Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro
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Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapySmall molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregatesNeuroserpin binds Abeta and is a neuroprotective component of amyloid plaques in Alzheimer diseaseMutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulumLatent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodiesThe tempered polymerization of human neuroserpin.The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization.Protein misfolding and the serpinopathies.Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular DynamicsLocal conformational flexibility provides a basis for facile polymer formation in human neuroserpinPractical genetics: alpha-1-antitrypsin deficiency and the serpinopathies.Accumulation of mutant neuroserpin precedes development of clinical symptoms in familial encephalopathy with neuroserpin inclusion bodies.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyDetermining serpin conformational distributions with single molecule fluorescenceEmbelin binds to human neuroserpin and impairs its polymerisation.IgE-tailpiece associates with α-1-antitrypsin (A1AT) to protect IgE from proteolysis without compromising its ability to interact with FcεRI.The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB.Interactions between N-linked glycosylation and polymerisation of neuroserpin within the endoplasmic reticulumNeuroserpin polymers activate NF-kappaB by a calcium signaling pathway that is independent of the unfolded protein response.alpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies.A successful strategy for the recovering of active P21, an insoluble recombinant protein of Trypanosoma cruzi.Unravelling the twists and turns of the serpinopathies.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.pH-dependent stability of neuroserpin is mediated by histidines 119 and 138; implications for the control of beta-sheet A and polymerization.Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition.The low density lipoprotein receptor-related protein modulates protease activity in the brain by mediating the cellular internalization of both neuroserpin and neuroserpin-tissue-type plasminogen activator complexes.The stability and activity of human neuroserpin are modulated by a salt bridge that stabilises the reactive centre loop.A hydrophobic patch surrounding Trp154 in human neuroserpin controls the helix F dynamics with implications in inhibition and aggregation.Cholesterol impairment contributes to neuroserpin aggregation.Two latent and two hyperstable polymeric forms of human neuroserpin.Probing neuroserpin polymerization and interaction with amyloid-beta peptides using single molecule fluorescence.Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the Proteinase Inhibitor 12 geneMutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis.Mutation-, aging-, and gene dosage-dependent accumulation of neuroserpin (G392E) in endoplasmic reticula and lysosomes of neurons in transgenic mice.Molecular bases of neuroserpin function and pathology.
P2860
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P2860
Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro
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2002 nî lūn-bûn
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2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@ast
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@en
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@nl
type
label
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@ast
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@en
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@nl
prefLabel
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@ast
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@en
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@nl
P2093
P356
P1476
Mutant Neuroserpin (S49P) that ...... eadily forms polymers in vitro
@en
P2093
Damian C Crowther
David A Lomas
Didier Belorgey
Ravi Mahadeva
P304
P356
10.1074/JBC.M200680200
P407
P577
2002-05-10T00:00:00Z