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Cystatin B

cystatin B, stefin B, EPM1, CSTB
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and kininogens. This gene encodes a stefin that functions as an intracellular thiol protease inhibitor. The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The protein is thought to play a role in protecting against the proteases leaking from lysosomes. Evidence indicates that mutations in this gene are responsible for the primary defects in patients with progressive myoclonic epilepsy (EPM1). [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, Cystatins, Cathepsins, HAD, CAN
Papers on cystatin B
Efficient expression and purification of biologically active human cystatin proteins.
Tomar et al., Bhopāl, India. In Protein Expr Purif, Feb 2016
In this study, we cloned and expressed human stefin A, stefin B and cystatin C in Escherichia coli.
Simple Method To Prepare Oligonucleotide-Conjugated Antibodies and Its Application in Multiplex Protein Detection in Single Cells.
Ramakrishnan et al., San Francisco, United States. In Bioconjug Chem, Feb 2016
When tested using recombinant proteins, some antibody binders, such as those specific to CSTB, MET, EpCAM, and CASP3, had dynamic ranges of 5-6 logs.
Tissue Levels of Stefin A and Stefin B in Hepatocellular Carcinoma.
Xie et al., Putian, China. In Anat Rec (hoboken), Feb 2016
In this study, the protein levels of stefin A and stefin B were assessed by immunohistochemical staining, and the mRNA levels were quantified by real-time polymerase chain reaction in 85 primary HCC tissues, 85 surrounding non-cancerous tissues, and 9 normal hepatic tissues.
Brivaracetam in Unverricht-Lundborg disease (EPM1): Results from two randomized, double-blind, placebo-controlled studies.
von Rosenstiel et al., Kuopio, Finland. In Epilepsia, Jan 2016
OBJECTIVE: To evaluate efficacy, tolerability, and safety of adjunctive brivaracetam (BRV) in patients with Unverricht-Lundborg disease (EPM1).
Assembly of Stefin B into Polymorphic Oligomers Probed by Discrete Molecular Dynamics.
Urbanc et al., Ljubljana, Slovenia. In J Chem Theory Comput, Jun 2015
Assembly of an amyloidogenic protein stefin B into molten globule oligomers is studied by efficient discrete molecular dynamics.
Innate Immune Response in Brain, NF-Kappa B Signaling and Cystatins.
Kopitar-Jerala, Ljubljana, Slovenia. In Front Mol Neurosci, 2014
Type I cystatin stefin B (cystatin B) is an endogenous cysteine cathepsin inhibitor localized in the cytosol, mitochondria and nucleus.
The Role of Stefin B in Neuro-inflammation.
Kopitar-Jerala, Ljubljana, Slovenia. In Front Cell Neurosci, 2014
Stefin B (cystatin B) is an endogenous cysteine cathepsin inhibitor localized in the cytosol, mitochondria and nucleus.
Macrophage derived cystatin B/cathepsin B in HIV replication and neuropathogenesis.
Melendez et al., San Juan, Puerto Rico. In Curr Hiv Res, 2013
Our group recently showed that HIV replication in monocyte-derived macrophages is associated with increased cystatin B. This cysteine protease inhibitor also inhibits the interferon-induced antiviral response by decreasing levels of tyrosine phosphorylated STAT-1.
Progressive myoclonus epilepsy.
Minassian et al., Toronto, Canada. In Handb Clin Neurol, 2012
Unverricht-Lundborg disease is presently thought to be due to damage to neurons by lysosomal cathepsins and reactive oxygen species due to absence of cystatin B, a small protein that inactivates cathepsins and, by ways yet unknown, quenches damaging redox compounds.
The regulation of cysteine cathepsins and cystatins in human gliomas.
Lah et al., Ljubljana, Slovenia. In Int J Cancer, 2012
Elevated StefA mRNA level is associated with invasive glioblastoma.
RP-HPLC-ESI-MS evidenced that salivary cystatin B is detectable in adult human whole saliva mostly as S-modified derivatives: S-Glutathionyl, S-cysteinyl and S-S 2-mer.
Castagnola et al., Cagliari, Italy. In J Proteomics, 2012
S-glutathionylation and S-cysteinylation were described as extensive PTM of a salivary protein and the first time that these PTMs were detected in naturally occurring cystatin B.
Early microglial activation precedes neuronal loss in the brain of the Cstb-/- mouse model of progressive myoclonus epilepsy, EPM1.
Lehesjoki et al., Helsinki, Finland. In J Neuropathol Exp Neurol, 2012
Pathologic events in the CSTB-deficient brain highlight the potential role of glial activation at the initial stages of progressive myoclonic epilepsy type 1.
The cross-road between the mechanisms of protein folding and aggregation; study of human stefin B and its H75W mutant.
Žerovnik et al., Tuzla, Bosnia and Herzegovina. In Biochem Biophys Res Commun, 2011
At pH 7.0 the mutant H75W folded in three kinetic phases to a native-like intermediate, analogous to folding of stefin B at pH 4.8.
Characterization of PTZ-induced seizure susceptibility in a down syndrome mouse model that overexpresses CSTB.
Hérault et al., Illkirch-Graffenstaden, France. In Plos One, 2010
An increase in Cstb does not induce any spontaneous epileptic activity.
Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice.
Myers et al., Stanford, United States. In Nat Genet, 1998
Loss-of-function mutations in the gene (CSTB) encoding human cystatin B, a widely expressed cysteine protease inhibitor, are responsible for a severe neurological disorder known as Unverricht-Lundborg disease (EPM1).
Dodecamer repeat expansion in cystatin B gene in progressive myoclonus epilepsy.
Antonarakis et al., Genève, Switzerland. In Nature, 1997
Two point mutations in the cysteine proteinase inhibitor gene cystatin B (CSTB), proved that this gene is responsible for EPM1 (ref.
Unstable minisatellite expansion causing recessively inherited myoclonus epilepsy, EPM1.
Lehesjoki et al., Helsinki, Finland. In Nat Genet, 1997
6) and the refinement of the critical region to a small interval, positional cloning identified the gene encoding cystatin B (CST6), a cysteine protease inhibitor, as the gene underlying EPM1 (ref.
Unstable insertion in the 5' flanking region of the cystatin B gene is the most common mutation in progressive myoclonus epilepsy type 1, EPM1.
Rouleau et al., Montréal, Canada. In Nat Genet, 1997
Recently, two mutations in the cystatin B gene (also known as stefin B, STFB) mapping to 21q22.3 have been implicated in the EPM1 phenotype: a G-->C substitution in the last nucleotide of intron 1 that was predicted to cause a splicing defect in one family, and a C-->T substitution that would change an Arg codon (CGA) to a stop codon (TGA) at amino acid position 68, resulting in a truncated cystatin B protein in two other families.
Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1)
Myers et al., Stanford, United States. In Science, 1996
Two mutations, a 3' splice site mutation and a stop codon mutation, were identified in the gene encoding cystatin B in EPM1 patients but were not present in unaffected individuals.
Progressive myoclonus epilepsy: Unverricht-Lundborg disease and Neuronal ceroid lipofuscinoses
Gardiner et al., Bethesda, United States. In Unknown Journal, 0001
The main gene underlying EPM1, CSTB, encodes Cystatin B, a cysteine protease inhibitor.
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