The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
about
Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimerAlpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapySerpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functionsCrystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loopElucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation.Organizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programsThe high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition.The roles of helix I and strand 5A in the folding, function and misfolding of α1-antitrypsin.Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesisThe Z mutation alters the global structural dynamics of α1-antitrypsin.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyWhat we owe to alpha(1)-antitrypsin and to Carl-Bertil Laurell.Molecular Mechanism of Z α1-Antitrypsin DeficiencyInhibition of intracellular degradation increases secretion of a mutant form of alpha1-antitrypsin associated with profound deficiency.New Findings in PiZZ alpha1-antitrypsin deficiency-related panniculitis. Demonstration of skin polymers and high dosing requirements of intravenous augmentation therapy.Intracellular processing of alpha1-antitrypsin.Unravelling the twists and turns of the serpinopathies.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.Alpha-1 antitrypsin deficiency: new developments in augmentation and other therapies.Broad spectrum of hepatocyte inclusions in humans, animals, and experimental models.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z.The pathological Trento variant of alpha-1-antitrypsin (E75V) shows nonclassical behaviour during polymerization.A novel transcription factor regulates expression of the vacuolar H+-ATPase B2 subunit through AP-2 sites during monocytic differentiation.Artificial DnaJ Protein for protein production and conformational diseases.Review: alpha 1-antitrypsin deficiency associated liver disease.Genetics and respiratory disease. 2. Alpha 1-antitrypsin deficiency, cirrhosis and emphysema.Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerizationHow the serpin α1-proteinase inhibitor folds.Loop-sheet mechanism of serpin polymerization tested by reactive center loop mutations.Retarded protein folding of deficient human alpha 1-antitrypsin D256V and L41P variants.Lung polymers in Z alpha1-antitrypsin deficiency-related emphysema.Probing the local conformational change of alpha1-antitrypsin.Medicine. Clearing conformational disease.Osmolytes as modulators of conformational changes in serpins.Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases.Oxidation of Z α1-antitrypsin by cigarette smoke induces polymerization: a novel mechanism of early-onset emphysema.Probing the unfolding pathway of alpha1-antitrypsin.Structural defects underlying protein dysfunction in human glucose-6-phosphate dehydrogenase A(-) deficiency.
P2860
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P2860
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@ast
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@en
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@nl
type
label
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@ast
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@en
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@nl
prefLabel
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@ast
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@en
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@nl
P2093
P2860
P356
P1476
The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.
@en
P2093
P2860
P304
P356
10.1038/NSB0595-363
P577
1995-05-01T00:00:00Z