Pharmaceutics | Free Full-Text | Identification of Autophagy as a Functional Target Suitable for the Pharmacological Treatment of Mitochondrial Membrane Protein-Associated Neurodegeneration (MPAN) In Vitro
C19orf12 Gene - GeneCards | CS012 Protein | CS012 Antibody
Dominant mitochondrial membrane protein-associated neurodegeneration (MPAN) variants cluster within a specific C19orf12 isoform - ScienceDirect
C19orf12 ablation causes ferroptosis in mitochondrial membrane protein-associated with neurodegeneration - ScienceDirect
C19orf12 antibody (27382-1-AP) | Proteintech
Pharmaceuticals | Free Full-Text | Neurodegeneration with Brain Iron Accumulation Disorders: Valuable Models Aimed at Understanding the Pathogenesis of Iron Deposition
Frontiers | Case Report: Identification of a De novo C19orf12 Variant in a Patient With Mitochondrial Membrane Protein–Associated Neurodegeneration
C19orf12 Gene - GeneCards | CS012 Protein | CS012 Antibody
Nazo, the Drosophila homolog of the NBIA-mutated protein – c19orf12, is required for triglyceride homeostasis | bioRxiv
Absence of an Orphan Mitochondrial Protein, C19orf12, Causes a Distinct Clinical Subtype of Neurodegeneration with Brain Iron Accumulation - ScienceDirect
C19orf12 CRISPR Knockout and Activation Products (h) | SCBT - Santa Cruz Biotechnology
Pharmaceutics | Free Full-Text | Identification of Autophagy as a Functional Target Suitable for the Pharmacological Treatment of Mitochondrial Membrane Protein-Associated Neurodegeneration (MPAN) In Vitro
e Schematic representation of proteins cellular localization and... | Download Scientific Diagram
C19orf12 antibody | Anti-C19orf12 | stjohnslabs
LC3 puncta formation in C19orf12 D18G/L132Q fibroblasts after 24 h of... | Download Scientific Diagram
![PDF] Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca2+ | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/dd2ecb2012d86f9d3853c6aef367791e936d0787/11-Figure9-1.png "PDF] Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca2+ | Semantic Scholar")
PDF] Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca2+ | Semantic Scholar
Review: Insights into molecular mechanisms of disease in neurodegeneration with brain iron accumulation: unifying theories - Arber - 2016 - Neuropathology and Applied Neurobiology - Wiley Online Library
Frontiers | Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca2+
C19orf12 Gene - GeneCards | CS012 Protein | CS012 Antibody
C19orf12 siRNA (h), shRNA and Lentiviral Particle Gene Silencers | SCBT - Santa Cruz Biotechnology
Recombinant Human C19ORF12 protein (ABIN2718593)
Redistribution of C19orf12 during oxidative stress. (Ai | Open-i
Frontiers | Mutations of C19orf12, coding for a transmembrane glycine zipper containing mitochondrial protein, cause mis-localization of the protein, inability to respond to oxidative stress and increased mitochondrial Ca2+
C19orf12 gene mutations in patients with neurodegeneration with brain iron accumulation - ScienceDirect
