Evidence map›Paper›PMID 23583036›Full record

ArticleStructure (London, England : 1993)2013

Structure and T cell inhibition properties of B7 family member, B7-H3.

Vladimir Vigdorovich, Udupi A Ramagopal, Eszter Lázár-Molnár, Eliezer Sylvestre, Jun Sik Lee, Kimberly A Hofmeyer, Xingxing Zang, Stanley G Nathenson, Steven C Almo

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

95 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.

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35 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

Vladimir VigdorovichDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. vladimir.vigdorovich@gmail.com
Udupi A Ramagopal
Eszter Lázár-Molnár
Eliezer Sylvestre
Jun Sik Lee
Kimberly A Hofmeyer
Xingxing Zang
Stanley G Nathenson
Steven C Almo
Albert Einstein College of Medicine · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI WINFRIED EDELMANN · 1985 to 2026
$111.2M
The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI ALMO, STEVEN C. · 2010 to 2014
$32.6M
Molecular and Structural Basis for T Cell CostimulationR01AI007289 · NIAID · YESHIVA UNIVERSITY · PI NATHENSON, STANLEY G · 1985 to 2012
$7.7M
IMMUNOLOGY AND IMMUNUNOOCOLOGY TRAINING PROGRAMT32CA009173 · NCI · YESHIVA UNIVERSITY · PI NATHENSON, STANLEY G · 1985 to 2009
$5.8M
Consortia for High-Throughput-Enabled Structural Biology Partnerships (U01)U01GM094665 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CASADEVALL, ARTURO · 2010 to 2014
$5.5M
New T Cell Coinhibitory Pathway and Type 1 DiabetesDP2DK083076 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI ZANG, XINGXING · 2008 to 2010
$2.6M
Molecular and Structural Basis for T Cell CostimulationR56AI007289 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI NATHENSON, STANLEY G · 2007 to 2007
$553k
BIOCHEMICAL STUDIES ON HISTOCOMPATIBILITY ANTIGENSR37AI007289 · NIAID · YESHIVA UNIVERSITY · PI NATHENSON, STANLEY G · 1987 to 1996
–
NCI NIH HHS CA009173NCI NIH HHS P30 CA013330NCI NIH HHS P30CA013330NCI NIH HHS T32 CA009173NIAID NIH HHS AI007289NIAID NIH HHS R01 AI007289NIAID NIH HHS R56 AI007289NIDDK NIH HHS DP2 DK083076NIDDK NIH HHS DP2DK083076NIGMS NIH HHS GM094662NIGMS NIH HHS GM094665NIGMS NIH HHS U01 GM094665NIGMS NIH HHS U54 GM094662
6 · The paper itself

Abstract

T cell activity is controlled by a combination of antigen-dependent signaling through the T cell receptor and a set of auxiliary signals delivered through antigen-independent interactions, including the recognition of the B7 family of ligands. B7-H3 is a recently identified B7 family member that is strongly overexpressed in a range of cancers and correlates with poor prognosis. We report the crystal structure of murine B7-H3 at a 3 Å resolution, which provides a model for the organization of the IgV and IgC domains within the ectodomain. We demonstrate that B7-H3 inhibits T cell proliferation and show that the FG loop of the IgV domain plays a critical role in this function. B7-H3 crystallized as an unusual dimer arising from the exchange of the G strands in the IgV domains of partner molecules. This arrangement, in combination with previous reports, highlights the dynamic nature and plasticity of the immunoglobulin fold.

Indexed as

Amino Acid SequenceAnimalsB7 AntigensCells, CulturedCrystallography, X-RayDrosophilaLymphocyte ActivationMiceModels, MolecularMolecular Sequence DataProtein ConformationT-LymphocytesB7 AntigensCd276 protein, mouse

Identifiers

PMID23583036
PMCPMC3998375
OpenAlexW2142291912

What OpenQuestion holds

Textmetadata
LicenceTDM
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.