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Serine proteases protease inhibitors

Fig. 9. Large interfaces in serine protease—protease inhibitor complexes. Trypsin and thrombin are evolutionarily related serine proteases of approximately the same size. The 58-residue PTI binds at the active site and makes with trypsin a standard size interface. Ornithodorin and hirudin are thrombin inhibitors that make a large interface with the enzyme. Ornithodorin is a duplicate of PTI hirudin has an extended C-terminal tail that is disordered in solution. Fig. 9. Large interfaces in serine protease—protease inhibitor complexes. Trypsin and thrombin are evolutionarily related serine proteases of approximately the same size. The 58-residue PTI binds at the active site and makes with trypsin a standard size interface. Ornithodorin and hirudin are thrombin inhibitors that make a large interface with the enzyme. Ornithodorin is a duplicate of PTI hirudin has an extended C-terminal tail that is disordered in solution.
A number of inhibitors of FAAH have been synthesized (207), and the more potent of these are depicted in Fig. 5.16. The most potent compounds contain a highly electrophilic carbonyl as part of either an a-ketoester, a-ke-toamide of trifluoromethyl ketone moiety, structural features common to serine/cysteine protease inhibitors. Several of these FAAH inhibitors caused sleep enhancement and lowering of body temperature in rats that were comparable with those induced by oleamide. Based on these findings, it has been suggested that FAAH may represent a therapeutic target for... [Pg.254]

Study of heparin binding to thrombin, 56 low-density lipoproteins, lipoprotein lipase, circulatory serine proteases, proteinase inhibitors, heparin-binding growth factors, blood vessel-associated proteins (fibronectin and laminin) and binding to cells and tissues. Study of anticoagulant activity and the modulation of the structure, function and metabolism of many proteins and en-2ymes. [Pg.622]

Sequences have been determined for plasminogen and bovine Factor XII, and they are not homologous with the other serine proteases. The amino-terminal sequence of Factor XII is homologous, however, with the active site of several naturally occurring protease inhibitors (11). [Pg.173]

An example of a pseudoirreversible inhibitor has been demonstrated for chymotrypsin (36). This enzyme is a serine protease, and its mechanism of catalysis may be outlined as follows, where or R2 preferentially is a hydrophobic amino acid residue. [Pg.324]

James, M.N.G., et al. Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. A model for serine protease catalysis. [Pg.220]

Maspin (Mammary serine protease inhibitor) Induces EC apoptosis... [Pg.85]

More than 50 endogenous and exogenous inhibitors of the calpains have been described as either transition-state reversible or irreversible inhibitors. The first transition-state inhibitors were the peptide aldehydes (e.g., leupeptin). Using this compound, new ones were synthesized that exhibited improved membrane permeability and calpain specificity (e.g., calpeptin). Other groups of inhibitors have since been discovered a-dicarbonyls (originally developed as serine protease inhibitors), nonpeptide quinolinecarboxamides,... [Pg.313]

The quantification of kinins in human tissues or body fluids has been limited due to the inherent difficulties in accurately measuring the concentration of ephemeral peptides. Today HPLC-based and RIA/capture-ELA measurements are established to determine kinins in human plasma, liquor or mine. Serine protease inhibitors need to be added to prevent rapid degradation of the kinins in vitro during sample preparation. Kinins and their degradation products have been studied in various biological milieus such as plasma/ serum, urine, joint fluids, kidney, lung and skeletal muscle [2]. Under normal conditions, the concentration of kinins in these compartments is extremely low for... [Pg.673]

Steinkiihler C, Koch U, Narjes F et al (2001) Hepatitis C vims serine protease inhibitors current progress and future challenges. CurrMedChem 8 919-932... [Pg.1287]

Chen KX, Njoroge FG, Arasappan A, Venkatraman S, Vibulbhan B, Yang W, Parekh TN, Pichardo J, Prongay A, Cheng KC, Butkiewicz N, Yao N, Madison V, Girijavallabhan V (2006) Novel potent hepatitis C vims NS3 serine protease inhibitors derived from proline-based macrocycles, J Med Chem 49 995-1005... [Pg.46]

