Evidence map›Paper›PMID 7935440›Full record

ArticleMolecular and cellular biology1994

Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein.

Y W Kim, G A Otterson, R A Kratzke, A B Coxon, F J Kaye

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.4field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 45 citations in OpenAlex.

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  5. Identifying novel SMYD3 interactors on the trail of cancer hallmarks.Computational and structural biotechnology journal · 2022
    Article
  6. Cell stemness is maintained upon concurrent expression of RB and the mitochondrial ribosomal protein S18-2.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Autochthonous tumors driven byProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. The histone demethylase KDM5A is required for the repression of astrocytogenesis and regulated by the translational machinery in neural progenitor cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
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  10. Review
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  19. Hypoxia-induced gene expression profiling in the euryoxic fish Gillichthys mirabilis.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Y W KimNCI-Navy Medical Oncology Branch, National Cancer Institute, Bethesda, Maryland.
G A Otterson
R A Kratzke
A B Coxon
F J Kaye
United States Department of the Navy · USNational Cancer Institute · UA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The growth suppressor activities of the RB and p107 products are believed to be mediated by the reversible binding of a heterogeneous family of cellular proteins to a conserved T/E1A pocket domain that is present within both proteins. To study the functional role of these interactions, we examined the properties of cellular retinoblastoma binding protein 2 (RBP2) binding to RB, p107, and the related TATA-binding protein (TBP) product. We observed that although RBP2 bound exclusively to the T/E1A pocket of p107, it could interact with RB through independent T/E1A and non-T/E1A domains and with TBP only through the non-T/E1A domain. Consistent with this observation, we found that a mutation within the Leu-X-Cys-X-Glu motif of RBP2 resulted in loss of ability to precipitate p107, while RB- and TBP-binding activities were retained. We located the non-T/E1A binding site of RBP2 on a 15-kDa fragment that is independent from the Leu-X-Cys-X-Glu motif and encodes binding activity for RB and TBP but does not interact with p107. Despite the presence of a non-T/E1A binding site, however, recombinant RBP2 retained the ability to preferentially precipitate active hypophosphorylated RB from whole-cell lysates. In addition, we found that cotransfection of RBP2 can reverse in vivo RB-mediated suppression of E2F activity. These findings confirm the differential binding specificities of the related RB, p107, and TBP proteins and support the presence of multifunctional domains on the nuclear RBP2 product which may allow complex interactions with the cellular transcription machinery.

Indexed as

Cell Cycle ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsTumor Suppressor ProteinsAmino Acid SequenceCarrier ProteinsDNA-Binding ProteinsE2F Transcription FactorsGenes, RetinoblastomaHumansModels, BiologicalMolecular Sequence DataMutationPeptide FragmentsProtein BindingProteinsCarrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsE2F Transcription FactorsIntracellular Signaling Peptides and ProteinsKDM5A protein, humanNuclear ProteinsPeptide FragmentsProteinsRBL1 protein, humanRecombinant Fusion ProteinsRetinoblastoma-Binding Protein 1Retinoblastoma-Binding Protein 2Retinoblastoma-Like Protein p107Retinoblastoma ProteinTATA-Box Binding ProteinTranscription Factor DP1Transcription FactorsTumor Suppressor Proteins

Identifiers

PMID7935440
PMCPMC359260
OpenAlexW2171081413

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.