ReviewBiochimie2010
Metallo-aminopeptidase inhibitors.
Review in Biochimie, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
49 citing papers in PubMed.
- Synthesis and Evaluation of Peptoid-Based Compound Libraries as Inhibitors of Parasite Metallo-Aminopeptidases.ChemMedChem · 2026Article
- Harnessing tumor-associated exosomal aminopeptidase N as a dual-function tool for monitoring and tackling chemoresistance in gastric cancer.Cell communication and signaling : CCS · 2026Article
- Hydroxamate-based inhibitors reveal structural determinants of selectivity for Plasmodium falciparum aminopeptidase P.The Journal of biological chemistry · 2026Article
- Enhancing leucine aminopeptidase activity in Aspergillus oryzae LL1 through multi-round UV irradiation mutagenesis with potential application in debittering.Biotechnology letters · 2025Article
- Chemodiversity and Biotechnological Potential of Microginins.International journal of molecular sciences · 2025Review
- Comprehensive analysis through multi-omics integration to compare and elucidate the specific substances in milk of donkey、horse、camel、human and pig.Food chemistry: X · 2025Article
- Synthesis, biological and pharmacokinetic characterization of a novel leucine ureido derivative as a multi-target anticancer agent.RSC advances · 2025Article
- Destined for destruction: The role of methionine aminopeptidases and plant cysteine oxidases in N-degron formation.Plant physiology · 2024Review
- Quantifying and Controlling the Proteolytic Degradation of Cell Adhesion Peptides.ACS biomaterials science & engineering · 2024Article
- Naturally based pyrazoline derivatives as aminopeptidase N, VEGFR2 and MMP9 inhibitors: design, synthesis and molecular modeling.RSC advances · 2024Article
- Quantifying and controlling the proteolytic degradation of cell adhesion peptides.bioRxiv : the preprint server for biology · 2024Article
- Drug targeting of aminopeptidases: importance of deploying a right metal cofactor.Biophysical reviews · 2024Review
- The Role of Aminopeptidase ERAP1 in Human Pathology-A Review.Current issues in molecular biology · 2024Review
- Antiplasmodial Activity Evaluation of a Bestatin-Related Aminopeptidase Inhibitor, Phebestin.Antimicrobial agents and chemotherapy · 2023Article
- A Molecular Analysis of the Aminopeptidase P-Related Domain of PID-5 fromBiomolecules · 2023Article
- Combination Vaccines ofTropical medicine and infectious disease · 2023Article
- Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families.Marine drugs · 2023Review
- Article
- Development of Hydroxamate Derivatives Containing a Pyrazoline Moiety as APN Inhibitors to Overcome Angiogenesis.Molecules (Basel, Switzerland) · 2022Article
- Extracellular Vesicles fromToxins · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Aminopeptidases are enzymes that selectively hydrolyze an amino acid residue from the N-terminus of proteins and peptides. They are important for the proper functioning of prokaryotic and eukaryotic cells, but very often are central players in the devastating human diseases like cancer, malaria and diabetes. The largest aminopeptidase group include enzymes containing metal ion(s) in their active centers, which often determines the type of inhibitors that are the most suitable for them. Effective ligands mostly bind in a non-covalent mode by forming complexes with the metal ion(s). Here, we present several approaches for the design of inhibitors for metallo-aminopeptidases. The optimized structures should be considered as potential leads in the drug discovery process against endogenous and infectious diseases.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.