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1. Full Text Valosin-Containing Protein (VCP) Is Required for Autophagy and Is Disrupted in VCP Disease
by Jeong-Sun Ju and Rodrigo A. Fuentealba and Sara E. Miller and Erin Jackson and David Piwnica-Worms and Robert H. Baloh and Conrad C. Weihl
The Journal of Cell Biology, ISSN 0021-9525, 12/2009, Volume 187, Issue 6, pp. 875 - 888
Mutations in valosin-containing protein (VCP) cause inclusion body myopathy (IBM), Paget's disease of the bone, and frontotemporal dementia (IBMPFD). Patient... 
Proteins | Muscular diseases | Transgenic animals | Inclusion bodies | Cell nucleus | Cell lines | Muscles | Small interfering RNA | Frontotemporal dementia | Skeletal muscle | GENE-MUTATIONS | NEURODEGENERATIVE DISEASE | SKELETAL-MUSCLE | IN-VITRO | AAA ATPASE CDC48/P97 | DEMENTIA | INCLUSION-BODY MYOPATHY | TDP-43 ACCUMULATION | FRONTOTEMPORAL LOBAR DEGENERATION | PAGET-DISEASE | CELL BIOLOGY | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Chloroquine | Humans | Valosin Containing Protein | Ubiquitin - metabolism | Recombinant Fusion Proteins - metabolism | Case-Control Studies | Osteitis Deformans - genetics | Osteitis Deformans - chemically induced | DNA-Binding Proteins - metabolism | Myositis, Inclusion Body - enzymology | Transfection | Quadriceps Muscle - enzymology | RNA Interference | Cell Cycle Proteins - genetics | Myositis, Inclusion Body - pathology | Female | Autophagy - genetics | Quadriceps Muscle - pathology | Disease Models, Animal | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Cell Line | Heat-Shock Proteins - metabolism | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Mice, Transgenic | Myositis, Inclusion Body - genetics | Osteitis Deformans - enzymology | Osteitis Deformans - pathology | Animals | Biopsy | Frontotemporal Dementia - chemically induced | Frontotemporal Dementia - enzymology | Myositis, Inclusion Body - chemically induced | Adenosine Triphosphatases - genetics | Mice | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Autophagy (Cytology) | Gene mutations | Genetic aspects | Research | Binding proteins | Health aspects | Risk factors | Brain diseases | Index Medicus
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2. Full Text Phosphoproteome analysis of capacitated human sperm: Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation
by Ficarro, Scott and Chertihin, Olga and Westbrook, V. Anne and White, Forest and Jayes, Friederike and Kalab, Petr and Marto, Jarrod A and Shabanowitz, Jeffrey and Herr, John C and Hunt, Donald F and Visconti, Pablo E
Journal of Biological Chemistry, ISSN 0021-9258, 03/2003, Volume 278, Issue 13, pp. 11579 - 11589
Before fertilization can occur, mammalian sperm must undergo capacitation, a process that requires a cyclic AMP-dependent increase in tyrosine phosphorylation.... 
HUMAN SPERMATOZOA | MEMBRANE-FUSION | ACROSOMAL EXOCYTOSIS | ELECTROPHORESIS | MOUSE SPERMATOZOA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ION AFFINITY-CHROMATOGRAPHY | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | P97 | Amino Acid Sequence | Phosphorylation | Humans | Valosin Containing Protein | Cell Cycle Proteins - metabolism | Molecular Sequence Data | Male | Proteome | Spermatozoa - metabolism | Phosphoproteins - metabolism | Tyrosine - metabolism | Carrier Proteins - metabolism | Adenosine Triphosphatases | Sperm Capacitation | Mass Spectrometry | Microscopy, Fluorescence
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3. Full Text Valosin-containing protein (VCP) is a novel IQ motif-containing GTPase activating protein 1 (IQGAP1)-interacting protein
by Itoh, Norimichi and Nagai, Taku and Watanabe, Takashi and Taki, Kentaro and Nabeshima, Toshitaka and Kaibuchi, Kozo and Yamada, Kiyofumi
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 12/2017, Volume 493, Issue 4, pp. 1384 - 1389
Scaffold proteins play a pivotal role in making protein complexes, and organize binding partners into a functional unit to enhance specific signaling pathways.... 