Lin C, Lin K, Luong YP, Rao BG, Wei YY, Brennan DL, Fulghum JR, Hsiao HM, Ma S, Maxwell JP, Cottrell KM, Pemi RB, Gates CA, Kwong AD (2004) In vitro resistance studies of hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061 structural analysis indicates different resistance mechanisms. J Biol Chem 279 17508-17514... [Pg.49]

Mo H, Lu L, Pilot-Matias T, PithawaUa R, Mondal R, Masse S, Dekhtyar T, Ng T, Koev G, StoU V, Stewart KD, Pratt J, Donner P, Rockway T, Mating C, Molla A (2005) Mutations conferring resistance to a hepatitis C vims (HCV) RNA-dependent RNA polymerase inhibitor alone or in combination with an HCV serine protease inhiltitor in vitro. Antimicrob Agents Chemother 49 4305 314... [Pg.49]

HavUr DV, Richman DD (1996) Viral dynamics of HIV implications for drug development and therapeutic strategies. Ann Intern Med 124(11) 984—994 Hinrichsen H, Benhamou Y, Wedemeyer H, Reiser M, Sentjens RE, Calleja JL, Foms X, Erhardt A, Cronlein J, Chaves RL, Yong CL, Nehmiz G, Steinmann GG (2004) Short-term antiviral efficacy of BILN 2061, a hepatitis C virus serine protease inhibitor, in hepatitis C genotype I patients. Gastroenterology 127(5) 1347-1355... [Pg.343]

Other topical bleaching agents include arbu-tin, licorice, unsaturated fatty acids, soy extracts, serine protease inhibitors, ellagic acid and resveratrol. [Pg.153]


See other pages where Serine proteases protease inhibitors is mentioned: [Pg.205]    [Pg.170]    [Pg.557]    [Pg.36]    [Pg.448]    [Pg.46]    [Pg.361]    [Pg.361]    [Pg.517]    [Pg.108]    [Pg.101]    [Pg.102]    [Pg.430]    [Pg.676]    [Pg.1287]    [Pg.863]    [Pg.29]    [Pg.48]    [Pg.52]    [Pg.86]    [Pg.99]    [Pg.103]    [Pg.104]    [Pg.106]    [Pg.107]    [Pg.107]    [Pg.108]    [Pg.331]    [Pg.332]    [Pg.345]   
See also in sourсe #XX -- [ Pg.607 ]

See also in sourсe #XX -- [ Pg.607 ]




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Bowman-Birk serine protease inhibitor

Bowman-Birk serine protease inhibitor ATI

Bowman-Birk serine protease inhibitor BTCIas

Bowman-Birk serine protease inhibitor CPTIsas

Bowman-Birk serine protease inhibitor D-IIas

Bowman-Birk serine protease inhibitor DATIas

Bowman-Birk serine protease inhibitor EBIas

Bowman-Birk serine protease inhibitor HGI-IIIas

Bowman-Birk serine protease inhibitor I (ABI

Bowman-Birk serine protease inhibitor bean)

