E
Ervin Welker
Researcher at Hungarian Academy of Sciences
Publications - 67
Citations - 3728
Ervin Welker is an academic researcher from Hungarian Academy of Sciences. The author has contributed to research in topics: Oxidative folding & Bovine pancreatic ribonuclease. The author has an hindex of 25, co-authored 63 publications receiving 3402 citations. Previous affiliations of Ervin Welker include Cornell University & MTA Biological Research Centre.
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Journal ArticleDOI
Disulfide Bonds and Protein Folding
TL;DR: The mechanism of regenerating the native disulfide bonds suggests an analogous scenario for conformational folding, and engineered covalent cross-links may be used to assay for the association of protein segments in the folding transition state, as illustrated with RNase A.
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Proline Cis-Trans Isomerization and Protein Folding †
TL;DR: The folding and unfolding of disulfide-intact bovine pancreatic ribonuclease A is used as an example to illustrate the kinetics and structural features of conformational changes from the heterogeneous unfolded state to the native structure in which only one set of proline isomers is present.
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Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain.
Éva Bakos,Raymond Evers,Gergely Szakács,Gábor E. Tusnády,Ervin Welker,Katalin Szabó,Marcel de Haas,Liesbeth van Deemter,Piet Borst,András Váradi,Balázs Sarkadi +10 more
TL;DR: Taken together, these experiments strongly suggest that the TMD0 region is neither required for the transport function of MRP1 nor for its proper routing to the plasma membrane.
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MDR3 P-glycoprotein, a Phosphatidylcholine Translocase, Transports Several Cytotoxic Drugs and Directly Interacts with Drugs as Judged by Interference with Nucleotide Trapping
Alexander J. Smith,Ardy van Helvoort,Ardy van Helvoort,Gerrit van Meer,Katalin Szabó,Ervin Welker,Gergely Szakács,András Váradi,Balázs Sarkadi,Piet Borst +9 more
TL;DR: In this article, an increased directional transport of several MDR1 P-glycoprotein substrates, such as digoxin, paclitaxel, and vinblastine, through polarized monolayers of MDR3-transfected cells was reported.
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Membrane topology and glycosylation of the human multidrug resistance-associated protein.
Éva Bakos,Tamás Hegedus,Zsolt Holló,Ervin Welker,Gábor E. Tusnády,Guido J.R. Zaman,Marcel J. Flens,András Váradi,Balázs Sarkadi +8 more
TL;DR: The membrane topology of the human multidrug resistance-associated protein (MRP) was examined by flow cytometry phenotyping, immunoblotting, and limited proteolysis in drug-resistant human and baculovirus-infected insect cells, expressing either the glycosylated or the underglycosylation forms of this protein.