Evidence map›Paper›PMID 8590804›Full record

ArticleMolecular biology of the cell1995

BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs.

G Rossi, K Kolstad, S Stone, F Palluault, S Ferro-Novick

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

32 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
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  10. Entry and exit mechanisms at the cis-face of the Golgi complex.Cold Spring Harbor perspectives in biology · 2011
    Review
  11. New links between vesicle coats and Rab-mediated vesicle targeting.Seminars in cell & developmental biology · 2011
    Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  17. 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 1 institution in 1 country.

G RossiDepartment of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
K Kolstad
S Stone
F Palluault
S Ferro-Novick
Yale University · US

Funding

ROLE OF YPT5 INTERACTING COMPONENTS IN ENDOCYTOSISP01CA046128 · NCI · YALE UNIVERSITY · PI NOVICK, PETER JAY · 1988 to 2007
$9.5M
DEFINING COMPONENTS REQUIRED FOR TRANSPORT FROM THE ERR01GM045431 · NIGMS · YALE UNIVERSITY · PI FERRO-NOVICK, SUSAN S · 1991 to 1995
–
NCI NIH HHS CA-46128NIGMS NIH HHS 1 RO1 GM-45431
6 · The paper itself

Abstract

Here we report the identification of BET3, a new member of a group of interacting genes whose products have been implicated in the targeting and fusion of endoplasmic reticulum (ER) to Golgi transport vesicles with their acceptor compartment. A temperature-sensitive mutant in bet3-1 was isolated in a synthetic lethal screen designed to identify new genes whose products may interact with BET1, a type II integral membrane protein that is required for ER to Golgi transport. At 37 degrees C, bet3-1 fails to transport invertase, alpha-factor, and carboxypeptidase Y from the ER to the Golgi complex. As a consequence, this mutant accumulates dilated ER and small vesicles. The SNARE complex, a docking/fusion complex, fails to form in this mutant. Furthermore, BET3 encodes an essential 22-kDa hydrophilic protein that is conserved in evolution, which is not a component of this complex. These findings support the hypothesis that Bet3p may act before the assembly of the SNARE complex.

Indexed as

Genes, FungalSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAmino Acid SequenceCloning, MolecularEndoplasmic ReticulumFungal ProteinsGolgi ApparatusKineticsMembrane ProteinsMicroscopy, ElectronMolecular Sequence DataRecombinant ProteinsRestriction MappingSaccharomyces cerevisiaeSequence Homology, Amino AcidBET3 protein, S cerevisiaeFungal ProteinsMembrane ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID8590804
PMCPMC301331
OpenAlexW2081933766

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.