Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (431) 431
mitofusin 2 (339) 339
humans (282) 282
animals (266) 266
mitochondria (262) 262
cell biology (206) 206
mitochondria - metabolism (171) 171
biochemistry & molecular biology (142) 142
mitochondrial dna (134) 134
proteins (129) 129
mitochondrial proteins - metabolism (128) 128
apoptosis (120) 120
fusion (118) 118
gtp phosphohydrolases - metabolism (108) 108
mitofusin (105) 105
fission (104) 104
mitochondrial dynamics (104) 104
mitochondrial proteins - genetics (104) 104
mice (97) 97
gtp phosphohydrolases - genetics (96) 96
endoplasmic-reticulum (95) 95
neurosciences (91) 91
oxidative stress (91) 91
male (84) 84
mitophagy (70) 70
physiological aspects (70) 70
mutation (68) 68
article (67) 67
mitochondrial fusion (67) 67
autophagy (62) 62
metabolism (62) 62
mfn2 (62) 62
female (60) 60
morphology (58) 58
mammalian-cells (57) 57
protein (56) 56
rats (56) 56
membrane proteins - metabolism (54) 54
analysis (51) 51
opa1 (51) 51
cells (50) 50
charcot-marie-tooth disease - genetics (50) 50
cell-death (47) 47
charcot-marie-tooth disease (47) 47
drp1 (47) 47
homeostasis (47) 47
membrane proteins - genetics (47) 47
genetic aspects (46) 46
mitofusins (46) 46
clinical neurology (45) 45
dysfunction (45) 45
gene expression (45) 45
mitochondria - pathology (45) 45
cells, cultured (44) 44
disease (44) 44
endoplasmic reticulum - metabolism (43) 43
mitochondria - physiology (43) 43
dominant optic atrophy (41) 41
dynamics (41) 41
physiology (41) 41
cell line (40) 40
mitochondria - ultrastructure (40) 40
skeletal-muscle (40) 40
endoplasmic reticulum (39) 39
nervous system diseases (39) 39
parkin (39) 39
research (39) 39
neuropathy (38) 38
molecular biology (37) 37
calcium (36) 36
mitochondria - genetics (36) 36
mitochondrial fission (36) 36
biology (35) 35
signal transduction (35) 35
biophysics (34) 34
obesity (33) 33
phenotype (33) 33
ubiquitin (33) 33
cell death (32) 32
endocrinology & metabolism (32) 32
expression (32) 32
neurodegeneration (32) 32
phosphorylation (32) 32
rodents (32) 32
adult (31) 31
insulin-resistance (31) 31
multidisciplinary sciences (31) 31
mutations (31) 31
reactive oxygen species - metabolism (31) 31
genes (30) 30
health aspects (30) 30
reactive oxygen species (30) 30
activation (29) 29
mice, knockout (29) 29
review (29) 29
cancer (28) 28
degradation (28) 28
energy metabolism (28) 28
heart (28) 28
middle aged (28) 28
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Early onset severe and late-onset mild Charcot-Marie-Tooth disease with mitofusin 2 (MFN2) mutations
by Chung, K.W and Kim, S.B and Park, K.D and Choi, K.G and Lee, J.H and Eun, H.W and Suh, J.S and Hwang, J.H and Kim, W.K and Seo, B.C and Kim, S.H and Son, I.H and Kim, S.M and Sunwoo, I.N and Choi, B.O
Brain, ISSN 0006-8950, 08/2006, Volume 129, Issue 8, pp. 2103 - 2118
Mutations in the mitofusin 2 (MFN2) gene, which encodes a mitochondrial GTPase mitofusin protein, have recently been reported to cause both Charcot-Marie-Tooth... 
