Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase
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The ocular albinism type 1 (OA1) G-protein-coupled receptor functions with MART-1 at early stages of melanogenesis to control melanosome identity and compositionThe tetraspanin CD63 regulates ESCRT-independent and -dependent endosomal sorting during melanogenesisEmerging roles of extracellular vesicles in the nervous systemPMEL Amyloid Fibril Formation: The Bright Steps of PigmentationActive-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.Endoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction.Glycoprotein nonmetastatic melanoma protein b, a melanocytic cell marker, is a melanosome-specific and proteolytically released protein.Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenicEffects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17.Proprotein convertases process Pmel17 during secretion.Mechanisms of protein delivery to melanosomes in pigment cells.The melanosomal protein PMEL17 as a target for antibody drug conjugate therapy in melanoma.[Biogenesis of melanosomes - the chessboard of pigmentation].SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.The Kringle-like Domain Facilitates Post-endoplasmic Reticulum Changes to Premelanosome Protein (PMEL) Oligomerization and Disulfide Bond Configuration and Promotes Amyloid Formation.Critical residues in the PMEL/Pmel17 N-terminus direct the hierarchical assembly of melanosomal fibrils.PMEL: a pigment cell-specific model for functional amyloid formationThe PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.BACE2 processes PMEL to form the melanosome amyloid matrix in pigment cells.A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions.N-terminal domains elicit formation of functional Pmel17 amyloid fibrilsMelanosomal formation of PMEL core amyloid is driven by aromatic residues.Exosomes: vesicular carriers for intercellular communication in neurodegenerative disorders.Fold modulating function: bacterial toxins to functional amyloids.Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.Regulation of Alpha-Secretase ADAM10 In vitro and In vivo: Genetic, Epigenetic, and Protein-Based Mechanisms.Why are Functional Amyloids Non-Toxic in Humans?Transmembrane semaphorin5B is proteolytically processed into a repulsive neural guidance cue.Biogenesis of Melanosomes
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Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on December 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Formation of Pmel17 amyloid is ...... substrate for gamma-secretase
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Formation of Pmel17 amyloid is ...... substrate for gamma-secretase.
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type
label
Formation of Pmel17 amyloid is ...... substrate for gamma-secretase
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Formation of Pmel17 amyloid is ...... substrate for gamma-secretase.
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altLabel
Formation of Pmel17 Amyloid Is ...... Is a Substrate for γ-Secretase
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prefLabel
Formation of Pmel17 amyloid is ...... substrate for gamma-secretase
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Formation of Pmel17 amyloid is ...... substrate for gamma-secretase.
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P2093
P2860
P356
P1476
Formation of Pmel17 amyloid is ...... substrate for gamma-secretase
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P2093
Claudia Huelsmann
Edward H Koo
Hiroko Maruyama
Sandra Baches
Sascha Weggen
P2860
P304
P356
10.1074/JBC.M808904200
P407
P577
2008-12-01T00:00:00Z