about
BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complexAn interaction map of endoplasmic reticulum chaperones and foldasesEffects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transportRefining protein subcellular localizationSolution structure of the bb' domains of human protein disulfide isomeraseStructure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72Structural Basis of Cyclophilin B Binding by the Calnexin/Calreticulin P-domainCrystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae,Cold adaptation in budding yeastInteraction of a G-protein beta-subunit with a conserved sequence in Ste20/PAK family protein kinases.Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae.Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association.Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae.Localization of endogenous Grb10 to the mitochondria and its interaction with the mitochondrial-associated Raf-1 poolProteomics characterization of abundant Golgi membrane proteinsCrystal structure of the bb' domains of the protein disulfide isomerase ERp57Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinasesA biochemical genomics screen for substrates of Ste20p kinase enables the in silico prediction of novel substratesReverse genetics in Candida albicans predicts ARF cycling is essential for drug resistance and virulenceERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ERPhosphorylation by CK2 and MAPK enhances calnexin association with ribosomes.gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomerFunctional characterization of myosin I tail regions in Candida albicansPCR-based unidirectional deletion method for creation of comprehensive cDNA libraries.Correctors of protein trafficking defects identified by a novel high-throughput screening assay.Chemogenomic profiling predicts antifungal synergies.CDC42 is required for polarized growth in human pathogen Candida albicans.Repression of hyphal proteinase expression by the mitogen-activated protein (MAP) kinase phosphatase Cpp1p of Candida albicans is independent of the MAP kinase Cek1p.Population genomics of drug resistance in Candida albicans.Organization of the Sec61 translocon, studied by high resolution native electrophoresis.Experimental design and statistical methods for improved hit detection in high-throughput screening.The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation.Transcription profiling of Candida albicans cells undergoing the yeast-to-hyphal transition.Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing.Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase.The dual phosphodiesterase 3 and 4 inhibitor RPL554 stimulates CFTR and ciliary beating in primary cultures of bronchial epithelia.Enhanced Ca2+ entry due to Orai1 plasma membrane insertion increases IL-8 secretion by cystic fibrosis airwaysSaccharomyces cerevisiae plasmid, Scp or 2 mum: intracellular distribution, stability and nucleosomal-like packaging
P50
Q24321768-4319C115-88DF-48A1-9D9A-6C03BDBA7097Q24337336-88B1E26F-B07B-4C10-8C04-0783D96CDEFFQ24633832-BDF0F001-B127-47A9-85E3-4D330813FC35Q24811585-6BCCBAE3-0A12-44BE-B59B-C488AE0D34CEQ27653624-26DC78C2-E622-4A76-B17A-361799F52D3DQ27655486-210AADC5-2323-4E65-A1F0-6477F98747DEQ27663027-536EB858-BAC1-465B-900D-623A2AD28BD2Q27664213-14B9775B-A7F3-4FD9-9024-120A3E17D498Q27740489-FAC63526-936F-49B6-ACF0-3408F93D0627Q27930221-989BAC6C-EAA1-4942-971C-C8000998F986Q27934420-7532CC8B-B7B8-400A-A6D8-81D7AFE963CFQ27936500-9A30CDBF-D18D-4BDA-9579-9BB47DA69F17Q27938632-395B65AC-AF75-4DC5-90D2-21C4F8961BE1Q27939643-21ABF737-7BBA-411E-865B-C89B62DD51CAQ27940026-923808C5-287D-4C54-9C8D-64D2C9643D8EQ28139493-CEC1625D-5FDC-4962-8D27-F425BE68B7D9Q28141807-065168F4-198C-4FBC-96FA-C160F8B7861FQ28257377-857131EC-6E69-4EEA-9B45-BD0CBA13EF37Q28268392-2B5E7C1A-4283-48A5-91B5-23BC65D1CB54Q28472248-4E538FAF-1A3C-49AB-B190-D68E3E99D3BFQ28472787-2E61242C-E11C-415C-93BD-921AB0DEC3F8Q28512215-6C9358ED-C549-45A4-A62C-D14FE6B10423Q28575744-027503D3-7807-453C-AB89-01776CC558F7Q28631479-D6D89516-7558-4F46-94DF-F8D1BA6F1769Q30163789-00481FF9-3825-41D4-9947-1C6D063CA8C9Q33213076-DB80916E-F190-4391-9AE7-538949E4E9EAQ33284421-A8C2FDF8-8BF4-46DA-A11E-82812DA5D444Q33668319-FB75CD2E-19C9-448C-8731-FB37D106EBB9Q33905537-3DC803DB-9FCF-4AEB-81EF-56878319C666Q34005397-B7268447-9160-4C51-9AF5-F3A076AA4CFAQ34034817-AD853509-13EF-4B8A-8F85-01A0D50BDE01Q34095637-CB855DF0-9E33-4919-A294-F1278E1E644EQ34136164-73612ED8-4A5F-443B-91D0-93628032EE59Q34141552-AC261E98-C770-420B-BC88-FAAE0E0906F7Q34167828-53A71AF3-F0E7-4C2B-B235-D1F4D711426BQ34173174-4DF74BA9-F311-48FE-A549-53850CDE1BB9Q34236548-830A2F3E-B2F0-4D4D-AB2C-C6ED5C0CD0C2Q34500909-4D4FD750-67A8-45BB-80EB-7D1781D7010DQ35609604-C12F7B15-7D7F-4091-9188-B1B0565744ADQ35620725-0F40406D-1C91-487C-B038-56670E565D35
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
David Y. Thomas
@ast
David Y. Thomas
@en
David Y. Thomas
@es
David Y. Thomas
@sl
type
label
David Y. Thomas
@ast
David Y. Thomas
@en
David Y. Thomas
@es
David Y. Thomas
@sl
prefLabel
David Y. Thomas
@ast
David Y. Thomas
@en
David Y. Thomas
@es
David Y. Thomas
@sl
P1053
M-7661-2017
P106
P1153
7601532483
P21
P31
P3829
P496
0000-0002-8854-762X