Evidence map›Paper›PMID 19890475›Full record

ArticleCurrent chemical biology2009

S100A1: Structure, Function, and Therapeutic Potential.

Nathan T Wright, Brian R Cannon, Danna B Zimmer, David J Weber

Open access · greenAbstract read
In one paragraph

Article in Current chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

51 citing papers in PubMed, 79 citations in OpenAlex.

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  7. Translational cancer research · 2024
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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

4 authors at 2 institutions in 1 country.

Nathan T WrightDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, Maryland, 21201.
Brian R Cannon
Danna B Zimmer
David J Weber
University of Maryland, Baltimore · USTexas A&M University · US

Funding

Restoration of Tumor Suppression Activity in Malignant MelanomaR01CA107331 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI WEBER, DAVID JOSEPH · 2006 to 2015
$5.4M
The Structure and Function of S100 ProteinsR01GM058888 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI WEBER, DAVID JOSEPH · 1999 to 2010
$3.4M
800 MHZ NMR SPECTROMETERS10RR015741 · NCRR · UNIVERSITY OF MARYLAND BALTIMORE · PI WEBER, DAVID JOSEPH · 2001 to 2001
$500k
600 MHz NMR Spectrometer ConsoleS10RR023447 · NCRR · UNIVERSITY OF MARYLAND BALTIMORE · PI WEBER, DAVID JOSEPH · 2007 to 2007
$362k
Cryoprobe for a 600 Mhz NMR spectrometerS10RR016812 · NCRR · UNIVERSITY OF MARYLAND BALTIMORE · PI WEBER, DAVID JOSEPH · 2002 to 2002
$231k
NCI NIH HHS R01 CA107331NCRR NIH HHS S10 RR015741NCRR NIH HHS S10 RR016812NCRR NIH HHS S10 RR023447NIGMS NIH HHS R01 GM058888
6 · The paper itself

Abstract

S100A1 is a member of the S100 family of calcium-binding proteins. As with most S100 proteins, S100A1 undergoes a large conformational change upon binding calcium as necessary to interact with numerous protein targets. Targets of S100A1 include proteins involved in calcium signaling (ryanidine receptors 1 & 2, Serca2a, phopholamban), neurotransmitter release (synapsins I & II), cytoskeletal and filament associated proteins (CapZ, microtubules, intermediate filaments, tau, mocrofilaments, desmin, tubulin, F-actin, titin, and the glial fibrillary acidic protein GFAP), transcription factors and their regulators (e.g. myoD, p53), enzymes (e.g. aldolase, phosphoglucomutase, malate dehydrogenase, glycogen phosphorylase, photoreceptor guanyl cyclases, adenylate cyclases, glyceraldehydes-3-phosphate dehydrogenase, twitchin kinase, Ndr kinase, and F1 ATP synthase), and other Ca2+-activated proteins (annexins V & VI, S100B, S100A4, S100P, and other S100 proteins). There is also a growing interest in developing inhibitors of S100A1 since they may be beneficial for treating a variety of human diseases including neurological diseases, diabetes mellitus, heart failure, and several types of cancer. The absence of significant phenotypes in S100A1 knockout mice provides some early indication that an S100A1 antagonist could have minimal side effects in normal tissues. However, development of S100A1-mediated therapies is complicated by S100A1's unusual ability to function as both an intracellular signaling molecule and as a secreted protein. Additionally, many S100A1 protein targets have only recently been identified, and so fully characterizing both these S100A1-target complexes and their resulting functions is a necessary prerequisite.

Identifiers

PMID19890475
PMCPMC2771873
OpenAlexW2017771253

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.