Evidence map›Paper›PMID 9006988›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997

Phospholipase C-beta1 is present in the botrysome, an intermediate compartment-like organelle, and Is regulated by visual experience in cat visual cortex.

P C Kind, G M Kelly, H J Fryer, C Blakemore, S Hockfield

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-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

9 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Cellular and subcellular localization of PKMζ.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Article
  3. Deletion of PLCB1 gene in schizophrenia-affected patients.Journal of cellular and molecular medicine · 2012
    Article
  4. Review
  5. Article
  6. Article
  7. Immunohistochemical localization of huntingtin-associated protein 1 in endocrine system of the rat.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2005
    Article
  8. Review
  9. The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): comparison with huntingtin in rat and human.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
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.

P C KindSection of Neurobiology, Yale University School of Medicine, New Haven, Connecticut 06511, USA.
G M Kelly
H J Fryer
C Blakemore
S Hockfield
Yale University · USUniversity of Oxford · GB

Funding

FIBROBLAST GROWTH FACTOR IN OCULAR DEVELOPMENTF32EY006511 · NEI · BAYLOR COLLEGE OF MEDICINE · PI ROBINSON, MICHAEL L · 1993 to 1995
–
MOLECULAR STUDIES OF VISUAL CORTICAL PLACTICITYF32EY006606 · NEI · YALE UNIVERSITY · PI KIND, PETER C · 1994 to 1996
–
NEI NIH HHS EY06511NEI NIH HHS EY06606NEI NIH HHS F32 EY006511NEI NIH HHS F32 EY006606
6 · The paper itself

Abstract

Monoclonal antibody Cat-307 identifies a 165 kDa neuronal protein expressed in the cat visual cortex during the period of sensitivity to alterations in visual experience (). Dark-rearing, which prolongs the sensitive period, also prolongs the expression of the Cat-307 protein. The Cat-307 protein localizes to an organelle, here called the botrysome (from the Greek botrys, cluster of grapes), that is located between the endoplasmic reticulum (ER) and Golgi apparatus. The botrysome is composed of small ring-shaped profiles with electron-dense coats. The size and morphology of the rings and their coats are similar to those described for ER to Golgi transport vesicles. Biochemically, the Cat-307 protein cofractionates with microsomes and partitions with subunits of the coatomer proteins that coat ER-to-Golgi transport vesicles. Partial amino acid sequencing reveals that the Cat-307 protein is phospholipase C-beta1, the G-protein-dependent phosphodiesterase that hydrolyses phosphatidylinositol 4,5 biphosphate into inositol 1,4,5 triphosphate and diacylglycerol after the stimulation of a variety of neurotransmitter receptors at the cell surface. These results suggest a role for phospholipase C-beta1 and the botrysome in developmental plasticity and provide a possible link between receptor activation at the cell surface and protein transport during neuronal development.

Indexed as

Animal HusbandryAnimalsAntibodies, MonoclonalCatsDark AdaptationDendritesEndoplasmic ReticulumGolgi ApparatusIsoenzymesMicrosomesNerve Tissue ProteinsNeuronsOrganellesSubcellular FractionsType C PhospholipasesVision, OcularAntibodies, MonoclonalIsoenzymesNerve Tissue ProteinsType C Phospholipases

Identifiers

PMID9006988
PMCPMC6793723
OpenAlexW1492798259

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.