Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
about
Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysisMutations in CSTA, encoding Cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesionProtease signalling: the cutting edgeStructure of an Fab–Protease Complex Reveals a Highly Specific Non-canonical Mechanism of InhibitionCrystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteasesCharacterization of Solanum tuberosum Multicystatin and Its Structural comparison with Other CystatinsVersatile Loops in Mycocypins Inhibit Three Protease FamiliesCrystal structure of human cystatin C stabilized against amyloid formationThe crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine modelStefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleftStructural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37Characterization of Solanum tuberosum Multicystatin and the Significance of Core DomainsCrystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: implications for angiogenic regulationStructural Basis for the Immunomodulatory Function of Cysteine Protease Inhibitor from Human Roundworm Ascaris lumbricoidesX-ray crystallography and NMR studies of domain-swapped canecystatin-1Solution structure of a phytocystatin from Ananas comosus and its molecular interaction with papainMouse stefins A1 and A2 (Stfa1 and Stfa2) differentiate between papain-like endo- and exopeptidasesTcCYPR04, a Cacao Papain-Like Cysteine-Protease Detected in Senescent and Necrotic Tissues Interacts with a Cystatin TcCYS4The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligandsStructural basis for unique mechanisms of folding and hemoglobin binding by a malarial proteaseThe origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship.Structure-function studies of an engineered scaffold protein derived from Stefin A. II: Development and applications of the SQT variant.Structure-function studies of an engineered scaffold protein derived from stefin A. I: Development of the SQM variant.Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.Structural basis of reduction-dependent activation of human cystatin F.Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins.Crystallization and preliminary X-ray diffraction analysis of Val57 mutants of the amyloidogenic protein human cystatin C.Structure-function of falcipains: malarial cysteine proteases.The many faces of protease-protein inhibitor interactionDifferences in aggregation properties of three site-specific mutants of recombinant human stefin B.Two decades of thyroglobulin type-1 domain research.Mechanisms of macromolecular protease inhibitorsC1A cysteine-proteases and their inhibitors in plants.Cystatins in immune system.The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L.Microbial inhibitors of cysteine proteases.Synthesis of a biologically active triazole-containing analogue of cystatin A through successive peptidomimetic alkyne-azide ligations.Peptide aptamer microarrays: bridging the bio-detector interface.Glycosylation directs targeting and activation of cystatin f from intracellular and extracellular sources.Modulation of contact order effects in the two-state folding of stefins A and B.
P2860
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P2860
Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@ast
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@en
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@nl
type
label
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@ast
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@en
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@nl
prefLabel
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@ast
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@en
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@nl
P2093
P1476
Crystal structure of Stefin A ...... tes of endo- and exopeptidases
@en
P2093
Andreja Dobersek
Dusan Turk
Gregor Guncar
Iztok Dolenc
Marjetka Podobnik
Sasa Jenko
P304
P356
10.1016/S0022-2836(02)01432-8
P407
P577
2003-02-21T00:00:00Z