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Academic Journal

Proteolysis of α-synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology.

  • Authors : Sacino AN; Department of Neuroscience, College of Medicine University of Florida, Gainesville, Florida, USA.; Center for Translational Research in Neurodegenerative Disease, College of Medicine University of Florida, Gainesville, Florida, USA.

Subjects: Proteolysis*; Amyloid/Amyloid/Amyloid/*metabolism ; Inclusion Bodies/Inclusion Bodies/Inclusion Bodies/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2017 Feb; Vol. 140 (4), pp. 662-678. Date of Electronic Publication: 2016 Aug 19.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Identification of truncated C-terminal fragments of the Alzheimer's disease amyloid protein precursor derived from sequential proteolytic pathways.

  • Authors : Mosser S; Foundation Eclosion, Plan-les-Ouates, CH-1228, Switzerland.; Campus Biotech Innovation Park, Geneva, CH-1202, Switzerland.

Subjects: Proteolysis* ; Signal Transduction*; Alzheimer Disease/Alzheimer Disease/Alzheimer Disease/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2021 Mar; Vol. 156 (6), pp. 943-956. Date of Electronic Publication: 2020 Sep 07.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Revisiting the proteolytic processing of cell adhesion molecule L1.

  • Authors : Kleene R; Research Group Biosynthesis of Neural Structures, Zentrum für Molekulare Neurobiologie, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany.; Lutz D

Subjects: Proteolysis*; Brain/Brain/Brain/*metabolism ; Neural Cell Adhesion Molecule L1/Neural Cell Adhesion Molecule L1/Neural Cell Adhesion Molecule L1/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2021 May; Vol. 157 (4), pp. 1102-1117. Date of Electronic Publication: 2020 Oct 16.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

A molecular toolbox for studying protein degradation in mammalian cells.

  • Authors : Eldeeb MA; Department of Chemistry (Biochemistry Division), Faculty of Science, Cairo University, Giza, Egypt.; Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.

Subjects: Proteolysis* ; Proteostasis*; Cells/Cells/Cells/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2019 Nov; Vol. 151 (4), pp. 520-533. Date of Electronic Publication: 2019 Aug 25.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Neuropeptide Y (NPY) in cerebrospinal fluid from patients with Huntington's Disease: increased NPY levels and differential degradation of the NPY1-30 fragment.

  • Authors : Wagner L; Deutschsprachige Selbsthilfegruppe für Alkaptonurie (DSAKU) e.V., Stuttgart, Germany.; Probiodrug AG, Halle (Saale), Germany.

Subjects: Proteolysis*; Huntington Disease/Huntington Disease/Huntington Disease/*cerebrospinal fluid ; Huntington Disease/Huntington Disease/Huntington Disease/*diagnosis

  • Source: Journal of neurochemistry [J Neurochem] 2016 Jun; Vol. 137 (5), pp. 820-37.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print Cited

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Academic Journal

Retromer and Rab2-dependent trafficking mediate PS1 degradation by proteasomes in endocytic disturbance.

  • Authors : Ueda N; Section of Cell Biology and Pathology, Department of Alzheimer's Disease Research, Center for Development of Advanced Medicine for Dementia, National Center for Geriatrics and Gerontology (NCGG), Aichi, Japan.; Tomita T

Subjects: Proteolysis*; Endocytosis/Endocytosis/Endocytosis/*physiology ; Presenilin-1/Presenilin-1/Presenilin-1/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2016 May; Vol. 137 (4), pp. 647-58. Date of Electronic Publication: 2016 Mar 08.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Enhanced ubiquitination and proteasomal degradation of catalytically deficient human choline acetyltransferase mutants.

  • Authors : Morey TM; Molecular Medicine Research Group, Robarts Research Institute, Department of Physiology and Pharmacology, Schulich School of Medicine & Dentistry, University of Western Ontario, London, Ontario, Canada.; Albers S

Subjects: Proteolysis*; Choline O-Acetyltransferase/Choline O-Acetyltransferase/Choline O-Acetyltransferase/*metabolism ; Mutation/Mutation/Mutation/*physiology

  • Source: Journal of neurochemistry [J Neurochem] 2016 May; Vol. 137 (4), pp. 630-46. Date of Electronic Publication: 2016 Mar 15.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Walking the tightrope: proteostasis and neurodegenerative disease.

  • Authors : Yerbury JJ; Proteostasis and Disease Research Centre, School of Biological Sciences, Faculty of Science, Medicine and Health, University of Wollongong, Wollongong, New South Wales, Australia.; Illawarra Health and Medical Research Institute, Wollongong, New South Wales, Australia.

Subjects: Proteolysis*; Neurodegenerative Diseases/Neurodegenerative Diseases/Neurodegenerative Diseases/*metabolism ; Proteostasis Deficiencies/Proteostasis Deficiencies/Proteostasis Deficiencies/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2016 May; Vol. 137 (4), pp. 489-505. Date of Electronic Publication: 2016 Mar 08.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Pathogenic mutation of UBQLN2 impairs its interaction with UBXD8 and disrupts endoplasmic reticulum-associated protein degradation.

  • Authors : Xia Y; Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, 1020 Locust Street, Philadelphia, Pennsylvania, USA.; Yan LH

Subjects: Proteolysis*; Blood Proteins/Blood Proteins/Blood Proteins/*metabolism ; Cell Cycle Proteins/Cell Cycle Proteins/Cell Cycle Proteins/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2014 Apr; Vol. 129 (1), pp. 99-106. Date of Electronic Publication: 2013 Nov 22.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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Academic Journal

Proteolytic processing of Alzheimer's β-amyloid precursor protein.

  • Authors : Zhang H; Fujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian, China.; Neurodegenerative Disease Research Program, Sanford-Burnham Medical Research Institute, La Jolla, California, USA.

Subjects: Proteolysis*; Alzheimer Disease/Alzheimer Disease/Alzheimer Disease/*metabolism ; Amyloid beta-Protein Precursor/Amyloid beta-Protein Precursor/Amyloid beta-Protein Precursor/*metabolism

  • Source: Journal of neurochemistry [J Neurochem] 2012 Jan; Vol. 120 Suppl 1, pp. 9-21. Date of Electronic Publication: 2011 Nov 28.Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic

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