Evidence map›Paper›PMID 7531036›Full record

ArticleMolecular biology of the cell1994

Transmembrane kit ligand cleavage does not require a signal in the cytoplasmic domain and occurs at a site dependent on spacing from the membrane.

H J Cheng, J G Flanagan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed, 45 citations in OpenAlex.

  1. Fingerprint changes in CSF composition associated with different aetiologies in human neonatal hydrocephalus: inflammatory cytokines.Child's nervous system : ChNS : official journal of the International Society for Pediatric Neurosurgery · 2014
    Article
  2. Article
  3. Ectodomain shedding of angiotensin converting enzyme 2 in human airway epithelia.American journal of physiology. Lung cellular and molecular physiology · 2009
    Article
  4. Article
  5. The distal ectodomain of angiotensin-converting enzyme regulates its cleavage-secretion from the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  6. Article
  7. Article
  8. Article
  9. Membrane protein secretases.The Biochemical journal · 1997
    Review
  10. 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

2 authors at 1 institution in 1 country.

H J ChengDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
J G Flanagan
Harvard University · US

Funding

Identification and Function of Receptors and LigandsR37HD029417 · NICHD · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FLANAGAN, JOHN G · 2002 to 2011
$4.0M
FUNCTION OF RECEPTOR TYROSINE KINASES AND THEIR LIGANDSR01HD029417 · NICHD · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FLANAGAN, JOHN G · 1992 to 2001
$657k
IDENTIFICATION AND ANALYSIS OF ORPHAN RECEPTOR LIGANDSR01DK045580 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FLANAGAN, JOHN G · 1992 to 1995
–
NICHD NIH HHS HD-29417NIDDK NIH HHS DK-45580
6 · The paper itself

Abstract

The kit ligand (KL) is one of several growth factors that are active as transmembrane molecules and can also be proteolytically cleaved to yield soluble forms. We have investigated the signals and structural determinants that control the cleavage of KL. Presentation at the membrane appears to be critical, because no cleavage occurs in variants that lack a transmembrane domain. Signals in the cytoplasmic domain do not seem to be required, because cleavage was not blocked by removal of the C-terminal valine residue, deletion of the whole cytoplasmic tail, or the replacement of the cytoplasmic tail that occurs in the Sl17H mutation. KL thus appears to differ from transforming growth factor-alpha, which apparently requires a C-terminal valine as a signal for cleavage. Although proteolysis must be tightly restricted to the correct cell surface proteins and sites within each protein, cleavage of KL does not seem to be determined entirely by a requirement for a specific substrate sequence. However, the effects of deletion or insertion variants of KL suggest that cleavage may be limited to sites within a specific range of distances from the cell membrane.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsCell Line, TransformedCell MembraneChlorocebus aethiopsHematopoietic Cell Growth FactorsMolecular Sequence DataStem Cell FactorHematopoietic Cell Growth FactorsStem Cell Factor

Identifiers

PMID7531036
PMCPMC301118
OpenAlexW1978849941

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.