about
Architecture of the yeast origin recognition complex bound to origins of DNA replication.Zinc fingers 1-7 of EVI1 fail to bind to the GATA motif by itself but require the core site GACAAGATA for bindingPurification and characterization of an arginine regulatory protein, ArgR, from Pseudomonas aeruginosa and its interactions with the control regions for the car, argF, and aru operonsThe rat poly pyrimidine tract binding protein (PTB) interacts with a single-stranded DNA motif in a liver-specific enhancerDistinct regions of Cu(I).ACE1 contact two spatially resolved DNA major groove sites.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.Contacts between steroid hormone receptors and thymines in DNA: an interference method.Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro.Cra-dependent transcriptional activation of the icd gene of Escherichia coli.Amino acid-DNA contacts by RhaS: an AraC family transcription activatorDNA flexibility of the UP element is a major determinant for transcriptional activation at the Escherichia coli acetate promoterDNA determinants in sequence-specific recognition by XmaI endonucleaseMissing-base and ethylation interference footprinting of P1 plasmid replication initiator.Recognition of specific nucleotide bases and cooperative DNA binding by the trans-acting nitrogen regulatory protein NIT2 of Neurospora crassaUracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: the GCN4-DNA complex.Fine structure of E. coli RNA polymerase-promoter interactions: alpha subunit binding to the UP element minor grooveMolecular architecture of a eukaryotic DNA replication terminus-terminator protein complexTowards novel amino acid-base contacts in gene regulatory proteins: AraR--a case study.Use of gel retardation to analyze protein-nucleic acid interactions.Lysine 188 of the catabolite gene activator protein (CAP) plays no role in specificity at base pair 7 of the DNA half site.Sequence requirements for binding of Rep68 to the adeno-associated virus terminal repeatsAn avian 40 KDa nucleoprotein binds preferentially to a promoter sequence containing one single pair of methylated CpG.The FLP protein contacts both major and minor grooves of its recognition target sequence.Substrate-assisted catalysis in the cleavage of DNA by the EcoRI and EcoRV restriction enzymesIdentification of base and backbone contacts used for DNA sequence recognition and high-affinity binding by LAC9, a transcription activator containing a C6 zinc finger.A nuclear single-stranded-DNA binding factor interacts with the long terminal repeats of the 1731 Drosophila retrotransposon.Highly conserved residues in the bZIP domain of yeast GCN4 are not essential for DNA bindingMultiple components are required for sequence recognition of the AP1 site in the gibbon ape leukemia virus enhancer.Photolyases from Saccharomyces cerevisiae and Escherichia coli recognize common binding determinants in DNA containing pyrimidine dimersCTCF, a conserved nuclear factor required for optimal transcriptional activity of the chicken c-myc gene, is an 11-Zn-finger protein differentially expressed in multiple forms.Mechanistic insights into replication termination as revealed by investigations of the Reb1-Ter3 complex of Schizosaccharomyces pombe.Hierarchical mechanisms build the DNA-binding specificity of FUSE binding protein.EVI1 Interferes with Myeloid Maturation via Transcriptional Repression of Cebpa, via Binding to Two Far Downstream Regulatory Elements.Analysis of DNA binding by a eubacterial zinc finger transcription factorA structural model for a homeotic protein-extradenticle-DNA complex accounts for the choice of HOX protein in the heterodimerThree protein binding sites form an enhancer that regulates sex- and fat body-specific transcription of Drosophila yolk protein genes.The sequence and binding specificity of UaY, the specific regulator of the purine utilization pathway in Aspergillus nidulans, suggest an evolutionary relationship with the PPR1 protein of Saccharomyces cerevisiae.Sequence-specific DNA recognition by the SmaI endonuclease.DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein.5-Methylcytosine DNA glycosylase activity is also present in the human MBD4 (G/T mismatch glycosylase) and in a related avian sequence.