Bowman-Birk serine protease inhibitor proteins

Effects of serine protease inhibitor

Endogenous serine protease inhibitors

Enzyme serine protease inhibitor

Non-protein serine protease inhibitor from natural sources

Non-protein serine protease inhibitor phenolics

Non-protein serine protease inhibitor terpenes

Plant Kunitz serine protease inhibitor

Plant Kunitz serine protease inhibitor BASI (barley a-amylase

Plant Kunitz serine protease inhibitor Carica KPI

Plant Kunitz serine protease inhibitor Erythrina

Plant Kunitz serine protease inhibitor activator

Plant Kunitz serine protease inhibitor effects on ETI-a - plasminogen

Plant Kunitz serine protease inhibitor effects on Factor Xlla

Plant Kunitz serine protease inhibitor effects on Kallikrein

Plant Kunitz serine protease inhibitor effects on chymotrypsin

Plant Kunitz serine protease inhibitor effects on elastase

Plant Kunitz serine protease inhibitor effects on inferred KPI

Plant Kunitz serine protease inhibitor effects on subtilisin

Plant Kunitz serine protease inhibitor effects on subtilisin BPN

Plant Kunitz serine protease inhibitor effects on trypsin

Plant Kunitz serine protease inhibitor from Brassica napus

Plant Kunitz serine protease inhibitor from Glycine max

Plant Kunitz serine protease inhibitor from Hordeum vulgare

Plant Kunitz serine protease inhibitor from Ipomoea batatas

Plant Kunitz serine protease inhibitor from Lycopersicon esculentu

Plant Kunitz serine protease inhibitor from Nicotiana glauca

Plant Kunitz serine protease inhibitor from Nicotiana glutinosa

Plant Kunitz serine protease inhibitor from Oryza sativa

Plant Kunitz serine protease inhibitor from Populus deltoides

Plant Kunitz serine protease inhibitor from Prosopis juliflora

Plant Kunitz serine protease inhibitor from Psophocarpus

Plant Kunitz serine protease inhibitor proteinase

Plant Kunitz serine protease inhibitor proteins

Plant Kunitz serine protease inhibitor tetragonolobus

Potato serine protease inhibitors

Potato type I serine protease inhibitor

Potato type I serine protease inhibitor Af4 gene product

Potato type I serine protease inhibitor effects on cathepsin

Potato type I serine protease inhibitor effects on chymotrypsin

Potato type II serine protease inhibitor

Potato type II serine protease inhibitor 6-domain PI precursor NaProPI

Potato type II serine protease inhibitor ARPIas

Potato type II serine protease inhibitor PCI-Ias

Potato type II serine protease inhibitor PTIas

Potato type II serine protease inhibitor Pepper leaf Pis

Potato type II serine protease inhibitor SaPIN2a SaPIN

Potato type II serine protease inhibitor aubergine

Potato type II serine protease inhibitor effects on Streptomyces griseus

Potato type II serine protease inhibitor effects on chymotrypsin

Potato type II serine protease inhibitor effects on pronase

Potato type II serine protease inhibitor effects on trypsin

Potato type II serine protease inhibitor from Capsicum annuum

Potato type II serine protease inhibitor from Lycopersicon esculentu

Potato type II serine protease inhibitor from Nicotiana alata

Potato type II serine protease inhibitor from Nicotiana alata (ornamental

Potato type II serine protease inhibitor from Nicotiana glutinosa

Potato type II serine protease inhibitor from Nicotiana tabacum

Potato type II serine protease inhibitor from Solanum tuberosum

Potato type II serine protease inhibitor proteinase

Potato type II serine protease inhibitor tobacco)

Serin proteases

Serine inhibitor

Serine protease

Serine protease factor Vila inhibitors

Serine protease inhibitor

Serine protease inhibitor

Serine protease inhibitor proteins

Serine protease inhibitor proteins inhibitors)

Serine protease inhibitors affinity labels

Serine protease thrombin inhibitors

Serpin, serine protease inhibitor

Squash family serine protease inhibitor

Squash family serine protease inhibitor CPGTI

Squash family serine protease inhibitor Cucumis CMCTI

Squash family serine protease inhibitor Ecballium EETI

Squash family serine protease inhibitor LATIas

Squash family serine protease inhibitor LLDTI

Squash family serine protease inhibitor effects on Xa, Xlla, kallikrein

Squash family serine protease inhibitor effects on cathepsin

Squash family serine protease inhibitor effects on elastase

Squash family serine protease inhibitor effects on endopeptidase

Squash family serine protease inhibitor effects on trypsin

Squash family serine protease inhibitor from Bryonia dioica

Squash family serine protease inhibitor from Citrullus vulgaris

Squash family serine protease inhibitor from Cucumis melo

Squash family serine protease inhibitor from Cucumis sativus

Squash family serine protease inhibitor from Cucurbita maxima

Squash family serine protease inhibitor from Cucurbita pepo

Squash family serine protease inhibitor from Echinocystis lobata

Squash family serine protease inhibitor from Luffa acutangula

Squash family serine protease inhibitor from Luffa cylindrica

Squash family serine protease inhibitor from Momordica charanti

Squash family serine protease inhibitor from Momordica cochinchinensi

Squash family serine protease inhibitor from Momordica repens

Squash family serine protease inhibitor from Tricosanthes

Subtilisin effects of serine protease inhibitor

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