Pepstatin, a new pepsin inhibitor produced by Actinomycetes
about
Interaction of human cathepsin D with the inhibitor pepstatinStructure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparumInfluence of culture medium pH and proteinase inhibitors on extracellular proteinase activity and cell growth of Sporothrix schenckiiHuman immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin ADirect observation by X-ray analysis of the tetrahedral “intermediate” of aspartic proteinasesThe Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-ray DiffractionCrystal Structures of the Histo-Aspartic Protease (HAP) from Plasmodium falciparumCrystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparumStructural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus proteaseHigh-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzymeX-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsinThe aspartic proteasesNew renin inhibitors homologous with pepstatinEvolution in the structure and function of aspartic proteasesDouble-blind randomised clinical trial of a pepsin-inhibitory pentapeptide (pepstatin) in the treatment of duodenal ulcerSynthesis and biological activity of new conformationally restricted analogues of pepstatinHistamine release from human basophils by pepstatin AStudies on new intracellular proteases in various organs of rat. 1. Purification and comparison of their propertiesComparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problemProtease inhibitors from marine actinobacteria as a potential source for antimalarial compoundDiscovery of New Compounds Active against Plasmodium falciparum by High Throughput Screening of Microbial Natural ProductsEsterase mutation is a mechanism of resistance to antimalarial compoundsGrassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation.Distribution of productive antigen-processing activity for MHC class II presentation in macrophages.Construction of a small peptide library related to inhibitor OM99-2 and its structure-activity relationship to beta-secretase.A genomic survey of proteases in Aspergilli.Autophagy defends pancreatic β cells from human islet amyloid polypeptide-induced toxicityThyroid hormones control lysosomal enzyme activities in liver and skeletal muscle.Comparative aspects of development and differentiation in actinomycetesCytotaxin receptors of neutrophils: evidence that F-methionyl peptides and pepstatin share a common receptorNew families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.Inhibition of cathepsin D-type proteinase of macrophages by pepstatin, a specific pepsin inhibitor, and other substances.Purification and properties of the cathepsin D types proteinase from beef and rabbit lung and its identification in macrophages.Autophagy upregulation by inhibitors of caspase-3 and mTOR enhances radiotherapy in a mouse model of lung cancer.Samarium iodide-mediated Reformatsky reactions for the stereoselective preparation of β-hydroxy-γ-amino acids: synthesis of isostatine and dolaisoleucineFermentation, Isolation, Structure, and antidiabetic activity of NFAT-133 produced by Streptomyces strain PM0324667M-opsin protein degradation is inhibited by MG-132 in Rpe65⁻/⁻ retinal explant cultureThe Apaf-1-binding protein Aven is cleaved by Cathepsin D to unleash its anti-apoptotic potentialConformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.Comparative modeling of proteins in the design of novel renin inhibitors.
P2860
Q24530145-D8C2347C-1173-4E69-8DD5-9501026EBD00Q24597864-87C0F93D-24ED-4149-97D0-A20E2B819A26Q24646088-6AE63ACA-E06A-4031-BAE6-58AB76E23918Q24649411-ABD5C1A5-76A8-44D1-AED9-389DCECE02FBQ27642040-0A095721-0CBE-4C6B-A7BB-E6448E48E2D9Q27650602-0CA1DBD3-82C3-40B2-8CB8-C3838B5EACECQ27654096-ABF115BD-73F3-4541-9563-171FF7C54565Q27667575-B9DD2068-79EC-4087-9141-645C2DB59391Q27674531-D33E086B-EF9E-4958-A247-979790052D17Q27703612-DB00C3C4-8D92-47A9-8AC6-294F973ECAC9Q27732078-3638EFE1-5C64-4B73-80E0-5C29E1FFE173Q28208915-9275CF36-ED70-499C-9C7B-E53134E58E57Q28277281-9C4EEC9D-8549-4657-9F87-CFCF47DEE262Q28300400-34BDA3EF-C8E3-428A-AD9A-53113BB78006Q28305750-8F6B9D03-1787-4B48-A86B-8022F884EE82Q28318009-C5248FCF-5DA7-4175-95C5-6CA0BE4C9D00Q28336400-9C7C7C8D-FA4B-45DE-9D9C-2D572ECA4D0BQ28339654-6FA35E35-79D1-499C-9881-6FCBC8C6DBAEQ28378131-6A6462B5-63B2-461D-889F-7C54750E0943Q28540732-D9766876-25D3-491A-8178-2786E854F99AQ28552116-012240EE-82DC-4E00-9194-E4A5C7B3FB6EQ30043987-476F865B-E6E5-4814-8B9E-68F99799E646Q30479486-647BC779-C4A7-4F03-ACE6-5D42B4A76031Q33223830-3FBE833F-779F-466F-9D0F-9A5F511F0A72Q33263969-A31C4520-C7B4-4CC5-ACFB-2807AEE4D1A6Q33917250-61C67A34-BF88-474C-8124-0B29509AB01EQ33944212-DB5C8C7F-6E30-441D-A31C-86E1A2D67785Q33968162-10FA5704-3C56-4AC0-AC0D-BF8DC1B547BAQ34071770-BC282BF9-AE83-417F-A504-223A456D8BAAQ34100237-3F691125-D9DA-4817-ACC2-3B2B3DC24484Q34226050-3B6A9038-1A29-4AAC-BE5F-1B1EC538391BQ34487764-DB183BD7-369D-4B1C-BDEB-A4D3F62808A4Q34499564-6A869259-EAD0-413D-9304-F832497255D9Q34775716-1E59198E-468A-4398-94E4-18FBEE64DAA0Q35676583-1125E959-8739-4081-B5CF-0C23EB38AE03Q35742182-839E35FA-9304-4672-B2B0-289B5BA51474Q36051615-B3A2F77D-6706-47E4-AFA1-786B75547C11Q36174027-442F0672-22BA-4A7D-AC05-01BB932E6CB3Q36315424-3650948F-CC90-45F7-ABA1-5BF9DC2261D5Q37253693-D964535C-9F45-46B7-B879-40468E5CE92A
P2860
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
description
1970 nî lūn-bûn
@nan
1970 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1970 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1970年の論文
@ja
1970年論文
@yue
1970年論文
@zh-hant
1970年論文
@zh-hk
1970年論文
@zh-mo
1970年論文
@zh-tw
1970年论文
@wuu
name
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@ast
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@en
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@nl
type
label
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@ast
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@en
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@nl
prefLabel
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@ast
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@en
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@nl
P2093
P1476
Pepstatin, a new pepsin inhibitor produced by Actinomycetes
@en
P2093
P304
P356
10.7164/ANTIBIOTICS.23.259
P407
P577
1970-05-01T00:00:00Z