HMSN VI | Mitofusin 2 (MFN2) | CMT2A | Charcot-Marie-Tooth disease | MITOCHONDRIAL FUSION | INVOLVEMENT | NEUROPATHY TYPE 2A | OPTIC ATROPHY | NEUROSCIENCES | CLINICAL NEUROLOGY | FAMILY | FEATURES | HEREDITARY MOTOR | GENE | mitofusin 2 ( MFN2) | TRANSIENT | TYPE-2 | GTP Phosphohydrolases | Optic Atrophies, Hereditary - genetics | Humans | Middle Aged | Molecular Sequence Data | Male | Mitochondrial Proteins - genetics | Charcot-Marie-Tooth Disease - genetics | Sural Nerve - ultrastructure | Adult | Female | Child | Disability Evaluation | Severity of Illness Index | Amino Acid Sequence | Membrane Proteins - genetics | Neural Conduction | Charcot-Marie-Tooth Disease - pathology | Microscopy, Electron | Magnetic Resonance Imaging | Phenotype | Pedigree | Adolescent | Age of Onset | Brain - pathology | Mutation | Index Medicus | Abridged Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Clinical and allelic heterogeneity in a pediatric cohort of 11 patients carrying MFN2 mutation
by Di Meglio, Chloé and Bonello-Palot, Nathalie and Boulay, Christophe and Milh, Mathieu and Ovaert, Caroline and Levy, Nicolas and Chabrol, Brigitte
Brain & Development, ISSN 0387-7604, 2015, Volume 38, Issue 5, pp. 498 - 506
Abstract Introduction The Mitofusin 2 gene ( MFN2 ), which encodes a mitochondrial membrane protein, is known to be the first cause of autosomal dominant... 
Neurology | Mitofusin 2 (MFN2) | Optic atrophy | Respiratory chain deficiency | Charcot–Marie–Tooth (CMT) | Subacute polyneuropathy | Neuropathy | White matter lesion | MARIE-TOOTH-DISEASE | MITOFUSIN 2 | CMT | Charcot-Marie-Tooth (CMT) | CLINICAL NEUROLOGY | FEATURES | HEREDITARY MOTOR | GENE | GDAP1 MUTATIONS | ONSET | Genetic Testing | GTP Phosphohydrolases - physiology | Membrane Proteins - genetics | Humans | Child, Preschool | Mitochondrial Proteins - physiology | Genotype | Infant | Male | Mitochondrial Proteins - genetics | Charcot-Marie-Tooth Disease - genetics | Phenotype | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Mitochondrial Proteins - metabolism | Pedigree | Alleles | Female | Child | Cohort Studies | Optic Atrophy - genetics | Pediatrics | Index Medicus | Life Sciences | Biochemistry, Molecular Biology | Genomics
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Mitochondrial oxidative stress causes mitochondrial fragmentation via differential modulation of mitochondrial fission–fusion proteins
by Wu, Shengnan and Zhou, Feifan and Zhang, Zhenzhen and Xing, Da
FEBS Journal, ISSN 1742-464X, 04/2011, Volume 278, Issue 6, pp. 941 - 954
Mitochondria are dynamic organelles that undergo continual fusion and fission to maintain their morphology and functions, but the mechanism involved is still... 
dynamin‐related protein 1 (Drp1) | high‐fluence low‐power laser irradiation (HF‐LPLI) | oxidative stress | fission | mitofusin 2 (Mfn2) | high-fluence low-power laser irradiation (HF-LPLI) | dynamin-related protein 1 (Drp1) | mitofusin 2 (Mfn2) | APOPTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IR RADIATION | DRP1 | DISEASE | DEPHOSPHORYLATION | CALCINEURIN | DYNAMIN-RELATED PROTEIN-1 | BAX | CYTOCHROME-C RELEASE | ASSOCIATION | Caspase 9 - metabolism | Cytochromes c - secretion | Reactive Oxygen Species - metabolism | Oxidative Stress | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Mitochondrial Proteins - biosynthesis | Mitochondria - ultrastructure | Membrane Proteins - biosynthesis | Animals | GTP Phosphohydrolases - metabolism | Lasers | Mitochondrial Proteins - metabolism | Cell Line, Tumor | Mitochondria - radiation effects | Apoptosis - physiology | Mitochondria - physiology | COS Cells | Cytochrome c | Oxidative stress | Mitochondrial DNA | Proteins | Mitochondria | Cellular biology | Molecular biology | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text An unusual splice defect in the mitofusin 2 gene (mfn2) is associated with degenerative axonopathy in tyrolean grey cattle
by Drögemüller, Cord and Reichart, Ursula and Seuberlich, Torsten and Oevermann, Anna and Baumgartner, Martin and Boghenbor, Kathrin Kühni and Stoffel, Michael H and Syring, Claudia and Meylan, Mireille and Müller, Simone and Müller, Mathias and Gredler, Birgit and Sölkner, Johann and Leeb, Tosso
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 4, pp. e18931 - e18931
Tyrolean Grey cattle represent a local breed with a population size of,5000 registered cows. In 2003, a previously unknown neurological disorder was recognized... 
