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Cited by 706

The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.

S100 proteins structure functions and pathology

Heizmann, Claus W·2002·Frontiers in Bioscience

Abstract

S100 proteins regulate intracellular processes such as cell growth and motility, cell cycle regulation, transcription and differentiation. Twenty members have been identified so far, and altogether, S100 proteins represent the largest subgroup in the EF-hand Ca2+ -binding protein family. A unique feature of these proteins is that individual members are localized in specific cellular compartments from which some are able to relocate upon Ca2+ activation, transducing the Ca2+ signal in a temporal and spacial manner by interacting with different targets specific for each S100 protein. Some members are even secreted from cells exerting extracellular, cytokine-like activities partially via the surface receptor RAGE (receptor for advanced glycation endproducts) with paracrine effects e.g. on neurons, promoting their survival during development or after injury. Another important aspect is that 14 bona fide S100 genes are found in a gene cluster on human chromosome 1q21 where a number of chromosomal abnormalities occur. This results in a deregulated expression of some S100 genes associated with neoplasias. Recently, S100 proteins have received increasing attention due to their close association with several human diseases including cardiomyopathy, neurodegenerative disorders and cancer. They have also been proven to be valuable in the diagnostic of these diseases, as predictive markers of improving clinical management, outcome and survival of patients and are considered having a potential as drug targets to improve therapies.

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Metadata

Authors
Heizmann, C. W.
Venue
Frontiers in Bioscience
Publisher
IMR Press
Published
2002
Volume
7
Issue
4
Pages
d1356-1368
ISSN
  • 1093-4715 (ISSN-L)
  • 1093-9946
OpenAlex
W173643440
Cited by
706
References
93
Type
conference abstract
Language
en
Open access
closed

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