ArticleProtein science : a publication of the Protein Society2000
A logical sequence search for S100B target proteins.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- The design and delivery of a thermally responsive peptide to inhibit S100B-mediated neurodegeneration.Neuroscience · 2011Article
- Identification of calcium-independent and calcium-enhanced binding between S100B and the dopamine D2 receptor.Biochemistry · 2011Article
- Glial S100B protein modulates mutant ataxin-1 aggregation and toxicity: TRTK12 peptide, a potential candidate for SCA1 therapy.Cerebellum (London, England) · 2011Article
- Bergmann glial S100B activates myo-inositol monophosphatase 1 and Co-localizes to purkinje cell vacuoles in SCA1 transgenic mice.Cerebellum (London, England) · 2009Article
- IQ motif selectivity in human IQGAP1: binding of myosin essential light chain and S100B.Molecular and cellular biochemistry · 2008Article
- Novel interaction of the dopamine D2 receptor and the Ca2+ binding protein S100B: role in D2 receptor function.Molecular pharmacology · 2008Article
- Glial S100B Positive Vacuoles In Purkinje Cells: Earliest Morphological Abnormality In SCA1 Transgenic Mice.Journal of neurological sciences (Turkish) · 2006Article
- S100B-mediated inhibition of the phosphorylation of GFAP is prevented by TRTK-12.Neurochemical research · 2004Article
- Ca(2+) sensor S100beta-modulated sites of membrane guanylate cyclase in the photoreceptor-bipolar synapse.The EMBO journal · 2002Article
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2 authors.
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Abstract
The EF-hand calcium-binding protein S100B has been shown to interact in vitro in a calcium-sensitive manner with many substrates. These potential S100B target proteins have been screened for the preservation of a previously identified consensus sequence across species. The results were compared to known structural and in vitro properties of the proteins to rationalize choices for potential binding partners. Our approach uncovered four oligomeric proteins tubulin (alpha and beta), glial fibrillary acidic protein (GFAP), desmin, and vimentin that have conserved regions matching the consensus sequence. In the type III intermediate filament proteins (GFAP, vimentin, and desmin), this region corresponds to a portion of a coiled-coil (helix 2A), the structural element responsible for their assembly. In tubulin, the sequence matches correspond to regions of alpha and beta tubulin found at the alpha beta tubulin interface. In both cases, these consensus sequence matches provide a logical explanation for in vitro observations that S100B is able to inhibit oligomerization of these proteins.
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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.