Re-emerging Aspartic Protease Targets: Examining
Antifungal Agents
/ chemistry
Aspartic Acid Proteases
/ antagonists & inhibitors
Binding Sites
Catalytic Domain
Cryptococcus neoformans
/ enzymology
Crystallography, X-Ray
Drug Evaluation, Preclinical
Fungal Proteins
/ antagonists & inhibitors
Fungi
/ drug effects
HIV
/ enzymology
HIV Protease
/ chemistry
Molecular Dynamics Simulation
Recombinant Proteins
/ biosynthesis
Structure-Activity Relationship
Substrate Specificity
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
27 05 2021
27 05 2021
Historique:
pubmed:
20
5
2021
medline:
22
6
2021
entrez:
19
5
2021
Statut:
ppublish
Résumé
Cryptococcosis is an invasive infection that accounts for 15% of AIDS-related fatalities. Still, treating cryptococcosis remains a significant challenge due to the poor availability of effective antifungal therapies and emergence of drug resistance. Interestingly, protease inhibitor components of antiretroviral therapy regimens have shown some clinical benefits in these opportunistic infections. We investigated Major aspartyl peptidase 1 (May1), a secreted
Identifiants
pubmed: 34006103
doi: 10.1021/acs.jmedchem.0c02177
pmc: PMC8165695
doi:
Substances chimiques
Antifungal Agents
0
Fungal Proteins
0
Recombinant Proteins
0
Aspartic Acid Proteases
EC 3.4.-
HIV Protease
EC 3.4.23.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6706-6719Subventions
Organisme : NIAID NIH HHS
ID : F32 AI152270
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI100272
Pays : United States
Organisme : NHLBI NIH HHS
ID : T32 HL007185
Pays : United States
Organisme : NIGMS NIH HHS
ID : P50 GM082250
Pays : United States
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