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Organic Azide Inhibitors of Cysteine Proteases
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1099-1352(199911/12)12:6<363::aid-jmr478>3.0.co;2-mopenalex-snapshot
Conformational homogeneity in molecular recognition by proteolytic enzymes
inferredcites →https://doi.org/10.1002/1521-3765(20020503)8:9<1976::aid-chem1976>3.0.co;2-kopenalex-snapshot
Pharmacophore Features of Potential Drugs
inferredcites →https://doi.org/10.1016/j.bmcl.2005.01.045openalex-snapshot
Discovery and SAR studies of a novel series of noncovalent cathepsin S inhibitors
inferredcites →https://doi.org/10.1016/s0021-9258(18)77334-1openalex-snapshot
Substrate specificity of the protease that processes human interleukin-1 beta.
inferredcites →https://doi.org/10.1016/s0960-894x(03)00344-5openalex-snapshot
Arylaminoethyl amides as inhibitors of the cysteine protease cathepsin K—investigating P1′ substituents
inferredcites →https://doi.org/10.1016/s1056-8719(00)00107-6openalex-snapshot
Drug-like properties and the causes of poor solubility and poor permeability
inferredcites →https://doi.org/10.1016/s1359644602025722openalex-snapshot
Nonleadlikeness and leadlikeness in biochemical screening
inferredcites →https://doi.org/10.1021/cr010182vopenalex-snapshot
Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
inferredcites →https://doi.org/10.1021/jm000060fopenalex-snapshot
Caspases as Targets for Anti-Inflammatory and Anti-Apoptotic Drug Discovery
inferredcites →https://doi.org/10.1021/jm010801sopenalex-snapshot
Arylaminoethyl Amides as Novel Non-Covalent Cathepsin K Inhibitors
inferredcites →https://doi.org/10.1021/jm020017nopenalex-snapshot
Molecular Properties That Influence the Oral Bioavailability of Drug Candidates
inferredcites →https://doi.org/10.1021/jm020238topenalex-snapshot
Design of Noncovalent Inhibitors of Human Cathepsin L. From the 96-Residue Proregion to Optimized Tripeptides
inferredcites →https://doi.org/10.1021/jm0496133openalex-snapshot
Nonpeptidic, Noncovalent Inhibitors of the Cysteine Protease Cathepsin S
inferredcites →https://doi.org/10.1021/jm990315topenalex-snapshot
Conformational Selection of Inhibitors and Substrates by Proteolytic Enzymes: Implications for Drug Design and Polypeptide Processing
inferredcites →https://doi.org/10.1021/jm990412mopenalex-snapshot
Protease Inhibitors: Current Status and Future Prospects
inferredcites →https://doi.org/10.1038/370270a0openalex-snapshot
Structure and mechanism of interleukin-lβ converting enzyme
inferredcites →https://doi.org/10.1038/nature02780openalex-snapshot
Variable ageing and storage of dissolved organic components in the open ocean
inferredcites →https://doi.org/10.1038/nature02791openalex-snapshot
Chemical remodelling of cell surfaces in living animals
inferredcites →https://doi.org/10.1038/nrd1342openalex-snapshot
Targeting IL-1 in inflammatory disease: new opportunities for therapeutic intervention
inferredcites →https://doi.org/10.1038/nsb0796-619openalex-snapshot
The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis
inferredcites →https://doi.org/10.2174/0929867024606704openalex-snapshot
Thiol-Dependent Enzymes and Their Inhibitors: A Review
inferredcites →https://doi.org/10.2174/1573406053402569openalex-snapshot
Protease Inhibitors in the Clinic
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4176343openalex-extracted
Mechanism-Based Inhibition of GH127/146 Cysteine Glycosidase by Stereospecifically Functionalized L-Arabinofuranosides
inferred← citeshttps://doi.org/10.1002/ange.202318773openalex-snapshot
Direct Activation of Nucleobases with Small Molecules for the Conditional Control of Antisense Function
inferred← citeshttps://doi.org/10.1002/anie.202318773openalex-snapshot
Direct Activation of Nucleobases with Small Molecules for the Conditional Control of Antisense Function
