Evidence map›Paper›PMID 11483498›Full record

ArticleThe EMBO journal2001

Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif.

H Terasawa, Y Noda, T Ito, H Hatanaka, S Ichikawa, K Ogura, H Sumimoto, F Inagaki

Abstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

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  7. Cdc42 GTPase dynamics control directional growth responses.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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

8 authors.

H TerasawaTokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan.
Y Noda
T Ito
H Hatanaka
S Ichikawa
K Ogura
H Sumimoto
F Inagaki

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PB1 domains are novel protein modules capable of binding to target proteins that contain PC motifs. We report here the NMR structure and ligand-binding site of the PB1 domain of the cell polarity establishment protein, Bem1p. In addition, we identify the topology of the PC motif-containing region of Cdc24p by NMR, another cell polarity establishment protein that interacts with Bem1p. The PC motif-containing region is a structural domain offering a scaffold to the PC motif. The chemical shift perturbation experiment and the mutagenesis study show that the PC motif is a major structural element that binds to the PB1 domain. A structural database search reveals close similarity between the Bem1p PB1 domain and the c-Raf1 Ras-binding domain. However, these domains are functionally distinct from each other.

Indexed as

Guanine Nucleotide Exchange FactorsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBinding SitesCell Cycle ProteinsFungal ProteinsHumansLigandsMiceMolecular Sequence DataPhosphoproteinsProtein Kinase CProtein Kinase C zetaAdaptor Proteins, Signal TransducingBEM1 protein, S cerevisiaeCDC24 protein, S cerevisiaeCell Cycle ProteinsFungal ProteinsGuanine Nucleotide Exchange FactorsLigandsneutrophil cytosol factor 67KPhosphoproteinsProtein Kinase CProtein Kinase C zetaProto-Oncogene ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteinsscd2 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID11483498
PMCPMC149143

What OpenQuestion holds

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Registered trials

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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.