VCP | Proteomics | IQGAP1 | TARGET | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | PAGET-DISEASE | CDC42 | EFFECTOR | BIOPHYSICS | RAC1 | BINDING | SCAFFOLDING PROTEINS | Immunohistochemistry | ras GTPase-Activating Proteins - chemistry | Humans | Valosin Containing Protein | Osteitis Deformans - metabolism | Osteitis Deformans - genetics | Cell Cycle Proteins - chemistry | Frontotemporal Dementia - metabolism | ras GTPase-Activating Proteins - genetics | Muscular Dystrophies, Limb-Girdle - genetics | HEK293 Cells | Cell Cycle Proteins - genetics | Neurons - metabolism | Protein Interaction Domains and Motifs | Frontotemporal Dementia - genetics | Recombinant Proteins - metabolism | ras GTPase-Activating Proteins - metabolism | Mutagenesis, Site-Directed | Cell Cycle Proteins - metabolism | Mutant Proteins - genetics | Adenosine Triphosphatases - metabolism | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Myositis, Inclusion Body - genetics | Hippocampus - metabolism | Muscular Dystrophies, Limb-Girdle - metabolism | Mutant Proteins - chemistry | Adenosine Triphosphatases - chemistry | Myositis, Inclusion Body - metabolism | Adenosine Triphosphatases - genetics | HeLa Cells | Amino Acid Substitution | Proteins | Physiological aspects | Protein binding | Medical colleges | Neurons | Index Medicus
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4. Full Text Valosin-containing protein (VCP) mutations in sporadic amyotrophic lateral sclerosis
by Abramzon, Yevgeniya and Johnson, Janel O and Scholz, Sonja W and Taylor, J.P and Brunetti, Maura and Calvo, Andrea and Mandrioli, Jessica and Benatar, Michael and Mora, Gabriele and Restagno, Gabriella and Chiò, Adriano and Traynor, Bryan J
Neurobiology of Aging, ISSN 0197-4580, 2012, Volume 33, Issue 9, pp. 2231.e1 - 2231.e6
Abstract We recently reported that mutations in the valosin-containing protein (VCP) gene are a cause of 1%–2% of familial amyotrophic lateral sclerosis (ALS)... 
Neurology | Internal Medicine | Mutations | Amyotrophic lateral sclerosis | Sporadic disease | Valosin-containing protein | FUS | FRONTOTEMPORAL DEMENTIA | ALS | NEUROSCIENCES | PAGET-DISEASE | GERIATRICS & GERONTOLOGY | INCLUSION-BODY MYOPATHY | TDP-43 | BONE | Amyotrophic Lateral Sclerosis - physiopathology | United States | Amyotrophic Lateral Sclerosis - genetics | Humans | Middle Aged | Valosin Containing Protein | Male | Mutation - genetics | DNA Mutational Analysis | Cell Cycle Proteins - genetics | Female | Italy | Adenosine Triphosphatases - genetics | Aged | Amyotrophic Lateral Sclerosis - epidemiology | Genes | Genetic aspects | sporadic disease | valosin-containing protein | mutations
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5. Full Text Valosin-containing protein mutation and Parkinson's disease
by Chan, Nora and Le, Cindy and Shieh, Perry and Mozaffar, Tahseen and Khare, Manaswitha and Bronstein, Jeff and Kimonis, Virginia
Parkinsonism and Related Disorders, ISSN 1353-8020, 01/2012, Volume 18, Issue 1, pp. 107 - 109
BONE | INCLUSION-BODY MYOPATHY | PAGET-DISEASE | CLINICAL NEUROLOGY | FRONTOTEMPORAL DEMENTIA | Humans | Middle Aged | Valosin Containing Protein | Male | Parkinson Disease - genetics | Mutation - genetics | Pedigree | Aged, 80 and over | Cell Cycle Proteins - genetics | Parkinson Disease - diagnosis | Female | Adenosine Triphosphatases - genetics | Aged
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6. Full Text Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
by Wymer, Jill and Darvish, Daniel and Kimonis, Virginia E and Mumm, Steven and Whyte, Michael P and Mehta, Sarju G and Kovach, Margaret J and Pestronk, Alan and Watts, Giles D J
Nature Genetics, ISSN 1061-4036, 04/2004, Volume 36, Issue 4, pp. 377 - 381
Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia (IBMPFD) is a dominant progressive disorder that maps to chromosome... 
