Evidence map›Paper›PMID 10716990›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex.

R Yamaji, R Adamik, K Takeda, A Togawa, G Pacheco-Rodriguez, V J Ferrans, J Moss, M Vaughan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

59 citing papers in PubMed, 115 citations in OpenAlex.

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  14. Enhancement of β-catenin activity by BIG1 plus BIG2 via Arf activation and cAMP signals.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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  20. Chlamydial intracellular survival strategies.Cold Spring Harbor perspectives in medicine · 2013
    Review
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 at 2 institutions in 1 country.

R YamajiPulmonary-Critical Care Medicine Branch and Pathology Section, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. yamajir@fido.nhlbi.nih.gov
R Adamik
K Takeda
A Togawa
G Pacheco-Rodriguez
V J Ferrans
J Moss
M Vaughan
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

Molecular Characterization and Regulation of GTP-binding ProteinsZIAHL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 2009 to 2016
$8.4M
REGULATION OF GTP-BINDING PROTEINSZ01HL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 1985 to 2008
$4.5M
6 · The paper itself

Abstract

Two brefeldin A (BFA)-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors, 200-kDa BIG1 and 190-kDa BIG2, were copurified from bovine brain cytosol associated with >670-kDa macromolecular complexes. When observed by immunofluorescence in HeLa S3 and HepG2 cells, endogenous BIG1 and coexpressed BIG2 were distributed in a punctate pattern throughout the cytosol, and also concentrated in the perinuclear region, where endogenous BIG1 and BIG2 each partially colocalized with Golgi-specific 58K protein and gamma-adaptin. On Western blot analysis, both BIG1 and BIG2 were clearly more abundant in the cytosol than in the microsomal fractions. After density gradient centrifugation of a microsomal fraction, BIG1 and BIG2 were recovered in the same fraction as beta-COP, a marker for Golgi membranes. When cytosol from HeLa S3 cells was subjected to gel filtration and fractions were analyzed by Western blotting, the largest percentages of both BIG1 and BIG2 were detected in fractions containing proteins with a molecular mass of >670 kDa. Western blotting using anti-peptide antibodies specific for BIG1 or BIG2 demonstrated that approximately 70% of BIG2 was immunoprecipitated along with 100% of BIG1 by the anti-BIG1 IgG, and approximately 75% of BIG1 was coprecipitated with 100% of BIG2 by the anti-BIG2 IgG. All observations were consistent with the conclusion that significant fractions of BIG1 and BIG2 exist as components of the same macromolecular complexes in bovine brain cytosol and are similarly localized in cultured cells.

Indexed as

ADP-Ribosylation FactorsBlotting, WesternBrefeldin ACytosolDose-Response Relationship, DrugGolgi ApparatusGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansMicroscopy, FluorescenceMicrosomesPeptidesPrecipitin TestsProtein Synthesis InhibitorsTime FactorsADP-Ribosylation FactorsARFGEF1 protein, humanARFGEF2 protein, humanBrefeldin AGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsPeptidesProtein Synthesis Inhibitors

Identifiers

PMID10716990
PMCPMC15969
OpenAlexW2125631857

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.