Positioning of aminopeptidase inhibitors in next generation cancer therapy

Aminopeptidases represent a class of (zinc) metalloenzymes that catalyze the cleavage of amino acids nearby the N-terminus of polypeptides, resulting in hydrolysis of peptide bonds. Aminopeptidases operate downstream of the ubiquitin–proteasome pathway and are implicated in the final step of intrace...

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Veröffentlicht in:	Amino acids Jg. 46; H. 4; S. 793 - 808
Hauptverfasser:	Hitzerd, Sarina M, Verbrugge, Sue Ellen, Ossenkoppele, Gert, Jansen, Gerrit, Peters, Godefridus J
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Vienna Springer-Verlag 01.04.2014 Springer Vienna Springer Nature B.V
Schlagworte:	Acute myeloid leukemia Amino acids Aminopeptidase Aminopeptidases - antagonists & inhibitors Aminopeptidases - genetics Aminopeptidases - metabolism Analytical Chemistry Animals Antigen presentation Antineoplastic Agents - administration & dosage Biochemical Engineering Biochemistry Biomedical and Life Sciences Cancer Cancer therapies Chemotherapy Clinical trials Data points Drug resistance drug therapy Drugs Effectiveness Endoplasmic reticulum Enzyme Inhibitors - administration & dosage free amino acids Health services Humans Hydrolysis Inhibitors Invited Review Leucine leucyl aminopeptidase Leukemia Life Sciences Lung cancer lung neoplasms mechanism of action membrane alanyl aminopeptidase myeloid leukemia N-Terminus Neoplasms - drug therapy Neoplasms - enzymology Neoplasms - genetics Neurobiology patients Peptides Polypeptides Position (location) Proteasomes Protein biosynthesis protein degradation Protein synthesis Proteins Proteomics Puromycin Ubiquitin Zinc Amino acids Aminopeptidase inhibitors Tosedostat Bestatin Aminopeptidases
ISSN:	0939-4451, 1438-2199, 1438-2199
Online-Zugang:	Volltext
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