ANIMALS | TYPE-2A | MITOCHONDRIAL FUSION | NEUROPATHY | MULTIDISCIPLINARY SCIENCES | DISEASE | MOTOR | MISSENSE MUTATION | EXONIC MUTATIONS | MODEL | Humans | Molecular Sequence Data | Nerve Degeneration - genetics | Cattle Diseases - genetics | Mitochondrial Proteins - genetics | RNA, Messenger - metabolism | Mitochondria - ultrastructure | Cattle | DNA Mutational Analysis | Mitochondrial Proteins - metabolism | Muscle Fibers, Skeletal - ultrastructure | Inheritance Patterns - genetics | Genetic Predisposition to Disease | Genome-Wide Association Study | RNA Splice Sites - genetics | RNA, Messenger - genetics | Gene Expression Regulation | Axons - metabolism | Cattle Diseases - pathology | Chromosome Mapping | Mitochondria - metabolism | Mutation - genetics | Nerve Degeneration - pathology | Homozygote | Phenotype | Animals | Axons - pathology | Muscle Fibers, Skeletal - pathology | Nervous system diseases | Analysis | Genomics | Beef cattle | Genetic aspects | Single nucleotide polymorphisms | Neurophysiology | Femur | Transcription | Disease | Nonsense mutation | Neuropathology | Central nervous system | Population number | Nervous system | Genomes | Single-nucleotide polymorphism | Neuropathy | Veterinary medicine | Retention | Defects | Mitochondria | Neurodegeneration | Coding | Rodents | Charcot-Marie-Tooth disease | Fibroblasts | Genetics | Ataxia | Population | Life sciences | Degeneration | Chromosome 16 | Age | Neuromuscular diseases | Genetic disorders | Splicing | Calves | Stop codon | Cation exchanging | Heredity | Breeding of animals | Membrane proteins | Livestock | Mutation | Aberration | Gene mapping | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Massively Parallel Sequencing Detected a Mutation in the MFN2 Gene Missed by Sanger Sequencing Due to a Primer Mismatch on an SNP Site
by Neupauerová, Jana and Grečmalová, Dagmar and Seeman, Pavel and Laššuthová, Petra
Annals of Human Genetics, ISSN 0003-4800, 05/2016, Volume 80, Issue 3, pp. 182 - 186
We describe a patient with early onset severe axonal Charcot‐Marie‐Tooth disease (CMT2) with dominant inheritance, in whom Sanger sequencing failed to detect a... 
