44 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
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Evaluation of transition-state mimics in a superior BACE1 cleavage sequence as peptide-mimetic BACE1 inhibitors.
Kyoto Pharmaceutical University
Inhibitors of melanogenesis in B16 melanoma 4A5 cells from flower buds of Lawsonia inermis (Henna).
Kyoto Pharmaceutical University
Optimization of plasmepsin inhibitor by focusing on similar structural feature with chloroquine to avoid drug-resistant mechanism of Plasmodium falciparum.
Kyoto Pharmaceutical University
Novel BACE1 inhibitors with a non-acidic heterocycle at the P1' position.
Kyoto Pharmaceutical University
Critical role of a methyl group on the¿-lactone ring of annonaceous acetogenins in the potent inhibition of mitochondrial complex I.
Kyoto Pharmaceutical University
Structures of new friedelane-type triterpenes and eudesmane-type sesquiterpene and aldose reductase inhibitors from Salacia chinensis.
Kyoto Pharmaceutical University
BACE1 inhibitors: optimization by replacing the P1' residue with non-acidic moiety.
Kyoto Pharmaceutical University
Truncation and non-natural amino acid substitution studies on HTLV-I protease hexapeptidic inhibitors.
Kyoto Pharmaceutical University
Identification of peptidomimetic HTLV-I protease inhibitors containing hydroxymethylcarbonyl (HMC) isostere as the transition-state mimic.
Kyoto Pharmaceutical University
Design and synthesis of new inhibitors of HIV-1 protease dimerization with conformationally constrained templates.
Kyoto Pharmaceutical University
Phytoestrogens from the roots of Polygonum cuspidatum (Polygonaceae): structure-requirement of hydroxyanthraquinones for estrogenic activity.
Kyoto Pharmaceutical University
Structure-guided design and synthesis of P1' position 1-phenylcycloalkylamine-derived pentapeptidic BACE1 inhibitors.
Kyoto Pharmaceutical University
Structural requirements of flavonoids for the adipogenesis of 3T3-L1 cells.
Kyoto Pharmaceutical University
Improvement of both plasmepsin inhibitory activity and antimalarial activity by 2-aminoethylamino substitution.
Kyoto Pharmaceutical University
Design of pentapeptidic BACE1 inhibitors with carboxylic acid bioisosteres at P1' and P4 positions.
Kyoto Pharmaceutical University
Melanogenesis inhibitors from the desert plant Anastatica hierochuntica in B16 melanoma cells.
Kyoto Pharmaceutical University
Melanogenesis inhibitors from the rhizomes of Alpinia officinarum in B16 melanoma cells.
Kyoto Pharmaceutical University
Significance of interactions of BACE1-Arg235 with its ligands and design of BACE1 inhibitors with P2 pyridine scaffold.
Kyoto Pharmaceutical University
Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin.
Kyoto Pharmaceutical University
Effects of amide constituents from pepper on adipogenesis in 3T3-L1 cells.
Kyoto Pharmaceutical University
Synthesis and activity of tetrapeptidic HTLV-I protease inhibitors possessing different P3-cap moieties.
Kyoto Pharmaceutical University
New flavonol oligoglycosides and polyacylated sucroses with inhibitory effects on aldose reductase and platelet aggregation from the flowers of Prunus mume.
Kyoto Pharmaceutical University
Additional interaction of allophenylnorstatine-containing tripeptidomimetics with malarial aspartic protease plasmepsin II.
Kyoto Pharmaceutical University
beta-Secretase inhibitors: modification at the P4 position and improvement of inhibitory activity in cultured cells.
Kyoto Pharmaceutical University
Design and synthesis of potent beta-secretase (BACE1) inhibitors with P1' carboxylic acid bioisosteres.
Kyoto Pharmaceutical University
Design and synthesis of highly active Alzheimer's beta-secretase (BACE1) inhibitors, KMI-420 and KMI-429, with enhanced chemical stability.
Kyoto Pharmaceutical University
Macrocyclic BACE1 inhibitors with hydrophobic cross-linked structures: Optimization of ring size and ring structure.
Kyoto Pharmaceutical University
Structure-activity relationship study of hydroxyethylamine isostere and P1' site structure of peptide mimetic BACE1 inhibitors.
Kyoto Pharmaceutical University
KMI-358 and KMI-370, highly potent and small-sized BACE1 inhibitors containing phenylnorstatine.
Kyoto Pharmaceutical University
KMI-008, a novel beta-secretase inhibitor containing a hydroxymethylcarbonyl isostere as a transition-state mimic: design and synthesis of substrate-based octapeptides.
Kyoto Pharmaceutical University
Design and synthesis of pseudo-symmetric HIV protease inhibitors containing a novel hydroxymethylcarbonyl (HMC)-hydrazide isostere.
Kyoto Pharmaceutical University
'Double-Drugs'--a new class of prodrug form of an HIV protease inhibitor conjugated with a reverse transcriptase inhibitor by a spontaneously cleavable linker.
Kyoto Pharmaceutical University
Structure-activity relationship studies of chloromethyl ketone derivatives for selective human chymase inhibitors.
Kyoto Pharmaceutical University
A new class of anti-HIV agents: synthesis and activity of conjugates of HIV protease inhibitors with a reverse transcriptase inhibitor.
Kyoto Pharmaceutical University
Adipogenetic effects of retrofractamide A derivatives in 3T3-L1 cells.
Kyoto Pharmaceutical University
Effects of 12 Ca2+ antagonists on multidrug resistance, MDR1-mediated transport and MDR1 mRNA expression.
Kyoto Pharmaceutical University
Structure-based design, synthesis, and evaluation of peptide-mimetic SARS 3CL protease inhibitors.
Kyoto Pharmaceutical University
Design and synthesis of several small-size HTLV-I protease inhibitors with different hydrophilicity profiles.
Kyoto Pharmaceutical University
Maintaining potent HTLV-I protease inhibition without the P3-cap moiety in small tetrapeptidic inhibitors.
Kyoto Pharmaceutical University
Small-sized human immunodeficiency virus type-1 protease inhibitors containing allophenylnorstatine to explore the S2' pocket.
Kyoto Pharmaceutical University
New developments for the design, synthesis and biological evaluation of potent SARS-CoV 3CL(pro) inhibitors.
Kyoto Pharmaceutical University
Locking the two ends of tetrapeptidic HTLV-I protease inhibitors inside the enzyme.
Kyoto Pharmaceutical University