Evidence map›Paper›PMID 1637321›Full record

ArticleThe Biochemical journal1992

Molecular cloning and expression of a new rat liver cell-CAM105 isoform. Differential phosphorylation of isoforms.

O Culic, Q H Huang, D Flanagan, D Hixson, S H Lin

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
14.9field-weighted citation impact, top 1% 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

15 citing papers in PubMed, 61 citations in OpenAlex.

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  15. PEST sequences in calmodulin-binding proteins.Molecular and cellular biochemistry
    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

5 authors at 2 institutions in 1 country.

O CulicDepartment of Molecular Pathology, University of Texas, M.D. Anderson Cancer Center, Houston 77030.
Q H Huang
D Flanagan
D Hixson
S H Lin
The University of Texas MD Anderson Cancer Center · USRhode Island Hospital · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Kathrin Milbury · 1985 to 2026
$290.8M
STUDIES ON LIVER ECTO-ATPASE AS A CELL ADHESION MOLECULER01GM043189 · NIGMS · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI LIN, SUE-HWA · 1991 to 1995
–
NCI NIH HHS CA16672NCI NIH HHS CA42715NIGMS NIH HHS GM43189
6 · The paper itself

Abstract

An hepatocyte cell-adhesion molecule (cell-CAM105) was recently shown to be identical with the liver plasma-membrane ecto-ATPase. This protein has structural features of the immunoglobulin superfamily and is homologous with carcinoembryonic antigen proteins. We have cloned a cDNA encoding a new form of the cell-CAM105 which is a variant of the previously isolated clone. In addition to having a shorter cytoplasmic domain, the new isoform also has substitutions clustered in the first 130 amino acids of the extracellular domain. Both of these isoforms are expressed on the surface of hepatocytes with the shorter variant being the predominant form. The previously isolated cell-CAM105 (long form) has more potential phosphorylation sites than does the new isoform (short form). Both isoforms are found to be phosphorylated after incubation with [32P]phosphate in vitro, with the long form being phosphorylated to a significantly higher extent. This observed differential phosphorylation could be one of the mechanisms for the regulation of isoform functions. Using antipeptide antibodies specific for the long form and antibodies that are reactive with both isoforms, we have shown that both isoforms are localized in the canalicular domain of hepatocytes. The sequence differences between these two isoforms suggest that they are probably derived from different genes rather than from alternative splicing.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsAntigens, CDBlotting, WesternCell AdhesionCell Adhesion MoleculesCell MembraneCells, CulturedCloning, MolecularDNAElectrophoresis, Gel, Two-DimensionalFluorescent Antibody TechniqueLiverMolecular Sequence DataPhosphorylationAdenosine TriphosphatasesAntigens, CDCD66 antigensCell Adhesion MoleculesDNA

Identifiers

PMID1637321
PMCPMC1132742
OpenAlexW2399703409

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.