mitofusin 2 | MFN2 | primer mismatch | Massively parallel sequencing (MPS) | polymerase chain reaction (PCR) | single nucleotide polymorphism (SNP) | Polymerase chain reaction (PCR) | Single nucleotide polymorphism (SNP) | mitofusin 2 (MFN2) | Primer mismatch | DIAGNOSIS | HEREDITARY MOTOR | DISEASE | GENETICS & HEREDITY | MECHANISMS | ALLELE DROPOUT | IDENTIFICATION | Humans | Child, Preschool | Male | Mitochondrial Proteins - genetics | DNA Primers | Charcot-Marie-Tooth Disease - genetics | DNA Mutational Analysis | GTP Phosphohydrolases - genetics | Pedigree | Female | High-Throughput Nucleotide Sequencing | Polymorphism, Single Nucleotide | Mutation | Charcot-Marie-Tooth Disease - diagnosis | Genetic aspects | Single nucleotide polymorphisms | Nucleotide sequencing | Multiprocessing | Genes | DNA sequencing | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Increased ER-mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress
by Bravo, Roberto and Vicencio, Jose Miguel and Parra, Valentina and Troncoso, Rodrigo and Munoz, Juan Pablo and Bui, Michael and Quiroga, Clara and Rodriguez, Andrea E and Verdejo, Hugo E and Ferreira, Jorge and Iglewski, Myriam and Chiong, Mario and Simmen, Thomas and Zorzano, Antonio and Hill, Joseph A and Rothermel, Beverly A and Szabadkai, Gyorgy and Lavandero, Sergio
Journal of Cell Science, ISSN 0021-9533, 07/2011, Volume 124, Issue 13, pp. 2143 - 2152
Increasing evidence indicates that endoplasmic reticulum (ER) stress activates the adaptive unfolded protein response (UPR), but that beyond a certain degree... 
Mitofusin 2 (Mfn2) | Mitochondria | Metabolism | Endoplasmic reticulum stress | Unfolded protein response (UPR) | INDUCED CELL-DEATH | APOPTOSIS | MECHANISM | ACTIN POLYMERIZATION | ENDOPLASMIC-RETICULUM STRESS | GLUCOSE DEPRIVATION | CELL BIOLOGY | UNFOLDED PROTEIN RESPONSE | Ca2 | DYNAMICS | PC12 CELLS | CALCIUM TRANSFER | Phosphatidylinositol Phosphates - secretion | Phosphatidylinositol Phosphates - metabolism | Calcium - metabolism | Humans | Enzyme Inhibitors - pharmacology | Stress, Physiological | Endoplasmic Reticulum - metabolism | Mitochondria - metabolism | Cell Respiration | Energy Metabolism | Oxygen Consumption - drug effects | Membrane Potential, Mitochondrial | Signal Transduction - physiology | Anti-Bacterial Agents - pharmacology | Apoptosis - physiology | HeLa Cells | Histamine Agonists - pharmacology | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text MiR-195 dependent roles of mitofusin2 in the mitochondrial dysfunction of hippocampal neurons in SAMP8 mice
by Zhang, Rui and Zhou, Huimin and Jiang, Lei and Mao, Yueran and Cui, Ximing and Xie, Bing and Cui, Dongsheng and Wang, Hui and Zhang, Qingfu and Xu, Shunjiang
Brain Research, ISSN 0006-8993, 2016, Volume 1652, pp. 135 - 143
Abstract Abnormal gene expression, including mRNAs, and microRNAs (miRNA), have been identified in the development of Alzheimer's disease (AD). Although... 
Neurology | Alzheimer's disease (AD) | miR-195 | MicroRNA | Mitofusin 2 (mfn2) | SAM mice | Hippocampus | APOPTOSIS | OXIDATIVE STRESS | FUSION | MECHANISM | DOWN-REGULATION | NEURODEGENERATION | MODEL | NEUROSCIENCES | AMYLOID-BETA | EXPRESSION | PLASTICITY | MicroRNAs - antagonists & inhibitors | Humans | Aging - drug effects | MicroRNAs - metabolism | Hippocampus - drug effects | Membrane Potential, Mitochondrial - drug effects | RNA, Messenger - metabolism | Cerebral Cortex - metabolism | HEK293 Cells | Membrane Potential, Mitochondrial - physiology | Neurons - metabolism | Cerebral Cortex - drug effects | Neurons - drug effects | Disease Models, Animal | Cell Line | Mitochondria - metabolism | Mitochondria - drug effects | Mice, Inbred Strains | Disease Progression | Hippocampus - metabolism | Animals | GTP Phosphohydrolases - metabolism | Alzheimer Disease - metabolism | MicroRNAs - genetics | Aging - metabolism | RNA | Gene expression | Neurons | Alzheimer's disease | Analysis | Genes | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Mitochondrial DNA disturbances and deregulated expression of oxidative phosphorylation and mitochondrial fusion proteins in sporadic inclusion body myositis
by Catalán-García, Marc and Garrabou, Glòria and Morén, Constanza and Guitart-Mampel, Mariona and Hernando, Adriana and Díaz-Ramos, Àngels and González-Casacuberta, Ingrid and Juárez, Diana-Luz and Bañó, Maria and Enrich-Bengoa, Jennifer and Emperador, Sonia and Milisenda, José César and Moreno, Pedro and Tobías, Ester and Zorzano, Antonio and Montoya, Julio and Cardellach, Francesc and Grau, Josep Maria
Clinical Science, ISSN 0143-5221, 2016, Volume 130, Issue 19, pp. 1741 - 1751
Sporadic inclusion body myositis (sIBM) is one of the most common myopathies in elderly people. Mitochondrial abnormalities at the histological level are... 
