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R Glockshuber

Explore the profile of R Glockshuber including associated specialties, affiliations and a list of published articles. Areas
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Articles 73
Citations 2507
Followers 0
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Recent Articles
1.
Mireku S, Sauer M, Glockshuber R, Locher K
Sci Rep . 2017 Nov; 7(1):14296. PMID: 29084999
Bacterial ABC importers catalyze the uptake of essential nutrients including transition metals and metal-containing co-factors. Recently, an IgG antibody targeting the external binding protein of the Staphylococcus aureus Mn(II) ABC...
2.
Stirnimann C, Grutter M, Glockshuber R, Capitani G
Cell Mol Life Sci . 2006 Jun; 63(14):1642-8. PMID: 16786221
DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain. nDsbD interacts with four different redox proteins involved in...
3.
Heuberger M, Widmer M, Zobeley E, Glockshuber R, Spencer N
Biomaterials . 2004 Sep; 26(10):1165-73. PMID: 15451636
Wear of articulated surfaces can be a major lifetime-limiting factor in arthroplasty. In the natural joint, lubrication is effected by the body's natural synovial fluid. Following arthroplasty, and the subsequent...
4.
Zhou G, Mo W, Sebbel P, Min G, Neubert T, Glockshuber R, et al.
J Cell Sci . 2001 Dec; 114(Pt 22):4095-103. PMID: 11739641
The binding of uropathogenic Escherichia coli to the urothelial surface is a crucial initial event for establishing urinary tract infection because it allows the bacteria to gain a foothold on...
5.
Glockshuber R
Adv Protein Chem . 2001 Jul; 57:83-105. PMID: 11447698
No abstract available.
6.
Cereghetti G, Schweiger A, Glockshuber R, Van Doorslaer S
Biophys J . 2001 Jun; 81(1):516-25. PMID: 11423433
Transmissible spongiform encephalopathies in mammals are believed to be caused by scrapie form of prion protein (PrP(Sc)), an abnormal, oligomeric isoform of the monomeric cellular prion protein (PrP(C)). One of...
7.
Winter J, Neubauer P, Glockshuber R, Rudolph R
J Biotechnol . 2000 Nov; 84(2):175-85. PMID: 11090689
The production of human proinsulin in its disulfide-intact, native form in Escherichia coli requires disulfide bond formation and the periplasmic space is the favourable compartment for oxidative folding. However, the...
8.
Hermanns U, Sebbel P, Eggli V, Glockshuber R
Biochemistry . 2000 Sep; 39(38):11564-70. PMID: 10995223
Assembly of type 1 pili from Escherichia coli is mediated by FimC, a periplasmic chaperone (assembly factor) consisting of two immunoglobulin-like domains. FimC is assumed to recognize the individual pilus...
9.
Mossner E, Iwai H, Glockshuber R
FEBS Lett . 2000 Jul; 477(1-2):21-6. PMID: 10899304
Thioredoxin constitutes the prototype of the thiol-disulfide oxidoreductase family. These enzymes contain an active-site disulfide bridge with the consensus sequence Cys-Xaa-Xaa-Cys. The more N-terminal active-site cysteine is generally a strong...
10.
Sillen A, Hennecke J, Roethlisberger D, Glockshuber R, Engelborghs Y
Proteins . 1999 Dec; 37(2):253-63. PMID: 10584070
The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and is required for efficient disulfide bond formation in the bacterial periplasm. DsbA contains two tryptophans: W76 and W126....