PATHWAYS | DOMAIN | GENE | UBIQUITIN | GENETICS & HEREDITY | DISORDERS | ENDOPLASMIC-RETICULUM | MUTATIONS | CHAPERONE | AAA-ATPASE P97 | FAMILY | Immunohistochemistry | Humans | Valosin Containing Protein | Male | Chromosome Mapping | Chromosomes, Human, Pair 9 | Osteitis Deformans - genetics | Adenosine Triphosphatases | Muscular Diseases - physiopathology | Pedigree | Osteitis Deformans - physiopathology | Cell Cycle Proteins - genetics | Female | Muscular Diseases - genetics | Mutation | Cell Cycle Proteins - physiology | Osteitis deformans | Muscle diseases | Genetic aspects | Research | Dementia
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7. Full Text Valosin-containing protein (VCP)/p97 segregase mediates proteolytic processing of Cockayne Syndrome Group B (CSB) in damaged chromatin
by He, Jinshan and Zhu, Qianzheng and Wani, Gulzar and Sharma, Nidhi and Wani, Altaf A
Journal of Biological Chemistry, ISSN 0021-9258, 04/2016, Volume 291, Issue 14, pp. 7396 - 7408
Cockayne syndrome group A and B (CSB) proteins act in transcription-coupled repair, a subpathway of nucleotide excision repair. Here we demonstrate that... 
RNA-POLYMERASE-II | UV-SENSITIVE SYNDROME | UBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | IN-VIVO | AAA-ATPASE | DOUBLE-STRAND BREAKS | XPC | TRANSCRIPTION-COUPLED REPAIR | NUCLEOTIDE EXCISION-REPAIR | Chromatin - metabolism | Valosin Containing Protein | DNA Repair Enzymes - genetics | Hexosyltransferases - metabolism | LIM Domain Proteins - metabolism | DNA-Binding Proteins - metabolism | Poly-ADP-Ribose Binding Proteins | Proteolysis | DNA Repair Enzymes - metabolism | Cell Cycle Proteins - genetics | Cullin Proteins - metabolism | DNA Helicases - genetics | Cell Line | ATPases Associated with Diverse Cellular Activities | Cell Cycle Proteins - metabolism | Hexosyltransferases - genetics | Adenosine Triphosphatases - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Ultraviolet Rays - adverse effects | Cullin Proteins - genetics | Proteasome Endopeptidase Complex - genetics | Proteins - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | DNA Helicases - metabolism | Carrier Proteins - metabolism | Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | LIM Domain Proteins - genetics | Ubiquitination - radiation effects | Adenosine Triphosphatases - genetics | DNA Damage | Proteasome Endopeptidase Complex - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Chromatin - genetics | Ubiquitination - genetics | Cockayne syndrome group B protein | DNA and Chromosomes | valosin-containing protein | DNA damage | DNA repair | nucleotide excision repair | protein degradation | ubiquitin | transcription-coupled repair
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8. Full Text Heterozygous mutations in valosin-containing protein (VCP) and resistance to VCP inhibitors
by Bastola, P and Bilkis, R and De Souza, C and Minn, K and Chien, J
SCIENTIFIC REPORTS, ISSN 2045-2322, 07/2019, Volume 9, Issue 1, pp. 11002 - 15
In recent years, multiple studies including ours have reported on the mechanism of resistance towards valosin-containing protein (VCP) inhibitors. While all... 