Mitofusin-2 | Mitochondria | Depletion | OPA1 | Sporadic inclusion body myositis | Deletions | depletion | MEDICINE, RESEARCH & EXPERIMENTAL | MITOFUSIN 2 MFN2 | deletions | KEARNS-SAYRE-SYNDROME | mitochondria | QUALITY-CONTROL | sporadic inclusion body myositis | SKELETAL-MUSCLE | FIBERS | INNATE IMMUNE-RESPONSES | DISEASE | DYNAMICS | mitofusin-2 | MUTATIONS | Leukocytes, Mononuclear - metabolism | DNA, Mitochondrial - metabolism | Humans | Middle Aged | Gene Expression Regulation | Oxidative Phosphorylation | Male | Mitochondria - metabolism | Mitochondrial Proteins - genetics | Myositis, Inclusion Body - genetics | Case-Control Studies | Mitochondria - genetics | Mitochondrial Proteins - metabolism | Female | Myositis, Inclusion Body - metabolism | Aged | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Upregulation of miR-195 accelerates oxidative stress-induced retinal endothelial cell injury by targeting mitofusin 2 in diabetic rats
by Zhang, Qingfu and Zhang, Rui and Garrett, Qian and Zhou, Huimin and Wu, Xiaoxi and Mao, Yueran and Cui, Ximing and Cui, Dongsheng and Xie, Bing and Liu, Zanchao and Jiang, Lei and Xu, Shunjiang
Molecular and Cellular Endocrinology, ISSN 0303-7207, 09/2017, Volume 452, Issue C, pp. 33 - 43
This study was performed to investigate the oxidative stress-induced miRNA changes in relation to pathogenesis of diabetic retinopathy (DR) and to establish a... 
Diabetic retinopathy | Oxidative stress | Endothelial cell | Mitofusin 2 (MFN2) | miR-195 | APOPTOSIS | ACTIVATION | BARRIER BREAKDOWN | MICRORNA EXPRESSION PROFILES | CELL BIOLOGY | TRANSPORT | INHIBITION | INFLAMMATION | ENDOCRINOLOGY & METABOLISM | RESISTANCE | MITOCHONDRIAL DYSFUNCTION | RETINOPATHY | Human Umbilical Vein Endothelial Cells | Up-Regulation | Retina - metabolism | Gene Expression - drug effects | Oxidative Stress | Humans | Cell Membrane Permeability | MicroRNAs - metabolism | Mitochondrial Proteins - genetics | Diabetic Retinopathy - pathology | Mitochondrial Proteins - metabolism | HEK293 Cells | Diabetes Mellitus, Experimental - complications | Membrane Proteins - metabolism | Diabetic Retinopathy - etiology | 3' Untranslated Regions | Diabetes Mellitus, Experimental - metabolism | Cell Survival - drug effects | Membrane Proteins - genetics | Rats | Rats, Sprague-Dawley | Diabetic Retinopathy - metabolism | Hydrogen Peroxide - metabolism | Animals | Analysis of Variance | Diabetes Mellitus, Experimental - pathology | MicroRNAs - genetics | Retina - pathology | Medical colleges | MicroRNA | Permeability | Endothelium | RNA | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text Role of the Ca2+-Calcineurin-Nuclear Factor of Activated T cell Pathway in Mitofusin-2-Mediated Immune Function of Jurkat Cells
by Xu, Xiu-Ping and Yao, Yong-Ming and Zhao, Guang-Ju and Wu, Zong-Sheng and Li, Jun-Cong and Jiang, Yun-Long and Lu, Zhong-Qiu and Hong, Guang-Liang
Chinese Medical Journal, ISSN 0366-6999, 02/2018, Volume 131, Issue 3, pp. 330 - 338
Background: Mitofusin-2 (MFN2), a well-known mitochondrial fusion protein, has been shown to participate in innate immunity, but its role in mediating adaptive... 
