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Journal Article
2008, Advances in biochemical engineering/biotechnology, ISBN 354068817X, Volume 110., xiv, 272
Book
Molecular Cell, ISSN 1097-2765, 09/2010, Volume 39, Issue 6, pp. 963 - 974
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, Issue 1, pp. 375 - 404
Inactivation of the transcription factor p53, through either direct mutation or aberrations in one of its many regulatory pathways, is a hallmark of virtually... 
cancer therapy | signaling pathways | protein evolution | drug design | p53 family | small-molecule stabilizers | Protein evolution | Signaling pathways | Drug design | Small-molecule stabilizers | P53 family | Cancer therapy | DNA-BINDING DOMAIN | TRANSIENT PROTEIN STATES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-CYCLE ARREST | TUMOR-SUPPRESSOR P53 | CORE-DOMAIN | STRUCTURAL BASIS | SMALL-MOLECULE INHIBITORS | MUTANT P53 | TETRAMERIZATION DOMAIN | TRANSACTIVATION DOMAIN | Neoplasms - metabolism | Proto-Oncogene Proteins c-mdm2 - genetics | Antineoplastic Agents, Alkylating - chemical synthesis | Humans | Protein Multimerization | Gene Expression Regulation, Neoplastic | Proto-Oncogene Proteins - chemistry | Molecular Targeted Therapy | Proto-Oncogene Proteins c-mdm2 - chemistry | Tumor Suppressor Protein p53 - genetics | Neoplasms - genetics | Tumor Suppressor Protein p53 - agonists | Drug Design | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-mdm2 - antagonists & inhibitors | Proto-Oncogene Proteins c-mdm2 - metabolism | Proto-Oncogene Proteins - metabolism | Proto-Oncogene Proteins - antagonists & inhibitors | Protein Structure, Secondary | Signal Transduction | Tumor Suppressor Protein p53 - metabolism | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Clinical Trials as Topic | Nuclear Proteins - chemistry | Neoplasms - drug therapy | Antineoplastic Agents, Alkylating - therapeutic use | Animals | Nuclear Proteins - antagonists & inhibitors | Molecular Docking Simulation | Tumor Suppressor Protein p53 - chemistry | Mutation | Neoplasms - pathology | Transcription factors | Care and treatment | Health aspects | Methods | Cancer
Journal Article
Biochemical Journal, ISSN 0264-6021, 04/2017, Volume 474, Issue 8, pp. 1417 - 1438
Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid... 
EUKARYOTIC STRESS GRANULES | MUTANT FUS PROTEINS | MULTISYSTEM PROTEINOPATHY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHASE-TRANSITION | TARDBP MUTATIONS | HNRNP A1 | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS | NEURODEGENERATIVE DISEASES | Proteostasis Deficiencies - metabolism | RNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - metabolism | Humans | Prion Proteins - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | RNA-Binding Protein FUS - chemistry | TDP-43 Proteinopathies - genetics | Protein Domains | TDP-43 Proteinopathies - pathology | Prion Proteins - chemistry | Prion Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | Calmodulin-Binding Proteins - genetics | Frontotemporal Dementia - genetics | Cytoplasmic Granules | Neurodegenerative Diseases - pathology | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Proteins - chemistry | TDP-43 Proteinopathies - metabolism | Proteostasis Deficiencies - pathology | RNA-Binding Protein FUS - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Neurodegenerative Diseases - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | RNA-Binding Protein FUS - metabolism | Neurodegenerative Diseases - metabolism | TATA-Binding Protein Associated Factors - chemistry | DNA-Binding Proteins - genetics | TATA-Binding Protein Associated Factors - genetics | DNA-Binding Proteins - chemistry | Heterogeneous Nuclear Ribonucleoprotein A1 | Proteostasis Deficiencies - genetics | Amyotrophic Lateral Sclerosis - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Mutation | RNA-Binding Proteins - metabolism | RNA-Binding Protein EWS
Journal Article