Evidence map›Paper›PMID 8528068›Full record

ArticleProtein science : a publication of the Protein Society1995

Modeled structure of the 75-kDa neurotrophin receptor.

B S Chapman, I D Kuntz

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 46 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

B S ChapmanUniversity of California, San Francisco 94143-0446, USA.
I D Kuntz
University of California, San Francisco · US

Funding

THEORETICAL STUDIES OF MACROMOLECULESR01GM031497 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KUNTZ, IRWIN D · 1985 to 2001
$428k
NIGMS NIH HHS GM-31497
6 · The paper itself

Abstract

Motifs in ligand-binding domains of the neurotrophin (NTR) and lymphotoxin (TNFR-I) receptors define a family of receptors that mediates programmed cell death. We have explored relationships of architecture and function in this family through a molecular model of NTR, also called p75NGFR or LANR. Modeling by homology took advantage of four modular subdomains in the crystal structure of TNFR-I that also occur in NTR. Hypothetical complexes between the model and a ligand structure (for nerve growth factor, NGF) were then examined using docking software. NTR appears to bind in the dimer interface of NGF, making two sets of contacts. NTR subdomains III and IV provide the ligand-contact surfaces, in contrast to TNFR, in which subdomains II and III contact TNF-beta. NTR subdomain II appears to have been evolutionarily modified, potentially contributing to an interface between receptor subunits. These and other specific predictions of the model will require experimental confirmation.

Indexed as

Amino Acid SequenceAnimalsApoptosisBinding SitesChemical PhenomenaChemistry, PhysicalComputer SimulationHumansHydrogen BondingLymphotoxin-alphaMiceModels, MolecularMolecular Sequence DataMolecular WeightNerve Growth FactorsRatsLymphotoxin-alphaNerve Growth FactorsReceptors, Nerve Growth FactorReceptors, Tumor Necrosis Factor

Identifiers

PMID8528068
PMCPMC2143228
OpenAlexW2097639959

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.