Nuclear Factor of Activated T cells | Calcium | Jurkat Cells | Calcineurin | Mitofusin-2 Protein | MITOFUSIN 2 MFN2 | MITOCHONDRIA | PROLIFERATION | IDENTIFICATION | MEDICINE, GENERAL & INTERNAL | ENDOPLASMIC-RETICULUM | EXPRESSION | LYMPHOCYTE-ACTIVATION | INNATE IMMUNITY | Immune response | Research | Gene expression | T cells | Analysis | Calcium ions | Enzymes | Cytokines | Metabolism | Kinases | Studies | Proteins | Mitochondria | Cell growth | Lymphocytes | Rodents | Penicillin | Cell cycle | Apoptosis | Index Medicus | Original | Calcineurin; Calcium; Jurkat Cells; Mitofusin-2 Protein; Nuclear Factor of Activated T cells
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Mitofusin 2 gene mutation causing early-onset cmt2a with different progressive courses
by Lv, He and Wang, Lu and Li, Wurong and Qiao, Xiaohui and Li, Yuexing and Wang, Zhaoxia and Yuan, Yun
Clinical Neuropathology, ISSN 0722-5091, 01/2013, Volume 32, Issue 1, pp. 16 - 23
Charcot-Marie-Tooth disease Type 2A2 (CMT2A2), caused by mitofusin 2 (MFN2) genes, has been clinically classified into two types: severe early-onset and mild... 
Marie | Opticatrophy | Gene mutation | Neuropathology | Charcot | Tooth2A2(CMT2A2) | Mitofusin 2(MFN2) | Charcot-Marie-Tooth 2A2(CMT2A2) | gene mutation | MARIE-TOOTH DISEASE | mitofusin 2(MFN2) | PATHOLOGY | CLINICAL NEUROLOGY | FEATURES | optic atrophy | MFN2 MUTATIONS | NEUROPATHY | FAMILIES | TYPE-2 | neuropathology | Humans | Middle Aged | Child, Preschool | Molecular Sequence Data | Genotype | Male | Mitochondrial Proteins - genetics | Charcot-Marie-Tooth Disease - pathology | Disease Progression | Charcot-Marie-Tooth Disease - genetics | Young Adult | Phenotype | GTP Phosphohydrolases - genetics | Pedigree | Base Sequence | Adolescent | Age of Onset | Adult | Female | Charcot-Marie-Tooth Disease - physiopathology | Mutation | Child
Journal Article
Details down arrow
12. Full Text MFN2 mutation distribution and genotype/phenotype correlation in Charcot-Marie-Tooth type 2
by Verhoeven, Kristien and Claeys, Kristl G and Züchner, Stephan and Schröder, J. Michael and Weis, Joachim and Ceuterick, Chantal and Jordanova, Albena and Nelis, Eva and De Vriendt, Els and Van Hul, Matthias and Seeman, Pavel and Mazanec, Radim and Saifi, Gulam Mustafa and Szigeti, Kinga and Mancias, Pedro and Butler, Ian J and Kochanski, Andrzej and Ryniewicz, Barbara and De Bleecker, Jan and Van Den Bergh, Peter and Verellen, Christine and Van Coster, Rudy and Goemans, Nathalie and Auer-Grumbach, Michaela and Robberecht, Wim and Milic Rasic, Vedrana and Nevo, Yoram and Tournev, Ivajlo and Guergueltcheva, Velina and Roelens, Filip and Vieregge, Peter and Vinci, Paolo and Moreno, Maria Teresa and Christen, H.-J and Shy, Michael E and Lupski, James R and Vance, Jeffery M and De Jonghe, Peter and Timmerman, Vincent
Brain, ISSN 0006-8950, 2006, Volume 129, Issue 8, pp. 2093 - 2102
Mutations in mitofusin 2 (MFN2) have been reported in Charcot-Marie-Tooth type 2 (CMT2) families. To study the distribution of mutations in MFN2 we screened... 
