Evidence map›Paper›PMID 19698085›Full record

ReviewThe Biochemical journal2009

Molecular biology, genetics and biochemistry of the repulsive guidance molecule family.

Christopher J Severyn, Ujwal Shinde, Peter Rotwein

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 17% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
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  13. B7-DC (PD-L2) costimulation of CD4Cellular & molecular immunology · 2018
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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

3 authors at 1 institution in 1 country.

Christopher J SeverynDepartment of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, OR 97239-3098, U.S.A.
Ujwal Shinde
Peter Rotwein
Oregon Health & Science University · US

Funding

INSULINLIKE GROWTH FACTORS AND MUSCLE DIFFERENTIATIONR01DK042748 · NIDDK · WASHINGTON UNIVERSITY · PI ROTWEIN, PETER S · 1991 to 2017
$5.6M
TRAINING PROGRAM IN MOLECULAR HEMATOLOGYT32HL007781 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI BAGBY, GROVER CARLTON · 1993 to 2012
$5.1M
OHSU Medical Scientist Training ProgramT32GM067549 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI JACOBY, DAVID B · 2004 to 2008
$996k
Characterizing the Mechanisms of Transcription Regulation of RGMc/HemojuvelinF30HL095327 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI SEVERYN, CHRISTOPHER JOHN · 2009 to 2011
$127k
NHLBI NIH HHS F30 HL095327NHLBI NIH HHS T32 HL007781NIDDK NIH HHS R01 DK042748NIDDK NIH HHS R01 DK42748NIGMS NIH HHS T32 GM067549
6 · The paper itself

Abstract

RGMs (repulsive guidance molecules) comprise a recently discovered family of GPI (glycosylphosphatidylinositol)-linked cell-membrane-associated proteins found in most vertebrate species. The three proteins, RGMa, RGMb and RGMc, products of distinct single-copy genes that arose early in vertebrate evolution, are approximately 40-50% identical to each other in primary amino acid sequence, and share similarities in predicted protein domains and overall structure, as inferred by ab initio molecular modelling; yet the respective proteins appear to undergo distinct biosynthetic and processing steps, whose regulation has not been characterized to date. Each RGM also displays a discrete tissue-specific pattern of gene and protein expression, and each is proposed to have unique biological functions, ranging from axonal guidance during development (RGMa) to regulation of systemic iron metabolism (RGMc). All three RGM proteins appear capable of binding selected BMPs (bone morphogenetic proteins), and interactions with BMPs mediate at least some of the biological effects of RGMc on iron metabolism, but to date no role for BMPs has been defined in the actions of RGMa or RGMb. RGMa and RGMc have been shown to bind to the transmembrane protein neogenin, which acts as a critical receptor to mediate the biological effects of RGMa on repulsive axonal guidance and on neuronal survival, but its role in the actions of RGMc remains to be elucidated. Similarly, the full spectrum of biological functions of the three RGMs has not been completely characterized yet, and will remain an active topic of ongoing investigation.

Indexed as

AnimalsCell Adhesion Molecules, NeuronalGPI-Linked ProteinsHemochromatosis ProteinHumansMembrane ProteinsModels, GeneticMuscle ProteinsNerve Tissue ProteinsPhylogenyProtein Structure, SecondaryCell Adhesion Molecules, NeuronalGPI-Linked ProteinsHemochromatosis ProteinHJV protein, mouseMembrane ProteinsMuscle ProteinsNerve Tissue ProteinsRGMA protein, humanRgma protein, mouseRgmb protein, mouse

Identifiers

PMID19698085
PMCPMC4242795
OpenAlexW2041648924

What OpenQuestion holds

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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.