TARGET | CLEARANCE | P97 AAA-ATPASE | MULTIDISCIPLINARY SCIENCES | DISEASE | VCP/P97 | DEGRADATION | CANCER | Proteins | CRISPR | Zygosity | Transcription | Alleles | Frameshift mutation | Mutation | Deoxyribonucleic acid--DNA | Valosin-containing protein | DNA sequencing
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9. Full Text Novel Ubiquitin Neuropathology in Frontotemporal Dementia With Valosin-Containing Protein Gene Mutations
by Forman, Mark S and Mackenzie, Ian R and Cairns, Nigel J and Swanson, Eric and Boyer, Philip J and Drachman, David A and Jhaveri, Bharati S and Karlawish, Jason H and Pestronk, Alan and Smith, Thomas W and Tu, Pang-Hsien and Watts, Giles D. J and Markesbery, William R and Smith, Charles D and Kimonis, Virginia E
Journal of Neuropathology and Experimental Neurology, ISSN 0022-3069, 06/2006, Volume 65, Issue 6, pp. 571 - 581
Frontotemporal dementia (FTD) with inclusion body myopathy and Paget disease of bone (IBMPFD) is a rare, autosomal-dominant disorder caused by mutations in the... 
Ubiquitin | Neurodegenerative disease | Inclusion body myopathy | Paget disease of bone | Frontotemporal dementia | Valosin-containing protein | valosin-containing protein | neurodegenerative disease | ATPASE ACTIVITY | LOBAR DEGENERATION | inclusion body myopathy | frontotemporal dementia | MOTOR-NEURON DISEASE | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | NEUROSCIENCES | ubiquitin | NEURODEGENERATIVE DISEASES | PAGET-DISEASE | CLINICAL NEUROLOGY | PATHOLOGICAL DIAGNOSIS | INCLUSION-BODY MYOPATHY | ENDOPLASMIC-RETICULUM | INTRANUCLEAR INCLUSIONS | Blotting, Western - methods | Dementia - pathology | Humans | Valosin Containing Protein | Ubiquitin - metabolism | Male | Dementia - genetics | Mutation - genetics | Myositis, Inclusion Body - genetics | Osteitis Deformans - genetics | Immunohistochemistry - methods | Dementia - metabolism | Osteitis Deformans - pathology | Adenosine Triphosphatases | Cell Cycle Proteins - genetics | Myositis, Inclusion Body - pathology | Female
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10. Full Text Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations
by Ritz, Danilo and Vuk, Maja and Kirchner, Philipp and Bug, Monika and Schütz, Sabina and Hayer, Arnold and Bremer, Sebastian and Lusk, Caleb and Baloh, Robert H and Lee, Houkeun and Glatter, Timo and Gstaiger, Matthias and Aebersold, Ruedi and Weihl, Conrad C and Meyer, Hemmo
Nature Cell Biology, ISSN 1465-7392, 09/2011, Volume 13, Issue 9, pp. 1116 - 1124
The AAA-ATPase VCP (also known as p97) cooperates with distinct cofactors to process ubiquitylated proteins in different cellular pathways(1-3). VCP missense... 
