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Bleomycin hydrolase

bleomycin hydrolase
Top mentioned proteins: aminopeptidase, ACID, CAN, fibrillin-1, HAD
Papers on bleomycin hydrolase
Design and Synthesis of Activity-Based Probes and Inhibitors for Bleomycin Hydrolase.
Bogyo et al., Stanford, United States. In Chem Biol, Sep 2015
Bleomycin hydrolase (BLMH) is a neutral cysteine aminopeptidase that has been ascribed roles in many physiological and pathological processes, yet its primary biological function remains enigmatic.
Skin dryness in apparently healthy human skin is associated with decreased expression of bleomycin hydrolase in the stratum corneum.
Lee et al., South Korea. In Clin Exp Dermatol, Apr 2015
Expression of the proteases caspase-14, calpain-1 and bleomycin hydrolase was measured by western blotting.
In a three-dimensional reconstructed human epidermis filaggrin-2 is essential for proper cornification.
Simon et al., Toulouse, France. In Cell Death Dis, 2014
However, we observed reduced proteolytic processing of corneodesmosin, hornerin and filaggrin in parallel with reduced amounts of caspase-14 and bleomycin hydrolase.
Histamine exerts multiple effects on expression of genes associated with epidermal barrier function.
Ogg et al., In J Investig Allergol Clin Immunol, 2013
Differential changes in filaggrin and the filaggrin-processing enzyme bleomycin hydrolase (BLMH) were validated at the protein level, and expression was also assessed in filaggrin knock-down keratinocytes.
Enhanced efficacy of bleomycin in bladder cancer cells by photochemical internalization.
Gederaas et al., Trondheim, Norway. In Biomed Res Int, 2013
Two additional strategies were explored to further enhance the cytotoxicity of bleomycin; a novel peptide drug ATX-101 which is known to impair DNA damage responses, and the protease inhibitor E-64 which may reduce bleomycin degradation by inhibition of bleomycin hydrolase.
Human valacyclovir hydrolase/biphenyl hydrolase-like protein is a highly efficient homocysteine thiolactonase.
Furlong et al., Seattle, United States. In Plos One, 2013
Human plasma paraoxonase-1 (PON1) and bleomycin hydrolase (Blmh) have been reported as the physiological HCTL detoxifying enzymes.
Variation in bleomycin hydrolase gene is associated with reduced survival after chemotherapy for testicular germ cell cancer.
Gietema et al., Groningen, Netherlands. In J Clin Oncol, 2008
A plausible candidate is the gene for bleomycin hydrolase (BLMH), an enzyme that inactivates bleomycin, an essential component of chemotherapy regimens for disseminated testicular germ-cell cancer (TC).
[Mechanisms that protect against homocysteine toxicity].
Zimny, Poznań, Poland. In Postepy Biochem, 2007
The third protective mechanism is the HcyTl hydrolysis catalyzed by intracellular enzyme known as bleomycin hydrolase.
Quantification of neutral cysteine protease bleomycin hydrolase and its localization in rat tissues.
Takeda et al., Sagamihara, Japan. In J Biochem, 2007
Blmh was localized as granular staining in the distal and proximal tubular cells of the kidney, and it was also detected in hepatocytes of the liver, in the red pulpy region of the spleen and in neurons of the brain.
Processing of amyloid beta-peptides by neutral cysteine protease bleomycin hydrolase.
Takeda et al., Sagamihara, Japan. In Protein Pept Lett, 2005
processing specificity of bleomycin hydrolase depends upon the structure and sequence of amyloid beta-peptides
Processing of antigenic peptides by aminopeptidases.
Tsujimoto et al., Wako, Japan. In Biol Pharm Bull, 2004
puromycin-sensitive aminopeptidase, bleomycin hydrolase and interferon-gamma-inducible leucine aminopeptidase) and recently identified metallo-aminopeptidase located in the endoplasmic reticulum (i.e.
Proteasome and peptidase function in MHC-class-I-mediated antigen presentation.
Ossendorp et al., Berlin, Germany. In Curr Opin Immunol, 2004
This is in part due to the existence of a panel of cytosolic aminopeptidases, such as bleomycin hydrolase (BH), puromycin-sensitive aminopeptidase (PSA) and thimet oligoendopeptidase (TOP), that can destroy epitopes or their precursors.
Beyond the proteasome: trimming, degradation and generation of MHC class I ligands by auxiliary proteases.
van Endert et al., Paris, France. In Mol Immunol, 2002
Several cytosolic enzymes, including bleomycin hydrolase (BH) and puromycin-sensitive aminopeptidase (PSA), but especially the IFNgamma-inducible leucyl aminopeptidase (LAP), can trim the aminoterminal ends of class I ligands.
[Genetics of late-onset Alzheimer's disease: vascular risk and beta-amyloid metabolism].
Capurso et al., Bari, Italy. In Recenti Prog Med, 2002
A number of genetic risk factors have been implicated that might increase the risk of developing sporadic disease: particularly, apolipoprotein E (apo E) polymorphism and many others suggested by linkage studies [alpha-macroglobulin, low density receptor protein (LRP1), bleomycin hydrolase], with a precise role in beta-amyloid metabolism and deposition.
Two new proteases in the MHC class I processing pathway.
Schild et al., Tübingen, Germany. In Nat Immunol, 2000
By using specific selective criteria we purified two cytosolic proteolytic activities, puromycin-sensitive aminopeptidase and bleomycin hydrolase.
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.
Joshua-Tor et al., Dallas, United States. In Cell, 1998
The Gal6 protease is in a class of cysteine peptidases identified by their ability to inactivate the anti-cancer drug bleomycin.
Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6.
Rees et al., Pasadena, United States. In Science, 1995
Bleomycin hydrolase is a cysteine protease that hydrolyzes the anticancer drug bleomycin.
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