نتائج البحث - "FA, fluorescence anisotropy"

1

Disease-associated mutations in a bifunctional aminoacyl-tRNA synthetase gene elicit the integrated stress response

المؤلفون: Karin Musier-Forsyth, Ronald C. Wek, Sheree A. Wek, Marina Bakhtina, William A. Cantara, Nathan T. Kudlapur, Danni Jin

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: Male, multisynthetase complex, ATF4, activating transcription factor 4, aminoacyl-tRNA synthetases, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, RNA, Transfer, enzyme kinetics, AIMP, ARS-complex interacting multifunctional protein, PERK, PKR-like endoplasmic reticulum kinase, glutamyl-prolyl-tRNA synthetase, Protein biosynthesis, Amino Acids, CD, circular dichroism, Amino acid activation, chemistry.chemical_classification, Mutation, FA, fluorescence anisotropy, Editors' Pick, integrated stress response, ARS, aminoacyl-tRNA synthetase, Amino acid, Cell biology, GAIT, gamma interferon-activated inhibition of translation, Bone Diseases, compound-heterozygous mutations, Research Article, SEC, size-exclusion chromatography, PRS, prolyl-tRNA synthetase, Mutation, Missense, tRNA charging, Amino Acyl-tRNA Synthetases, Editors' Pick Highlight, MSC, multisynthetase complex, Stress, Physiological, genetic disease, aaRSs, aminoacyl-tRNA synthetases, GST, glutathione-S-transferase, Diabetes Mellitus, medicine, Integrated stress response, Humans, EPRS, glutamyl-prolyl-tRNA synthetase, Molecular Biology, CHOP, C/EBP-homologous protein, ISR, integrated stress response, MALS, multiangle laser light scattering, GCN2, general control nonderepressible 2, Aminoacyl tRNA synthetase, Genetic Diseases, Inborn, Cell Biology, stress response, EPRS, TRNA binding, WT, wild-type, compound heterozygous mutations, Glutamate-tRNA Ligase, HEK293 Cells, Amino Acid Substitution, chemistry, DTT, dithiothreitol, Protein Biosynthesis, Aminoacyl-tRNA synthetase, endoplasmic reticulum stress (ER stress), ERS, glutamyl-tRNA synthetase

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ce97fb563092e3b298c457fe5bda992Test
http://europepmc.org/articles/PMC8511952Test

2

Intrinsically disordered substrates dictate SPOP subnuclear localization and ubiquitination activity

المؤلفون: Amie K. Boal, Scott A. Showalter, Nafiseh Sabri, Roman Rohac, Emery T. Usher, Tanja Mittag

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, endocrine system diseases, SBM1, SB motif 1, Amino Acid Motifs, SPOP, Biochemistry, IDRs, intrinsically disordered regions, PBST, Triton X-100 in PBS, Ubiquitin, Pdx1, biology, diabetes, FA, fluorescence anisotropy, Nuclear Proteins, Editors' Pick, multivalency, MATH, meprin and tumor necrosis factor receptor-associated factor homology, Ubiquitin ligase, Cell biology, LLPS, liquid–liquid phase separation, Protein Transport, Ni-NTA, nickel-nitrilotriacetic acid, PDX1, SBM2, SB motif 2, Protein Binding, Research Article, DAXX, death domain-associated protein 6, SPOP, speckle-type POZ protein, endocrine system, ubiquitination, digestive system, 03 medical and health sciences, Death-associated protein 6, Humans, structure, Molecular Biology, Transcription factor, Puc, puckered protein, Homeodomain Proteins, Nucleoplasm, 030102 biochemistry & molecular biology, Cell Biology, Repressor Proteins, 030104 developmental biology, SB, SPOP-binding, biology.protein, Trans-Activators, Homeobox, AR, androgen receptor, Pdx1, pancreatic and duodenal homeobox 1, DAPI, 4′,6-diamidino-2-phenylindole

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::865b2261c9773bb5532b2ebeb6469bacTest
https://pubmed.ncbi.nlm.nih.gov/33894201Test

3

Multisite NHERF1 phosphorylation controls GRK6A regulation of hormone-sensitive phosphate transport

المؤلفون: Peter A. Friedman, Kristian Strømgaard, Tatyana Mamonova, Sofie Bach, W. Bruce Sneddon, Maria Vistrup-Parry

المصدر: The Journal of Biological Chemistry
Vistrup-Parry, M, Sneddon, W B, Bach, S, Strømgaard, K, Friedman, P A & Mamonova, T 2021, ' Multisite NHERF1 phosphorylation controls GRK6A regulation of hormone-sensitive phosphate transport ', Journal of Biological Chemistry, vol. 296, 100473 . https://doi.org/10.1016/j.jbc.2021.100473Test

مصطلحات موضوعية: 0301 basic medicine, Protein Conformation, Parathyroid hormone, PDZ Domains, TBST, Tris-buffered saline plus Tween 20, GRK6A, G protein–coupled receptor kinase 6A, Biochemistry, GRK6Act-9, -568SEEELPTRL576, binding affinity, OKH, opossum kidney clone H, Phosphorylation, PTH, parathyroid hormone, Receptor, Alanine, GRK6Act-22, -553QRLFSRQDCCGNCSEEELPTRL576, Chemistry, Kinase, FA, fluorescence anisotropy, simulation, Cell biology, pSer162, phosphorylated Ser162, Parathyroid Hormone, CFTR, cystic fibrosis transmembrane conductance regulator, Protein Binding, Research Article, NPT2A, type II sodium-dependent phosphate cotransporter, Sodium-Hydrogen Exchangers, PDZ domain, Molecular Dynamics Simulation, Sodium-Phosphate Cotransporter Proteins, Type IIa, parathyroid hormone (PTH), Phosphates, 03 medical and health sciences, C-terminal, carboxy-terminal, Humans, phosphate transport, Molecular Biology, Ion Transport, 030102 biochemistry & molecular biology, Biological Transport, Cell Biology, NHERF1, Na+/H+-exchanger regulatory factor-1, G-Protein-Coupled Receptor Kinases, Phosphoproteins, Fibroblast Growth Factors, PDZ-ligand interaction, Fibroblast Growth Factor-23, 030104 developmental biology, G protein–coupled receptor kinase 6A (GRK6A), EBD, ezrin-binding domain, Phosphoprotein, OK cells, opossum kidney cells, Cotransporter