UBIQUITIN-SELECTIVE CHAPERONE | VALOSIN-CONTAINING PROTEIN | COMPLEX | FRONTOTEMPORAL DEMENTIA | CDC48/P97 | AAA-ATPASE | ENDOPLASMIC-RETICULUM | MYOPATHY | PAGET-DISEASE | P97 | CELL BIOLOGY | Humans | Valosin Containing Protein | Endosomal Sorting Complexes Required for Transport - genetics | Endosomes - metabolism | Lysosomes - metabolism | RNA Interference | Mass Spectrometry | Endosomes - ultrastructure | HEK293 Cells | Cell Cycle Proteins - genetics | Sarcolemma - metabolism | Ubiquitinated Proteins - metabolism | Muscular Diseases - metabolism | Cell Cycle Proteins - metabolism | Cells, Cultured | Endosomal Sorting Complexes Required for Transport - metabolism | Adenosine Triphosphatases - metabolism | Caveolin 1 - genetics | Rats | Muscular Diseases - pathology | Microscopy, Electron | Blotting, Western | Caveolin 1 - metabolism | Lysosomes - ultrastructure | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Cell Line, Tumor | Protein Binding | Luminescent Proteins - genetics | Ubiquitinated Proteins - genetics | Adenosine Triphosphatases - genetics | Muscular Diseases - genetics | Mutation | Microscopy, Fluorescence | Luminescent Proteins - metabolism | Usage | Degeneration (Pathology) | Gene mutations | Genetic aspects | Diagnosis | Research | Mass spectrometry | Health aspects | Risk factors
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11. Full Text Structural basis for ovarian tumor domain-containing protein 1 (otu1) binding to p97/valosin-containing protein (vcp)
by Kim, Su Jin and Cho, Jinhong and Song, Eun Joo and Kim, Soo Jin and Kim, Ho Min and Lee, Kyung Eun and Suh, Se Won and Kim, Eunice EunKyeong
Journal of Biological Chemistry, ISSN 0021-9258, 1761, Volume 289, Issue 18, pp. 12264 - 12274
Background: Ovarian tumor domain-containing protein 1 (OTU1) acts as a deubiquitinating enzyme in the endoplasmic reticulum-associated degradation (ERAD)... 
Site-directed Mutagenesis | Crystal Structure | SUITE | COMPLEX | UBIQUITIN-PROTEASOME SYSTEM | COFACTORS | Deubiquitination | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY CONTROL | Electron Microscopy (EM) | P97 | Isothermal Titration Calorimetry | AAA ATPASE P97/VCP | ENDOPLASMIC-RETICULUM | DEGRADATION ERAD | ATPases | ER-associated Degradation | Protein-Protein Interactions | Humans | Valosin Containing Protein | Immunoblotting | Cell Cycle Proteins - chemistry | Multiprotein Complexes - metabolism | HEK293 Cells | Cell Cycle Proteins - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Endoplasmic Reticulum-Associated Degradation - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | Signal Transduction - genetics | Binding Sites - genetics | Saccharomyces cerevisiae Proteins - genetics | Microscopy, Electron | Protein Interaction Mapping | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Mutation | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | Protein Structure and Folding
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12. Full Text KUS121, a valosin-containing protein modulator, attenuates ischemic stroke via preventing ATP depletion
by Kinoshita, H and Maki, T and Yasuda, K and Kishida, N and Sasaoka, N and Takagi, Y and Kakizuka, A and Takahashi, R
SCIENTIFIC REPORTS, ISSN 2045-2322, 08/2019, Volume 9, Issue 1, pp. 11519 - 9
Reduced adenosine triphosphate (ATP) levels in ischemic stroke constitute an upstream contributor to neuronal cell death. We have recently created a small... 
SURVIVAL | MYELIN | MODELS | MULTIDISCIPLINARY SCIENCES | RANDOMIZED-TRIAL | DEATH | MECHANISMS | GLUCOSE DEPRIVATION | STRESS | ISCHEMIA/REPERFUSION | OLIGODENDROCYTES | Cerebral infarction | Neuroprotection | Cell culture | Stroke | Animal models | Cortex | Ischemia | Cell death | Cerebral blood flow | ATP | Adenosine triphosphate | Valosin-containing protein | Apoptosis
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13. Full Text mTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy
by Ching, James K and Elizabeth, Sarita V and Ju, Jeong-Sun and Lusk, Caleb and Pittman, Sara K and Weihl, Conrad C
Human Molecular Genetics, ISSN 0964-6906, 03/2013, Volume 22, Issue 6, pp. 1167 - 1179
Autophagy is dysfunctional in many degenerative diseases including myopathies. Mutations in valosin-containing protein (VCP) cause inclusion body myopathy... 
ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | VCP MUTATIONS | MOUSE MODEL | GENETICS & HEREDITY | MUSCLE | DEGRADATION | AUTOPHAGY | INHIBITOR | PAGET-DISEASE | P97 | DEGENERATION | Signal Transduction | TOR Serine-Threonine Kinases - metabolism | Myositis, Inclusion Body - physiopathology | Humans | Mice, Inbred C57BL | Valosin Containing Protein | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Mice, Transgenic | Myositis, Inclusion Body - genetics | Autophagy | Vacuoles - pathology | Animals | TOR Serine-Threonine Kinases - genetics | Cell Cycle Proteins - genetics | Myositis, Inclusion Body - pathology | Vacuoles - metabolism | Myositis, Inclusion Body - metabolism | Adenosine Triphosphatases - genetics | Mice | TOR protein | Phosphorylation | valosin-containing protein | Phagosomes | AKT protein | Amino acids | Amyotrophic lateral sclerosis | Rapamycin | Insulin | Atrophy | Paget's disease | Signal transduction | Inclusion bodies | Nutrients | Mutation | Frontotemporal dementia | Phagocytosis | FOXO3 protein | Myopathy
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14. Full Text The N-terminal region of the ubiquitin regulatory X (UBX) domain-containing protein 1 (UBXD1) modulates interdomain communication within the valosin-containing protein p97
by Trusch, Franziska and Matena, Anja and Vuk, Maja and Koerver, Lisa and Knævelsrud, Helene and Freemont, Paul S and Meyer, Hemmo and Bayer, Peter
Journal of Biological Chemistry, ISSN 0021-9258, 12/2015, Volume 290, Issue 49, pp. 29414 - 29427
Valosin-containing protein/p97 is an ATP-driven protein segregase that cooperates with distinct protein cofactors to control various aspects of cellular... 
CIRCULAR-DICHROISM SPECTRA | ATPASE ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE | AAA-ATPASE | VCP/P97 | CRYSTAL-STRUCTURES | SECONDARY STRUCTURE | SUBSTOICHIOMETRIC INHIBITION | MOLECULAR-BASIS | CAVEOLIN-1 | Protein Structure, Tertiary | Cell Line | Green Fluorescent Proteins - metabolism | Magnetic Resonance Spectroscopy | Humans | Valosin Containing Protein | Cell Cycle Proteins - metabolism | Ubiquitin - chemistry | Adenosine Triphosphatases - metabolism | Homeostasis | Nuclear Proteins - metabolism | Endosomes - metabolism | Amino Acid Motifs | Caveolin 1 - metabolism | Carrier Proteins - metabolism | Lysosomes - metabolism | Protein Binding | Carrier Proteins - chemistry | Epitopes - chemistry | Mutation | Fluorescence Polarization | Binding Sites | Circular Dichroism | protein structure | Protein Structure and Folding | endosome | UBXD1 | ATPase | nuclear magnetic resonance (NMR) | protein-protein interaction | p97
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15. Full Text B-Cell receptor-associated protein 31 regulates the expression of valosin-containing protein through Elf2
by Jia, Cong-Cong and Du, Juan and Liu, Xia and Jiang, Rui and Huang, Yongye and Wang, Tianyi and Hou, Yue and Wang, Bing
Cellular Physiology and Biochemistry, ISSN 1015-8987, 12/2018, Volume 51, Issue 4, pp. 1799 - 1814
Background/conserved, ubiquitously expressed, polytopic integral membrane protein in the endoplasmic reticulum (ER) that is involved in the regulation of... 
Bap31 | ERAD | CFTRδF508 | VCP | Elf2 | CNS diseases | PHYSIOLOGY | EXPORT | CANCER | CELL BIOLOGY | ELEVATED EXPRESSION | CFTR Delta F508 | PROTEASOME | DEGRADATION | ENDOPLASMIC-RETICULUM | STRESS | PROMOTES | Cell Line | Animals | Valosin Containing Protein - genetics | Membrane Proteins - genetics | RNA, Messenger - genetics | Gene Expression Regulation | Mice | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Mice, Knockout | Immunoglobulins | Transcription factors | Genes | Proteins | Neurodegeneration | Plasmids | Transgenic animals | Cell cycle | Regulation | Endoplasmic reticulum | Binding sites | Cancer | Apoptosis | CFTR∆F508
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