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Carboxypeptidase Z

carboxypeptidase Z, Cpz, Carboxypeptidase Z is
This gene encodes a member of the metallocarboxypeptidase family. This enzyme displays carboxypeptidase activity towards substrates with basic C-terminal residues. It is most active at neutral pH and is inhibited by active site-directed inhibitors of metallocarboxypeptidases. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: carboxypeptidase, ACID, Frizzled, HAD, CAN
Papers on carboxypeptidase Z
Modulation of the COMT Val(158)Met polymorphism on resting-state EEG power.
Gutiérrez-Muñoz et al., León, Mexico. In Front Hum Neurosci, 2014
The resting EEG spectral absolute power in the frontal (F3, F4, F7, F8, FC3 and FC4), parietal (CP3, CP4, P3 and P4) and midline (Fz, FCz, Cz, CPz, Pz and Oz) was analyzed during the eyes-open and eyes-closed conditions.
Rate control and quality assurance during rhythmic force tracking.
Hwang et al., Taipei, Taiwan. In Behav Brain Res, 2014
Our results showed that frequency demand significantly affected EEG delta oscillation (1-4 Hz) in the C3, CP3, CPz, and CP4 electrodes, with the greatest delta power and lowest delta peak around 1.5 Hz for slower tracking at 0.5 Hz.
Microarray expression analysis of genes and pathways involved in growth plate cartilage injury responses and bony repair.
Xian et al., Adelaide, Australia. In Bone, 2012
Four major functional groupings of differentially expressed genes with known roles in skeletal development were identified across the time-course of bone bridge formation, including Wnt signalling (SFRP1, SFRP4, β-catenin, Csnk2a1, Tcf7, Lef1, Fzd1, Fzd2, Wisp1 and Cpz), BMP signalling (BMP-2, BMP-6, BMP-7, Chrd, Chrdl2 and Id1), osteoblast differentiation (BMP-2, BMP-6, Chrd, Hgn, Spp1, Axin2, β-catenin, Bglap2) and skeletal development (Chrd, Mmp9, BMP-1, BMP-6, Spp1, Fgfr1 and Traf6).
Central adaptations to repetitive grasping in healthy aging.
Earhart et al., East Orange, United States. In Brain Topogr, 2011
Significant interactions (P < 0.05) were observed for MRCPs recorded from mesial (FCz, Cz, CPz) and motor (C1, C3, Cz) electrode sites, with younger adults demonstrating significant increases in MRCP amplitude.
Carboxypeptidase Z (CPZ) links thyroid hormone and Wnt signaling pathways in growth plate chondrocytes.
Ballock et al., Cleveland, United States. In J Bone Miner Res, 2009
These data indicate that thyroid hormone may regulate terminal differentiation of growth plate chondrocytes in part by modulating Wnt signaling pathways through the induction of CPZ and subsequent CPZ-enhanced activation of Wnt-4.
Early and late auditory sensory gating: moderating influences from schizotypal personality, tobacco smoking status, and acute smoking.
Boutros et al., Blacksburg, United States. In Psychiatry Res, 2007
Midline and hemispheric sites were evaluated at frontal (F3/Fz/F4), fronto-central (FC3/FCz/FC4), central (C3/Cz/C4), centro-parietal (CP3/CPz/CP4), and parietal (P3/Pz/P4) regions.
Cortical activation following a balance disturbance.
McIlroy et al., Toronto, Canada. In Exp Brain Res, 2004
Average N1 measures at FCz, Cz, and CPz were comparable between active and passive tasks ( p>0.05).
Carboxypeptidase Z (CPZ) modulates Wnt signaling and regulates the development of skeletal elements in the chicken.
Eichele et al., Hannover, Germany. In Development, 2003
Carboxypeptidase Z (CPZ) is a secreted Zn-dependent enzyme whose biological function is largely unknown.
Genomic analysis of alachlor-induced oncogenesis in rat olfactory mucosa.
Aronow et al., Cincinnati, United States. In Physiol Genomics, 2003
Acute alachlor exposure caused upregulation of matrix metalloproteinases (MMP)-2 and -9, tissue inhibitor of metalloproteinase-1, carboxypeptidase Z, and other genes related to extracellular matrix homeostasis.
Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary.
Johnson et al., Nashville, United States. In J Histochem Cytochem, 2002
We have recently demonstrated carboxypeptidase E (CPE) and carboxypeptidase Z (CPZ) in the majority of adenohypophyseal cells with carboxypeptidase D (CPD) immunoreactivity largely confined to adrenocorticotrophs.
Carboxypeptidases from A to z: implications in embryonic development and Wnt binding.
Fricker et al., New York City, United States. In Cell Mol Life Sci, 2001
In this review, we focus on the recently discovered carboxypeptidase Z (CPZ).
Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues.
Fricker et al., New York City, United States. In J Biol Chem, 2000
Carboxypeptidase Z (CPZ) is a newly reported member of the metallocarboxypeptidase gene family, but unlike other members of this family, CPZ contains an N-terminal domain that has amino acid sequence similarity to Wnt-binding proteins.
Purification and characterization of human metallocarboxypeptidase Z.
Fricker et al., New York City, United States. In Biochem Biophys Res Commun, 1999
Carboxypeptidase Z (CPZ) is a recently discovered member of the metallocarboxypeptidase gene family that has an N-terminal domain related to the Wnt/wingless binding domain of frizzled receptors and other proteins.
Cloning, sequence analysis, and distribution of rat metallocarboxypeptidase Z.
Fricker et al., United States. In Dna Cell Biol, 1998
A cDNA encoding human carboxypeptidase Z (CPZ), a novel metallocarboxypeptidase, was recently cloned (Song and Fricker, J. Biol.
Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase.
Fricker et al., New York City, United States. In J Biol Chem, 1997
A novel cDNA, designated carboxypeptidase Z (CPZ), was identified based on its homology to known metallocarboxypeptidases.
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