Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain.
about
Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIIDIdentification of a mouse TBP-like protein (TLP) distantly related to the drosophila TBP-related factorA functional interaction between the survival motor neuron complex and RNA polymerase IIInhibition of TATA binding protein dimerization by RNA polymerase III transcription initiation factor Brf1.TATA-Binding protein-interacting protein 120, TIP120, stimulates three classes of eukaryotic transcription via a unique mechanismPushing, pulling, dragging, and vibrating renal epithelia by using atomic force microscopy.Identification of a novel 70 kDa protein that binds to the core promoter element and is essential for ribosomal DNA transcription.Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein.Functional interaction of yeast and human TATA-binding proteins with an archaeal RNA polymerase and promoterSlow dimer dissociation of the TATA binding protein dictates the kinetics of DNA bindingYeast TATA binding protein interaction with DNA: fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics.Self-association of the amino-terminal domain of the yeast TATA-binding protein.TBP-like protein (TLP) interferes with Taspase1-mediated processing of TFIIA and represses TATA box gene expression.Structural and functional analysis of mutations along the crystallographic dimer interface of the yeast TATA binding proteinVertebrate TBP-like protein (TLP/TRF2/TLF) stimulates TATA-less terminal deoxynucleotidyl transferase promoters in a transient reporter assay, and TFIIA-binding capacity of TLP is required for this function.Transcription stimulation of the adenovirus type 12 E1a gene in vitro by the 266-amino-acid E1A protein.Shutoff of RNA polymerase II transcription by poliovirus involves 3C protease-mediated cleavage of the TATA-binding protein at an alternative site: incomplete shutoff of transcription interferes with efficient viral replication.Functional characterization of multiple transactivating elements in beta-catenin, some of which interact with the TATA-binding protein in vitro.TBP-interacting protein TIP120A is a new global transcription activator with bipartite functional domains.Specific interaction with transcription factor IIA and localization of the mammalian TATA-binding protein-like protein (TLP/TRF2/TLF).Engineering dimer-stabilizing mutations in the TATA-binding protein.
P2860
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P2860
Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Multimerization of the mouse T ...... s C-terminal conserved domain.
@en
type
label
Multimerization of the mouse T ...... s C-terminal conserved domain.
@en
prefLabel
Multimerization of the mouse T ...... s C-terminal conserved domain.
@en
P2093
P2860
P356
P1476
Multimerization of the mouse T ...... s C-terminal conserved domain.
@en
P2093
Kishimoto T
Muramatsu M
Yamauchi J
P2860
P304
P356
10.1093/NAR/22.7.1179
P577
1994-04-01T00:00:00Z