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Matrix metallopeptidase 23B

MMP23, MMP23A, MMP22, MIFR, MMP21, matrix metalloproteinase-23, matrix metalloproteinase 23B
This gene (MMP23B) encodes a member of the matrix metalloproteinase (MMP) family, and it is part of a duplicated region of chromosome 1p36.3. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. This gene belongs to the more telomeric copy of the duplicated region. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, MMP-28, stromelysin-3, HAD, MMP-12
Papers on MMP23
A human laterality disorder caused by a homozygous deleterious mutation in MMP21.
Katsanis et al., Jerusalem, Israel. In J Med Genet, Dec 2015
RESULTS: We identified a homozygous 2 bp deletion in MMP21, encoding matrix metalloproteinase-21, as the sole coding mutation that segregated with the phenotype.
MMP21 is mutated in human heterotaxy and is required for normal left-right asymmetry in vertebrates.
Gordon et al., Paris, France. In Nat Genet, Nov 2015
By whole-exome sequencing, whole-genome sequencing and high-throughput cohort resequencing, we identified recessive mutations in MMP21 (encoding matrix metallopeptidase 21) in nine index cases with heterotaxy.
MMP and TIMP temporal gene expression during osteocytogenesis.
Farquharson et al., Adelaide, Australia. In Gene Expr Patterns, May 2015
Mmp2, Mmp23 and Mmp28 were decreased concurrent with mineralisation onset (P < 0.05*).
Tumor size, stage and grade alterations of urinary peptidome in RCC.
Magni et al., Monza, Italy. In J Transl Med, 2014
Among them, C1RL, A1AGx, ZAG2G, PGBM, MMP23, GP162, ADA19, G3P, RSPH3, DREB, NOTC2 SAFB2 and CC168 were identified.
Pseudomonas aeruginosa MifS-MifR Two-Component System Is Specific for α-Ketoglutarate Utilization.
Mathee et al., Miami, United States. In Plos One, 2014
MifS (PA5512) and MifR (PA5511) form one such TCS implicated in biofilm formation.
Domain structure and function of matrix metalloprotease 23 (MMP23): role in potassium channel trafficking.
Norton et al., Australia. In Cell Mol Life Sci, 2014
MMP23 is a member of the matrix metalloprotease family of zinc- and calcium-dependent endopeptidases, which are involved in a wide variety of cellular functions.
Melanoma expression of matrix metalloproteinase-23 is associated with blunted tumor immunity and poor responses to immunotherapy.
Krogsgaard et al., New York City, United States. In J Transl Med, 2013
BACKGROUND: Matrix metalloproteinase-23 (MMP-23) can block the voltage-gated potassium channel Kv1.3, whose function is important for sustained Ca(2+) signaling during T cell activation.
Matrix metalloproteinase gene expressions might be oxidative stress targets in gastric cancer cell lines.
Irmak-Yazicioglu et al., İstanbul, Turkey. In Chin J Cancer Res, 2013
We aimed to analyze the effect of the accumulation of oxidative stress in the gastric cancer MKN-45 and 23132/87 cells following hydrogen peroxide (H2O2) exposure on the expression patterns of MMP-1, MMP-3, MMP-7, MMP-9, MMP-10, MMP-11, MMP-12, MMP-14, MMP-15, MMP-17, MMP-23, MMP-28, and β-catenin genes.
Intracellular trafficking of the KV1.3 potassium channel is regulated by the prodomain of a matrix metalloprotease.
Chandy et al., Irvine, United States. In J Biol Chem, 2013
Here we report a novel metalloprotease-independent, channel-modulating function for the prodomain of MMP23 (MMP23-PD).
Microcolony formation by the opportunistic pathogen Pseudomonas aeruginosa requires pyruvate and pyruvate fermentation.
Sauer et al., Binghamton, United States. In Mol Microbiol, 2012
In the pathogen Pseudomonas aeruginosa, microcolony formation is dependent on the two-component regulator MifR, with mifR mutant biofilms exhibiting an overall thin structure lacking microcolonies, and overexpression of mifR resulting in hyper-microcolony formation.
Matrix metalloproteinase 14 and 19 expression is associated with thoracic aortic aneurysms.
Eriksson et al., Stockholm, Sweden. In J Thorac Cardiovasc Surg, 2012
RESULTS: We detected messenger RNA expression for gelatinases (MMP2 and MMP9), stromelysin 3 (MMP11), all membrane bound MMPs (MMP14, MMP15, MMP16, MMP17, MMP24, MMP25), MMP19, MMP21, and MMP28 in ascending aorta.
CD147 is required for matrix metalloproteinases-2 production and germ cell migration during spermatogenesis.
Chan et al., Shenzhen, China. In Mol Hum Reprod, 2011
Of the eight MMPs studied, MMP-2, MMP-7, MMP-9 and MMP-23 were detected to have changes in expression during testicular development, with MMP-2 showing the largest change.
The gene expression profile of matrix metalloproteinases and their inhibitors in children with Henoch-Schönlein purpura.
Lee et al., Seoul, South Korea. In Br J Dermatol, 2011
The duration of steroid administration was negatively correlated with MMP-1, MMP-2, MMP-7, MMP-10, MMP-12, MMP-19, MMP-23 and TIMP-1 levels (P < 0·05), suggesting a suppressive effect of steroids on the expressions of MMPs and TIMPs.
Expression changes and roles of matrix metalloproteinases in a rat model of traumatic deep vein thrombosis.
Zhang et al., Kunming, China. In Chin J Traumatol, 2010
The main outcome parameters measured included expressions of MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13, MMP-14, MMP-16, MMP-23 and MMP-24.
Identification of genes related to heart failure using global gene expression profiling of human failing myocardium.
Kitakaze et al., Ōsaka, Japan. In Biochem Biophys Res Commun, 2010
After the in vitro functional screening using adenovirus transfections of 12 genes into rat cardiomyocytes, we generated gene-targeting mice of five candidate genes, namely, MYLK3, GPR37L1, GPR35, MMP23, and NBC1.
Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development.
Takahashi et al., Sapporo, Japan. In Mol Endocrinol, 2001
Compares rat and human proteins, describes unique Type II membrane topology, and suggests a role in reproductive processes.
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