P2860
Q27940033-7DF8F6B9-D3BB-4DD8-AA52-CD83F2FF9CBFQ28273005-7E295385-204B-4817-A7C3-FD40571F739EQ28492637-91A67BE1-67F9-4E19-B141-C7366BC1FD7DQ28577456-397D513E-BD65-4D6C-93AC-81AC17C6C88DQ30418272-B5FF2F10-5B86-46A6-83D9-0C32018775C6Q33640827-64B6B36E-7C50-498D-9628-43BE0E51380EQ33797438-409C1900-9A67-4378-AFDB-FEAA7CD57339Q33888644-F33D534F-35BE-403D-8743-894654B6E9A5Q33991145-38C7AE2E-D103-47D7-8261-5AC04F31CDF7Q33992786-DC0A81A1-490B-4D54-B5E9-171EEF1BDAE6Q34625812-066867FB-AC6F-4312-9E9B-5EF7AE1D5512Q34770269-52506F92-6591-4D57-A987-5790D62CBD41Q34800398-A999EA98-B2D5-428D-AAE1-BA3B076525C9Q34998584-B03BB835-E189-4712-8457-FB7D47842DCFQ35060086-3575C898-D7E5-4E18-BD8C-26B3C28CF91FQ35077442-E2EFA2D5-85FD-4F06-B6CD-1A7B248675ABQ35131404-A7CCFBF2-28D6-4BD7-8EAD-C46366DB9AE2Q35387166-195919D0-9E60-4EF0-9336-BD3F7F6A7ADBQ35655392-B45F4614-BC51-43F8-B8C6-6B9742849703Q35833611-306A0105-507B-4946-9E19-BBCE27818D70Q35856414-19E2A18A-5C7B-48E4-8D36-6018F444A13EQ35915877-60C855E0-E7A9-4788-A41E-EDD47D4A9B43Q35934766-81107F0B-A01E-4DF8-84EF-054001E8E67CQ36536632-C22ABD2E-1880-4CED-92D7-A7E9D1D16411Q36687052-BB29E43F-1938-4263-8211-0B79C75F86D4Q36692894-0C04561C-0664-4FA6-AD0F-3A41F178B763Q36735327-CED18C24-E2BD-4AEE-AD16-2F000D2F6052Q36794633-D2FBDD58-2D48-4F83-AA8B-EDC92DA46615Q36794833-AE2D85D1-6114-4869-877D-D5CAE81E6F7CQ36827796-3CF59C6D-306B-4824-9AB6-927402AC3524Q36949911-5E108E19-89A0-4A76-948C-3980A60ADA8FQ36985184-476FA15D-2457-4152-8F5D-91B86197EC27Q37034398-68F92F00-3E4F-4EE5-9F67-917C423703BCQ37247863-9F8C095D-5407-4D51-8C6C-7EEFEB6C5173Q37580602-B6D6B3A6-F271-43D7-8594-1C168E3B96FBQ37695186-7F8A7625-58AE-4259-8B60-E2C1C560C9EFQ38296879-D4FDA7C6-92A0-4D44-8D09-62A5CFC00C0CQ38297419-4BB90F5C-F82A-4E8E-AF44-3209D32E8B0FQ38301846-0C4B7AD3-4ED2-4482-9DB7-E9F91B393216Q38307104-4C2F0038-FA2F-4494-A90E-B17F12B4D83D
P2860
description
1987 nî lūn-bûn
@nan
1987 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Missing contact probing of DNA-protein interactions.
@ast
Missing contact probing of DNA-protein interactions.
@en
Missing contact probing of DNA-protein interactions.
@nl
type
label
Missing contact probing of DNA-protein interactions.
@ast
Missing contact probing of DNA-protein interactions.
@en
Missing contact probing of DNA-protein interactions.
@nl
prefLabel
Missing contact probing of DNA-protein interactions.
@ast
Missing contact probing of DNA-protein interactions.
@en
Missing contact probing of DNA-protein interactions.
@nl
P2860
P356
P1476
Missing contact probing of DNA-protein interactions.
@en
P2093
A Brunelle
R F Schleif
P2860
P304
P356
10.1073/PNAS.84.19.6673
P407
P577
1987-10-01T00:00:00Z