Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Critical role of amino acid 23 in mediating activity and specificity of vinckepain-2, a papain-family cysteine protease of rodent malaria parasites.

The Biochemical journal - 15 Nov 2002

Singh Ajay, Shenai Bhaskar R, Choe Youngchool, Gut Jiri, Sijwali Puran S, Craik Charles S, Rosenthal Philip J

Abstract excerpt

Cysteine proteases of Plasmodium falciparum, known as falcipains, have been identified as haemoglobinases and potential drug targets. As anti-malarial drug discovery requires the analysis of non-primate malaria, genes encoding related cysteine proteases of the rodent malaria parasites P. vinckei (vinckepain-2) and P. berghei (berghepain-2) were characterized. These genes encoded fairly typical papain-family...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cysteine Endopeptidases
Share to Helminth Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Malaria

Share to Papain

Share to Peptide Library

Share to Plasmodium falciparum

Share to Rodent Diseases

Share to Rodentia

Source

Open in PubMed Open full text

Identifiers

PMID: 12169096
DOI: 10.1042/BJ20020753
PMCID: PMC1222974

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Critical role of amino acid 23 in mediating activity and specificity of vinckepain-2, a papain-family cysteine protease of rodent malaria parasites.PMID 12169096Read ↗

The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif.Semantic proximity Read ↗

Hemoglobin Degrading Proteases of Plasmodium falciparum as Antimalarial Drug Targets.Semantic proximity Read ↗

Evaluation of cysteine proteases of Plasmodium vivax as antimalarial drug targets: sequence analysis and sensitivity to cysteine protease inhibitors.Semantic proximity Read ↗

Mapping the substrate sequence and length of the <i>Plasmodium</i> M1 and M17 aminopeptidasesSemantic proximity Read ↗

Dual role of an essential HtrA2/Omi protease in the human malaria parasite: maintenance of mitochondrial homeostasis and induction of apoptosis like cell death under cellular stressSemantic proximity Read ↗

Cross-talk between malarial cysteine proteases and falstatin: the BC loop as a hot-spot target.Semantic proximity Read ↗

Trypanosoma Cruzi Presenilin-like Transmembrane Aspartyl Protease: Characterization and Cellular LocalizationSemantic proximity Read ↗

Dissecting The role of Plasmodium metacaspase-2 in malaria gametogenesis and sporogonySemantic proximity Read ↗

Expression and alteration of the S2 subsite of the Leishmania major cathepsin B-like cysteine protease.Semantic proximity Read ↗

Roles of Tyr13 and Phe219 in the unique substrate specificity of pepsin B.Semantic proximity Read ↗

Modeling and resistant alleles explain the selectivity of antimalarial compound 49c towards apicomplexan aspartyl proteases.Semantic proximity Read ↗

Accelerated evolution in the reactive centre regions of serine protease inhibitors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.