Mitofusin 2 | Charcot-Marie-Tooth type 2 | Genotype-phenotype correlation | NEUROPATHY | GENE | ATROPHY | genotype-phenotype correlation | DISEASE TYPE-2 | MITOFUSIN-2 | mitofusin 2 | NEUROSCIENCES | CLINICAL NEUROLOGY | FEATURES | Severity of Illness Index | GTP Phosphohydrolases | Membrane Proteins - genetics | Humans | Middle Aged | Child, Preschool | Electrophysiology | Genotype | Mitochondrial Proteins - genetics | Charcot-Marie-Tooth Disease - pathology | Microscopy, Electron | Charcot-Marie-Tooth Disease - genetics | Sural Nerve - ultrastructure | Phenotype | Adolescent | Age of Onset | Adult | Aged | Charcot-Marie-Tooth Disease - physiopathology | Mutation | Child | Index Medicus | Abridged Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
13. Full Text Deubiquitinating enzymes regulate PARK2-mediated mitophagy
by Wang, Yuqing and Serricchio, Mauro and Jauregui, Miluska and Shanbhag, Riya and Stoltz, Tasha and Di Paolo, Caitlin T and Kim, Peter K and McQuibban, G Angus
Autophagy, ISSN 1554-8627, 04/2015, Volume 11, Issue 4, pp. 595 - 606
The selective degradation of mitochondria by the process of autophagy, termed mitophagy, is one of the major mechanisms of mitochondrial quality control. The... 
USP35 | l-USP35, long form of ubiquitin specific peptidase 35 | s-USP35, short form of ubiquitin specific peptidase 35 | TOMM20, translocase of outer mitochondrial membrane 20 homolog (yeast) | USP, ubiquitin specific peptidase | MTS | PARK2 | SYNJ2BP, synaptojanin 2 binding protein | DUB | neurodegenerative diseases | CCCP | Cer, cerulean | PARK2, parkin RBR E3 ubiquitin protein ligase | USP30 | MFN2, mitofusin 2 | OMM, outer mitochondrial membrane | GFP, green fluorescent protein | autophagy | DsRed, Discosoma sp. red fluorescent protein | deubiquitinating enzyme | PINK1, PTEN-induced putative kinase 1 | deubiquitinating enzymes | carbonyl cyanide m-chlorophenylhydrazone | ubiquitin | mitochondrial dynamics | mitophagy | DMSO, dimethyl sulfoxide | GAPDH, glyceraldehyde 3-phosphate dehydrogenase | HA, human influenza hemagglutinin | mitochondrial targeting sequence | Deubiquitinating enzymes | Neurodegenerative diseases | Mitochondrial dynamics | Mitophagy | Autophagy | Ubiqui tin | FUSION | P62/SQSTM1 | RECEPTOR | MITOCHONDRIAL FISSION | CELL BIOLOGY | PARKIN | DEGRADATION | PROMOTES | Endopeptidases - metabolism | Mitochondrial Proteins - metabolism | Humans | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Cytosol - metabolism | Autophagy - physiology | Mitochondria - metabolism | Thiolester Hydrolases - metabolism | Ubiquitination - physiology | Mitochondrial Degradation - physiology | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
14. Full Text Ursodeoxycholic Acid Improves Mitochondrial Function and Redistributes Drp1 in Fibroblasts from Patients with Either Sporadic or Familial Alzheimer's Disease
by Bell, Simon M and Barnes, Katy and Clemmens, Hannah and Al-Rafiah, Aziza R and Al-ofi, Ebtisam A and Leech, Vicki and Bandmann, Oliver and Shaw, Pamela J and Blackburn, Daniel J and Ferraiuolo, Laura and Mortiboys, Heather
Journal of Molecular Biology, ISSN 0022-2836, 10/2018, Volume 430, Issue 21, pp. 3942 - 3953
Alzheimer's disease (AD) is the leading cause of dementia worldwide. Mitochondrial abnormalities have been identified in many cell types in AD, with deficits... 
