - Wikidata - awgldk - TriplyDB

Determination of the orientation of a DNA binding motif in a protein-DNA complex by photocrosslinking.

Determination of the orientation of a DNA binding motif in a protein-DNA complex by photocrosslinking.

http://www.wikidata.org/entity/Q37274524

about

High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2 Protein-DNA photo-crosslinking with a genetically encoded benzophenone-containing amino acid.Architecture of high mobility group protein I-C.DNA complex and its perturbation upon phosphorylation by Cdc2 kinase.Specific photocrosslinking of DNA-protein complexes: identification of contacts between integration host factor and its target DNA.Structural Mechanisms of Nucleosome Recognition by Linker Histones.Disparity in the DNA translocase domains of SWI/SNF and ISW2.Orientation of the LexA DNA-binding motif on operator DNA as inferred from cysteine-mediated phenyl azide crosslinking.Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking.The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.High-resolution mapping of nucleoprotein complexes by site-specific protein-DNA photocrosslinking: organization of the human TBP-TFIIA-TFIIB-DNA quaternary complex.The functional subunit of a dimeric transcription activator protein depends on promoter architecture.Probing FinO-FinP RNA interactions by site-directed protein-RNA crosslinking and gelFRET.Furan oxidation based cross-linking: a new approach for the study and targeting of nucleic acid and protein interactions.Determinants of affinity and mode of DNA binding at the carboxy terminus of the bacteriophage SPO1-encoded type II DNA-binding protein, TF1 The structure and function of the replication terminator protein of Bacillus subtilis: identification of the 'winged helix' DNA-binding domain.Photocross-linking of nucleic acids to associated proteins.A single domain of the replication termination protein of Bacillus subtilis is involved in arresting both DnaB helicase and RNA polymerase.Cross-linking of DNA-binding proteins to DNA with psoralen and psoralen furan-side monoadducts. Comparison of action spectra with DNA-DNA cross-linking.The Sequence of Nucleosomal DNA Modulates Sliding by the Chd1 Chromatin Remodeler.Interdomain Communication of the Chd1 Chromatin Remodeler across the DNA Gyres of the Nucleosome.Evidence for contact between the cyclic AMP receptor protein and the delta 70 subunit of Escherichia coli RNA polymerase.A twist defect mechanism for ATP-dependent translocation of nucleosomal DNA.

P2860

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P2860

Determination of the orientation of a DNA binding motif in a protein-DNA complex by photocrosslinking.

http://www.wikidata.org/entity/Q37274524

description

1992 nî lūn-bûn

@nan

1992年の論文

@ja

1992年学术文章

@wuu

1992年学术文章

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1992年学术文章

@zh-hans

1992年学术文章

@zh-my

1992年学术文章

@zh-sg

1992年學術文章

@yue

1992年學術文章

@zh

1992年學術文章

@zh-hant

name

Determination of the orientati ...... complex by photocrosslinking.

@en

Determination of the orientati ...... complex by photocrosslinking.

@nl

type

label

Determination of the orientati ...... complex by photocrosslinking.

@en

Determination of the orientati ...... complex by photocrosslinking.

@nl

prefLabel

Determination of the orientati ...... complex by photocrosslinking.

@en

Determination of the orientati ...... complex by photocrosslinking.

@nl

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PNAS.89.21.10287

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Determination of the orientati ...... complex by photocrosslinking.

@en

P2093

P S Pendergrast

http://www.w3.org/2001/XMLSchema#string

R H Ebright

http://www.w3.org/2001/XMLSchema#string

Y Chen

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Y W Ebright

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P2860

Tissue sulfhydryl groups

Sequencing end-labeled DNA with base-specific chemical cleavages

Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees

Identification of a contact between arginine-180 of the catabolite gene activator protein (CAP) and base pair 5 of the DNA site in the CAP-DNA complex.

Mutations that alter the DNA sequence specificity of the catabolite gene activator protein of E. coli.

Role of glutamic acid-181 in DNA-sequence recognition by the catabolite gene activator protein (CAP) of Escherichia coli: altered DNA-sequence-recognition properties of [Val181]CAP and [Leu181]CAP

Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving.

Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site.

Modification of DNA by aflatoxin B1 creates alkali-labile lesions in DNA at positions of guanine and adenine.

Efficient site-directed mutagenesis using uracil-containing DNA.

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10287-10291

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scholarly article

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10.1073/PNAS.89.21.10287

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21

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89

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21823752

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1332042

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50323

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