Evidence map›Paper›PMID 7687928›Full record

ArticleCell and tissue research1993

The hypophyseal pars tuberalis is enriched with distinct phosphotyrosine-containing proteins not detected in other areas of the brain and pituitary.

J W Unger, A M Moss, J N Livingston

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Cell and tissue research, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 51% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

3 authors at 2 institutions in 2 countries.

J W UngerAnatomische Anstalt, Universität München, Germany.
A M Moss
J N Livingston
University of Rochester Medical Center · USLudwig-Maximilians-Universität München · DE

Funding

INSULIN AND IGF-I RECEPTORS IN THE CNSR01DK044135 · NIDDK · YALE UNIVERSITY · PI LIVINGSTON, JAMES N · 1992 to 1996
–
NIDDK NIH HHS 1RO1 DK44135-01A1
6 · The paper itself

Abstract

The regulation of cell activity, growth and metabolism by a number of growth factor receptors and proto-oncogene products involves tyrosine kinase activity resulting in autophosphorylation of the receptors and production of phosphorylated tyrosine-containing protein substrates. The identification and precise localization of phosphotyrosine (PY)-containing proteins are first steps in elucidating the functional role of tyrosine kinases in the modulation of the central nervous system and related areas. In the present report, we describe PY-containing proteins in the median eminence and adjacent pars tuberalis of the rat adenohypophysis by immunocytochemistry using light and electron microscopy, and by Western blotting analysis. PY-immunoreactivity was found to be most intense throughout the cytoplasm of a population of epithelial pars tuberalis cells. Polyacrylamide gel electrophoresis and Western blotting of tissue extracts from various brain and pituitary regions demonstrated a general pattern of 4 major bands of PY-proteins, with an additional dense band representing a 44 kDa protein that was highly phosphorylated on tyrosines and that was exclusively found in the pars tuberalis. Additional investigation for the presence of insulin receptors, a tyrosine kinase previously correlated with the distribution of PY-proteins, demonstrated a receptor localization in axons and nerve terminals in the external and internal zone of the median eminence. However, the large amount of different PY-proteins present in the secretory cell population of the pars tuberalis could not be attributed to the insulin receptor.(ABSTRACT TRUNCATED AT 250 WORDS)

Indexed as

Brain ChemistryAnimalsBlotting, WesternBrainCytoplasmElectrophoresis, Polyacrylamide GelImmunohistochemistryMaleMedian EminenceMicroscopy, ElectronPhosphorylationPhosphotyrosinePituitary GlandProtein-Tyrosine KinasesRatsRats, Sprague-DawleyPhosphotyrosineProtein-Tyrosine KinasesReceptor, InsulinTyrosine

Identifiers

PMID7687928
OpenAlexW1989201870

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.