Structural studies of cysteine proteases and their inhibitors.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Acta Biochimica Polonica

• Publication date

  Unknown publication date

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.18388/ABP.2001_5108PMID 11440158
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Cystatin C-Properties and use as diagnostic marker

  2006cited by this paper
• Evolution of proteins of the cystatin superfamily

  2005cited by this paper
• MNDO study of the mechanism of the inhibition of cysteine proteinases by diazomethyl ketones

  2004cited by this paper
• Peptidyl diazomethylketones as cysteine protease inhibitors structurally based upon the inhibitory centers of cystatins

  2001cited by this paper
• A peptidyl derivative structurally based on the inhibitory center of cystatin C inhibits bone resorption in vitro.

  2000cited by this paper
• Synthesis and antibacterial properties of peptidyl derivatives and cyclopeptides structurally based upon the inhibitory centre of human cystatin C: Dissociation of antiproteolytic and antibacterial effects

  2000cited by this paper
• Hereditary cystatin C amyloid angiopathy

  2000cited by this paper
• Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?

  1999cited by this paper
• Self-association of cystatin

  1999cited by this paper
• MEROPS: the peptidase database

  1999cited by this paper
• Serum Cystatin C as an Endogenous Marker of the Renal Function – a Review

  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
• Expression of a selenomethionyl derivative and preliminary crystallographic studies of human cystatin C

  1999cited by this paper
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  1998cited by this paper
• Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C.

  1998cited by this paper
• A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution.

  1998cited by this paper
• Amino acid substitutions in the N-terminal segment of cystatin C create selective protein inhibitors of lysosomal cysteine proteinases.

  1998cited by this paper
• Structural basis for different inhibitory specificities of human cystatins C and D.

  1998cited by this paper
• Revised Definition of Substrate Binding Sites of Papain-Like Cysteine Proteases

  1998cited by this paper
• Cystatin F Is a Glycosylated Human Low Molecular Weight Cysteine Proteinase Inhibitor*

  1998cited by this paper
• Cysteine Proteases and Their Inhibitors.

  1997cited by this paper
• Cystatin E is a Novel Human Cysteine Proteinase Inhibitor with Structural Resemblance to Family 2 Cystatins*

  1997cited by this paper
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  1997cited by this paper
• NMR structural studies of human cystatin C dimers and monomers.

  1997cited by this paper
• The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation.

  1997cited by this paper
• Thermal denaturation of human cystatin C and two of its variants; comparison to chicken cystatin.

  1997cited by this paper
• Identification, Cloning, and Characterization of Cystatin M, a Novel Cysteine Proteinase Inhibitor, Down-regulated in Breast Cancer*

  1997cited by this paper
• Friends and relations of the cystatin superfamily—new members and their evolution

  1997cited by this paper
• Differences in specificity for the interactions of stefins A, B and D with cysteine proteinases

  1996cited by this paper
• Genetics of epilepsy : Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1)

  1996cited by this paper
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  1996cited by this paper
• Folding-related Dimerization of Human Cystatin C (*)

  1996influential reference
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1994cited by this paper
• [1] Classification of peptidases

  1994cited by this paper
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  1993cited by this paper
• Localization of the human cystatin D gene (CST5) to chromosome 20p11.21 by in situ hybridization.

  1993cited by this paper
• A sequence variation in the human cystatin D gene resulting in an amino acid (Cys/Arg) polymorphism at the protein level

  1993cited by this paper
• Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution.

  1993cited by this paper
• X‐ray crystallographic structure of a papain‐leupeptin complex

  1993cited by this paper
• Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors.

  1993cited by this paper
• Cystatin C (CST3), the candidate gene for hereditary cystatin C amyloid angiopathy (HCCAA), and other members of the cystatin gene family are clustered on chromosome 20p11.2.

  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
• Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family

  1993cited by this paper
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  1993cited by this paper
• The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.

  1993cited by this paper
• Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells

  1992cited by this paper
• Structure of monoclinic papain at 1.60 Å resolution

  1992cited by this paper
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  1992cited by this paper
• Isolation and characterization of bovine stefin B.

  1992cited by this paper
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  1992cited by this paper
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  1992cited by this paper
• Identification of full-sized forms of salivary (S-type) cystatins (cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of phosphorylation sites of cystatin S.

  1991cited by this paper
• Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21.

  1991cited by this paper
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  1991cited by this paper
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  1990cited by this paper
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  1990cited by this paper
• The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.

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  1989cited by this paper
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  1989cited by this paper
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• The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20.

  1989cited by this paper
• The 2.0 A X‐ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

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  1987cited by this paper
• Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

  1987cited by this paper
• Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin.

  1987cited by this paper
• The cystatins: a new class of peptidase inhibitors

  1987cited by this paper
• Properties and structure of human spleen stefin B - a low molecular weight protein inhibitor of cysteine proteinases

  1986cited by this paper
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• Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids.

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• Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data.

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  1985cited by this paper
• The disulphide bridges of human cystatin C (γ‐trace) and chicken cystatin

  1984cited by this paper
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  1984cited by this paper
• Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes.

  1983cited by this paper
• Isolation and characterization of two thiol proteinase inhibitors of low molecular weight from newborn rat epidermis.

  1983cited by this paper
• The gamma-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma.

  1983cited by this paper
• The γ-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma

  1983cited by this paper
• L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.

  1982cited by this paper
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  1982cited by this paper
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  1977cited by this paper
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  1977cited by this paper
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  1977cited by this paper
• Some properties of a ficin-papain inhibitor from avian egg white.

  1973cited by this paper

• Systematic analysis of the cystatin gene family: From whole-genome identification to immunological role validation in silver pomfret (Pampus argenteus)

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• Two Japanese families with adult-onset leukoencephalopathy caused by pathogenic variants in CST3.

  2025cites this paper
• Characteristics and immunoprotective functions of three cysteine proteases from Clonorchis sinensis

  2025cites this paper
• A Novel Cystatin Gene from Sea Cucumber (Apostichopus japonicus): Characterization and Comparative Expression with Cathepsin L During Early Stage of Hypoxic Exposure-Induced Autolysis

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