Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase inhibitor.
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Elucidating the structural chemistry of glycosaminoglycan recognition by protein C inhibitorThromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp)Recombinant human pigment epithelium-derived factor (PEDF): characterization of PEDF overexpressed and secreted by eukaryotic cellsReminiscences from a life in protein physical chemistryCrystal structure of neuroserpin: a neuronal serpin involved in a conformational diseaseThe murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain.Pigment epithelium-derived factor (PEDF), a serpin with potent anti-angiogenic and neurite outgrowth-promoting properties.Serpin alpha 1proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopyStructural investigation of the alpha-1-antichymotrypsin: prostate-specific antigen complex by comparative model buildingNeuroserpin, an axonally secreted serine protease inhibitor.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Comparative Study of the Interactions between Ovalbumin and five Antioxidants by Spectroscopic Methods.The mechanism by which serpins inhibit thrombin and other serine proteinases.Structural aspects of serpin inhibition.The biostructural pathology of the serpins: critical function of sheet opening mechanism.S-ovalbumin, an ovalbumin conformer with properties analogous to those of loop-inserted serpins.Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop.The N-terminal domain of antithrombin-III is essential for heparin binding and complex-formation with, but not cleavage by, alpha-thrombin.Interaction between the P14 residue and strand 2 of beta-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor-2.Refolding mechanism of ovalbumin: investigation by using a starting urea-denatured disulfide isomer with mispaired CYS367-CYS382.Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins.Residues in the human corticosteroid-binding globulin reactive center loop that influence steroid binding before and after elastase cleavage.Cleaved serpin refolds into the relaxed state via a stressed conformer.Deletion mutagenesis of heparin cofactor II: defining the minimum size of a thrombin inhibiting serpin.Significance of secondary structure predictions on the reactive center loop region of serpins: a model for the folding of serpins into a metastable state."How I chose research on proteases or, more correctly, how it chose me".Characterization of a human alpha1-antitrypsin variant that is as stable as ovalbumin.A serpin from the gut bacterium Bifidobacterium longum inhibits eukaryotic elastase-like serine proteases.
P2860
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P2860
Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase inhibitor.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
1990年學術文章
@zh
1990年學術文章
@zh-hant
name
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@en
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@nl
type
label
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@en
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@nl
prefLabel
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@en
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@nl
P2093
P1476
Crystal structure of plakalbum ...... alpha-1-proteinase inhibitor.
@en
P2093
P304
P356
10.1016/S0022-2836(05)80212-8
P407
P577
1990-06-01T00:00:00Z