about
Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specificallyAutodigestion of lexA and phage lambda repressorsA tale of two repressorsMobile DNA and evolution in the 21st centuryThe Leptospira interrogans lexA gene is not autoregulated.Correlation of two-hybrid affinity data with in vitro measurementsCleavage of bacteriophage lambda cI repressor involves the RecA C-terminal domain.Purification of bacteriophage lambda repressorGenetic selection for dissociative inhibitors of designated protein-protein interactions.Combinatorial approaches to novel proteins.Activation of ara operons by a truncated AraC protein does not require inducerProbing the Escherichia coli glnALG upstream activation mechanism in vivoHomologies between different procaryotic DNA-binding regulatory proteins and between their sites of action.The bacteriophage 434 repressor dimer preferentially undergoes autoproteolysis by an intramolecular mechanism.A variant of lambda repressor with an altered pattern of cooperative binding to DNA sites.Bacteriophage crosstalk: coordination of prophage induction by trans-acting antirepressors.Identification of the lexA gene product of Escherichia coli K-12.Interactions between DNA-bound repressors govern regulation by the lambda phage repressor.Operator binding by lambda repressor heterodimers with one or two N-terminal arms.Bacteria-based in vivo peptide library screening using biopanning approach.Submillisecond folding of monomeric lambda repressorProtein-Protein Interactions in DNA Recognition: H-NMR Studies of Lambda cI Repressors Genetically Altered by Site-Directed MutagenesisDNA gyrase: structure and function.Escherichia coli RNA polymerase subunit omega and its N-terminal domain bind full-length beta' to facilitate incorporation into the alpha2beta subassembly.The preferred substrate for RecA-mediated cleavage of bacteriophage 434 repressor is the DNA-bound dimer.The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinityAmino acid-amino acid contacts at the cooperativity interface of the bacteriophage lambda and P22 repressorsVirus-coded DNA endonuclease from avian retrovirusTranslational regulation: identification of the site on bacteriophage T4 rIIB mRNA recognized by the regA gene function.Isotope-detected 1H NMR studies of proteins: a general strategy for editing interproton nuclear Overhauser effects by heteronuclear decoupling, with application to phage lambda repressor.The c1 repressor of bacteriophage P1 operator-repressor interaction of wild-type and mutant repressor proteins.A monocysteine approach for probing the structure and interactions of the UmuD proteinStructural analysis of the carboxy terminus of bacteriophage lambda repressor determined by antipeptide antibodiesCocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator.Mutant lambda phage repressor with a specific defect in its positive control functionEfficiency of induction of prophage lambda mutants as a function of recA allelesBacteriophage lambda int protein recognizes two classes of sequence in the phage att site: characterization of arm-type sites.Mutations in bacteriophage lambda repressor that prevent RecA-mediated cleavage.Site-specific recombination functions of bacteriophage lambda: DNA sequence of regulatory regions and overlapping structural genes for Int and XisSequences of the recA gene and protein
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1979
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The lambda repressor contains two domains.
@en
The lambda repressor contains two domains.
@nl
type
label
The lambda repressor contains two domains.
@en
The lambda repressor contains two domains.
@nl
prefLabel
The lambda repressor contains two domains.
@en
The lambda repressor contains two domains.
@nl
P2093
P2860
P356
P1476
The lambda repressor contains two domains.
@en
P2093
P2860
P304
P356
10.1073/PNAS.76.4.1608
P407
P577
1979-04-01T00:00:00Z