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MPP11, PMPCB, M-phase phosphoprotein 11, betaMPP
This gene is a member of the peptidase M16 family and encodes a protein with a zinc-binding motif. This protein is located in the mitochondrial matrix and catalyzes the cleavage of the leader peptides of precursor proteins newly imported into the mitochondria, though it only functions as part of a heterodimeric complex. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PRAME, HSP70, carbonic anhydrase IX, MPP, CAN
Papers on MPP11
Distinct methylation patterns in genes that affect mitochondrial function are associated with kidney disease in blood-derived DNA from individuals with Type 1 diabetes.
McKnight et al., Belfast, United Kingdom. In Diabet Med, Aug 2015
Three genes, PMPCB, TSFM and AUH, were observed with differential methylation at multiple Cytosine-phosphate-Guanine sites each (P < 10(-12) ).
Genomic analysis of stress response against arsenic in Caenorhabditis elegans.
Cinar et al., Laurel, United States. In Plos One, 2012
FastMEDUSA analysis identified cancer-related genes, particularly genes associated with leukemia, such as dnj-11, which encodes a protein orthologous to the mammalian ZRF1/MIDA1/MPP11/DNAJC2 family of ribosome-associated molecular chaperones.
Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment.
Fon et al., Montréal, Canada. In Embo Rep, 2012
These results highlight a new role for MPP in PINK1 import and mitochondrial quality control via the PINK1-Parkin pathway.
M-phase phosphoprotein 11 is a highly immunogenic tumor antigen in patients with acute myeloid leukemia.
Zeis et al., Hamburg, Germany. In Acta Haematol, 2011
the majority of AML patients elicited a humoral immune response against the tumor antigen MPP11
The chaperone network connected to human ribosome-associated complex.
Rospert et al., Freiburg, Germany. In Mol Cell Biol, 2011
Mammalian ribosome-associated complex (mRAC), consisting of the J-domain protein MPP11 and the atypical Hsp70 homolog (70-homolog) Hsp70L1, can partly complement the function of RAC, which is the homologous complex from Saccharomyces cerevisiae.
Transcriptional activation of polycomb-repressed genes by ZRF1.
Di Croce et al., Barcelona, Spain. In Nature, 2011
At the onset of differentiation, ZRF1 specifically displaces polycomb-repressive complex 1 (PRC1) from chromatin and facilitates transcriptional activation
Definition of a target for immunotherapy and results of the first Peptide vaccination study in chronic lymphocytic leukemia.
Giannopoulos et al., Lublin, Poland. In Transplant Proc, 2010
RHAMM/CD168, fibromodulin, PRAME, and MPP11 were expressed in CLL patients but not in healthy volunteers.
Identification of a novel peptide derived from the M-phase phosphoprotein 11 (MPP11) leukemic antigen recognized by human CD8+ cytotoxic T lymphocytes.
Dermime et al., Riyadh, Saudi Arabia. In Hematol Oncol Stem Cell Ther, 2009
describe a novel epitope derived from the MPP11 antigen that has been recognized by human CD8+ CTL
Autocatalytic processing of m-AAA protease subunits in mitochondria.
Langer et al., Köln, Germany. In Mol Biol Cell, 2009
Data show that Afg3l1 or Afg3l2 are required for maturation of newly imported paraplegin subunits after their cleavage by MPP.
Reductive evolution of the mitochondrial processing peptidases of the unicellular parasites trichomonas vaginalis and giardia intestinalis.
Tachezy et al., Praha, Czech Republic. In Plos Pathog, 2008
By contrast, and so far uniquely among eukaryotes, the Giardia processing peptidase functions as a monomer comprising a single betaMPP-like catalytic subunit.
Acute lymphoblastic leukemia-derived dendritic cells express tumor associated antigens: PNPT1, PMPCB, RHAMM, BSG and ERCC1.
Chyczewski et al., Białystok, Poland. In Neoplasma, 2008
maintained expression and even up-regulation of some (PNPT1, PMPCB, HMMR/RHAMM, BSG and ERCC1) tumor associated antigens in CD40-activated leukemic cells.
Characterization of gene expression regulated by American ginseng and ginsenoside Rg3 in human colorectal cancer cells.
Yuan et al., Chicago, United States. In Int J Oncol, 2008
To validate the microarray data, quantitative real-time PCR of six candidate target genes was conducted, whereby it was found that three genes were up-regulated (AKAPA8L, PMPCB and PDE5A) and three were down-regulated (PITPNA, DUS2L and RIC8A).
A functionally divergent hydrogenosomal peptidase with protomitochondrial ancestry.
Johnson et al., Los Angeles, United States. In Mol Microbiol, 2007
Matrix proteins of mitochondria, hydrogenosomes and mitosomes are typically targeted and translocated into their respective organelles using N-terminal presequences that are subsequently cleaved by a peptidase.
C/EBPalphap30 plays transcriptional regulatory roles distinct from C/EBPalphap42.
Hu et al., Shanghai, China. In Cell Res, 2007
By expression profiling, it was revealed that C/EBPalphap30 specifically inhibited a unique set of genes, including MPP11, p84N5 and SMYD2, which were not affected by C/EBPalphap42 in both QSG-7701 hepatocyte cell line and QGY-7703 hepatoma cells.
Chronic myeloid leukemia cells express tumor-associated antigens eliciting specific CD8+ T-cell responses and are lacking costimulatory molecules.
Greiner et al., Ulm, Germany. In Exp Hematol, 2006
Several LAAs are expressed in CML and therefore are candidate structures for specific immunotherapies: bcr-abl (100%), G250 (24%), hTERT (53%), MPP11 (91%), NEWREN60 (94%), PRAME (62%), Proteinase3 (71%), RHAMM/CD168 (83%), and WT1 (53%), but not BAGE, MAGE-A1, SSX2, or NY-ESO-1.
Expression of RHAMM/CD168 and other tumor-associated antigens in patients with B-cell chronic lymphocytic leukemia.
Schmitt et al., Ulm, Germany. In Int J Oncol, 2006
We screened the mRNA expression of tumor-associated antigens (TAAs) from the literature (fibromodulin, survivin, OFA-iLRP, BAGE, G250, MAGE1, PRAME, proteinase, syntaxin, hTERT, WT-1) and TAAs defined previously by serological analysis of cDNA expression libraries from leukemic cells (PINCH, HSJ2, MAZ, MPP11, RHAMM/CD168, NY-Ren60).
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex.
Rospert et al., Freiburg, Germany. In Proc Natl Acad Sci U S A, 2005
MPP11 is localized to the cytosol and with Hsp70L1, forms the mammalian ribosome-associated complex.
Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous.
Craig et al., Madison, United States. In Science, 2005
concluded that Mpp11, an ortholog of yeast Zuo, is a ribosome-associated J protein; proposed that in metazoans, ribosome-associated Zuo and Mpp11 orthologs recruit cytosolic Hsc70 to short ribosome-bound nascent chains as they exit the ribosome
mRNA expression of leukemia-associated antigens in patients with acute myeloid leukemia for the development of specific immunotherapies.
Schmitt et al., Ulm, Germany. In Int J Cancer, 2004
The following antigens showed high mRNA expression in AML patients: MPP11 was detected in 43/50 (86%), RHAMM in 35/50 (70%), WT1 in 40/60 (67%), PRAME in 32/50 (64%), G250 in 18/35 (51%), hTERT in 7/25 (28%) and BAGE in 8/30 (27%) of AML patients.
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