inferred← citeshttps://doi.org/10.1002/chem.201603150openalex-snapshot
Fused Bicyclic Caspase‐1 Inhibitors Assembled by Copper‐Free Strain‐Promoted Alkyne–Azide Cycloaddition (SPAAC)
inferred← citeshttps://doi.org/10.1002/cmdc.200900531openalex-snapshot
A Highly Potent and Selective Caspase 1 Inhibitor that Utilizes a Key 3‐Cyanopropanoic Acid Moiety
inferred← citeshttps://doi.org/10.1002/ejoc.201001227openalex-snapshot
Ionic Liquid Brush as a Highly Efficient and Reusable Catalyst for On‐Water Nucleophilic Substitutions
inferred← citeshttps://doi.org/10.1002/jms.1940openalex-snapshot
Azidoacetone as a complexing agent of transition metals Ni2+/Co2+ promoted dissociation of the CC bond in azidoacetone
inferred← citeshttps://doi.org/10.1002/qua.22332openalex-snapshot
Reaction mechanism of cysteine proteases model compound HSH with diketone inhibitor PhCOCOCH3−nXn, (X = F, Cl,n= 0, 1, 2)
inferred← citeshttps://doi.org/10.1002/rcm.3397openalex-snapshot
Study of doubly charged alkaline earth metal and 3‐azidopropionitrile complexes by electrospray ionization mass spectrometry
inferred← citeshttps://doi.org/10.1002/rcm.7877openalex-snapshot
An electrospray ionization mass spectrometry study of azidoacetic acid/transition metal complexes
inferred← citeshttps://doi.org/10.1007/s00253-013-4886-xopenalex-snapshot
Microbial transglutaminase displays broad acyl-acceptor substrate specificity
inferred← citeshttps://doi.org/10.1016/j.bmc.2009.03.026openalex-snapshot
Synthesis and biological evaluation of reversible inhibitors of IdeS, a bacterial cysteine protease and virulence determinant
inferred← citeshttps://doi.org/10.1016/j.bmc.2022.117054openalex-snapshot
Mechanism-based inhibition of GH127/146 cysteine glycosidases by stereospecifically functionalized l-arabinofuranosides
inferred← citeshttps://doi.org/10.1016/j.ejmech.2023.115861openalex-snapshot
Interleukin-1β converting enzyme (ICE): A comprehensive review on discovery and development of caspase-1 inhibitors
inferred← citeshttps://doi.org/10.1016/j.ijms.2013.05.012openalex-snapshot
Gas-phase interaction between nickel (II) and nitrobenzyl azides: An ESI-MSn study
inferred← citeshttps://doi.org/10.1016/j.jorganchem.2007.05.052openalex-snapshot
Zirconium-catalyzed methylalumination of heterosubstituted arylethynes: Factors affecting the regio-, stereo-, and chemoselectivities
inferred← citeshttps://doi.org/10.1016/j.pharmthera.2011.07.003openalex-snapshot
Allosteric modulation of caspases
inferred← citeshttps://doi.org/10.1016/j.trac.2023.117337openalex-snapshot
Recent advances in fluorescence biosensor for caspase detecting and imaging in biomedical applications
inferred← citeshttps://doi.org/10.1021/acsami.7b14845openalex-snapshot
Caspase-1 Specific Light-Up Probe with Aggregation-Induced Emission Characteristics for Inhibitor Screening of Coumarin-Originated Natural Products
inferred← citeshttps://doi.org/10.1021/ci800101jopenalex-snapshot
Discovery of Novel Cathepsin S Inhibitors by Pharmacophore-Based Virtual High-Throughput Screening
inferred← citeshttps://doi.org/10.1021/jacs.1c08060openalex-snapshot
Discovery of Di- and Trihaloacetamides as Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity
inferred← citeshttps://doi.org/10.1021/jm901790wopenalex-snapshot
Noncovalent Tripeptidyl Benzyl- and Cyclohexyl-Amine Inhibitors of the Cysteine Protease Caspase-1
inferred← citeshttps://doi.org/10.1021/ol800575zopenalex-snapshot
Solid-Phase Synthesis of Azidomethylene Inhibitors Targeting Cysteine Proteases
inferred← citeshttps://doi.org/10.1039/b708134kopenalex-snapshot
Unexpected photolytic decomposition of alkyl azides under mild conditions
inferred← citeshttps://doi.org/10.7314/apjcp.2014.15.23.10137openalex-snapshot
An in silico Appraisal to Identify High Affinity Anti-Apoptotic Synthetic Tetrapeptide Inhibitors Targeting the Mammalian Caspase 3 Enzyme
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