neurodegeneration | treatment | UDCA | presenilin | mitochondrial morphology | APP/PS1 MICE | APOPTOSIS | CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYNAPTIC DAMAGE | CYTOCHROME-OXIDASE | IMPAIRMENT | MUTATION | DYNAMIN-RELATED PROTEIN-1 | DYSFUNCTION | Ursodiol | Genetic aspects | Alzheimer's disease | Analysis | PSEN1, presenilin 1 | Drp1, dynamin-related protein | Mfn2, mitofusin 2 | Opa1, optic atrophy 1 | Mfn1, mitofusin 1
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
15. Full Text SIRT5 regulation of ammonia-induced autophagy and mitophagy
by Polletta, Lucia and Vernucci, Enza and Carnevale, Ilaria and Arcangeli, Tania and Rotili, Dante and Palmerio, Silvia and Steegborn, Clemens and Nowak, Theresa and Schutkowski, Mike and Pellegrini, Laura and Sansone, Luigi and Villanova, Lidia and Runci, Alessandra and Pucci, Bruna and Morgante, Emanuela and Fini, Massimo and Mai, Antonello and Russo, Matteo A and Tafani, Marco
Autophagy, ISSN 1554-8627, 02/2015, Volume 11, Issue 2, pp. 253 - 270
In liver the mitochondrial sirtuin, SIRT5, controls ammonia detoxification by regulating CPS1, the first enzyme of the urea cycle. However, while SIRT5 is... 
PEG, polyethylene glycol | MAP1LC3B, microtubule-associated protein 1 light chain 3 β | GLUL, glutamate-ammonia ligase | ammonia | ATG, autophagy-related | BPTES, bis-2-(5-phenylacetamido-1, 3, 4-thiadiazol-2-yl)ethyl sulfide | glutamine | GABARAPL2, GABA(A) receptor-associated protein-like 2 | succinylation | PARK2, parkin RBR E3 ubiquitin protein ligase | GABARAP, GABA(A) receptor-associated protein | OPA1, optic atrophy 1 (autosomal dominant) | COX4I1, cytochrome c oxidase subunit IV isoform 1 | MFN2, mitofusin 2 | GLUD1, glutamate dehydrogenase 1 | autophagy | hexachlorophene, 2, 2′-methylenebis(3, 4, 6-trichlorophenol) | sirtuin 5 | ACTB, actin, β | BNIP3, BCL2/adenovirus E1B 19kDa interacting protein 3 | TEM, transmission electron microscopy | mitochondrial dynamics | molecular rehabilitation | TCA, tricarboxylic acid cycle | mitophagy | SQSTM1, sequestosome 1 | PINK1, PTEN induced putative kinase 1 | glutaminase | SIRT5, sirtuin 5 | GLS, glutaminase | CPS1, carbamoyl-phosphate synthase 1, mitochondrial | Ammonia | Mitochondrial dynamics sirtuin 5 | Succinylation | Mitophagy | Autophagy | Glutaminase | Molecular rehabilitation | Glutamine | OXIDATIVE STRESS | PROTEIN | MECHANISM | PHOSPHATE-DEPENDENT GLUTAMINASE | SIRTUINS | CELL BIOLOGY | UREA CYCLE | CANCER METABOLISM | GLUTAMINOLYSIS | DEACETYLASE SIRT1 | CELL-METABOLISM | Proteolysis - drug effects | Mitochondrial Degradation - drug effects | Humans | Ubiquitin-Protein Ligases - metabolism | Ammonia - pharmacology | Autophagy - physiology | Glutaminase - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Mitochondrial Degradation - physiology | Sirtuins - metabolism | Autophagy - drug effects | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights