Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
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Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimerSerpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functionsHistone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiencyTargeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells93-kDa twin-domain serine protease inhibitor (Serpin) has a regulatory function on the beetle Toll proteolytic signaling cascadeThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyA minimal sequence code for switching protein structure and functionDeterminants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with MesotrypsinStructural and Functional Characterization of a Highly Specific Serpin in the Insect Innate ImmunityTherapeutic target-site variability in α1-antitrypsin characterized at high resolutionClinical utility gene card for: α-1-antitrypsin deficiencyIn silico assessment of potential druggable pockets on the surface of α1-antitrypsin conformersCrystallization and preliminary X-ray crystallographic analysis of a highly specific serpin from the beetle Tenebrio molitor.Modeling inherited metabolic disorders of the liver using human induced pluripotent stem cells.ERAD defects and the HFE-H63D variant are associated with increased risk of liver damages in Alpha 1-Antitrypsin DeficiencyAltered native stability is the dominant basis for susceptibility of α1-antitrypsin mutants to polymerization.Characterization of a novel serine protease inhibitor gene from a marine metagenome.A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.Molecular signature of mineralocorticoid receptor signaling in cardiomyocytes: from cultured cells to mouse heartDefining the mechanism of polymerization in the serpinopathies.The tempered polymerization of human neuroserpin.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization.A novel SERPINA1 mutation causing serum alpha(1)-antitrypsin deficiency.Strand 6B deformation and residues exposure towards N-terminal end of helix B during proteinase inhibition by Serpins.Bioinformatic analyses of male and female Amblyomma americanum tick expressed serine protease inhibitors (serpins).Blocking formation of large protein aggregates by small peptides.The diuretic torasemide does not prevent aldosterone-mediated mineralocorticoid receptor activation in cardiomyocytes.Transgenic α-1-antitrypsin secreted into the bloodstream from salivary glands is biologically activeFunctional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular DynamicsTissue plasminogen activator-independent roles of neuroserpin in the central nervous system.Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.The Z mutation alters the global structural dynamics of α1-antitrypsin.Local conformational flexibility provides a basis for facile polymer formation in human neuroserpinEnergy landscapes of functional proteins are inherently risky.The aggregation-prone intracellular serpin SRP-2 fails to transit the ER in Caenorhabditis elegans.Autoprocessing of neutrophil elastase near its active site reduces the efficiency of natural and synthetic elastase inhibitors.Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.Folding mechanism of the metastable serpin α1-antitrypsin.
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P2860
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@en
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@nl
type
label
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@en
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@nl
prefLabel
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@en
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@nl
P1476
Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
@en
P2093
Bibek Gooptu
David A Lomas
P304
P356
10.1146/ANNUREV.BIOCHEM.78.082107.133320
P577
2009-01-01T00:00:00Z