Zobrazeno 1 - 10
of 196
pro vyhledávání: '"L. Lehle"'
Autor:
Gudrun Nürnberg, Thorsten Marquardt, Janine Reunert, C. Hertzberg, A.E. Würde, L. Lehle, Stephan Rust, S. Haverkämper, R. Rossi, Peter Nürnberg
Publikováno v:
Molecular Genetics and Metabolism. 105:634-641
Congenital disorders of glycosylation (CDG) are caused by enzymatic defects of the formation or processing of lipid-linked oligosaccharides and glycoproteins. Since the majority of proteins is glycosylated, a defect in a singular CDG enzyme leads to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25fec88d63fe7e5afe0c7f2d20c693a1
https://doi.org/10.1016/j.ymgme.2012.01.001
https://doi.org/10.1016/j.ymgme.2012.01.001
Publikováno v:
The EMBO Journal. 11:2071-2075
Asparagine-linked N-glycosylation is a highly conserved and functionally important modification of proteins in eukaryotic cells. The central step in this process is a cotranslational transfer of lipid-linked core oligosaccharides to selected Asn-X-Se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e923aa9f8be39a1ced5ed45adb8c8f9
https://doi.org/10.1002/j.1460-2075.1992.tb05265.x
https://doi.org/10.1002/j.1460-2075.1992.tb05265.x
Publikováno v:
The Journal of biological chemistry. 276(31)
The Golgi plays a fundamental role in posttranslational glycosylation, transport, and sorting of proteins. The mechanism of protein transport through the Golgi has been seen as controversial in recent years. During the characterization of N-glycosyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb7356900ec3ec4630542a37d5fa8c28
https://pubmed.ncbi.nlm.nih.gov/11477110
https://pubmed.ncbi.nlm.nih.gov/11477110
Publikováno v:
The Journal of biological chemistry. 274(24)
The key step of N-glycosylation of proteins, an essential and highly conserved protein modification, is catalyzed by the hetero-oligomeric protein complex oligosaccharyltransferase (OST). So far, eight genes have been identified in Saccharomyces cere
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2d95feb59b7c417bdfc5087b808694bc
https://pubmed.ncbi.nlm.nih.gov/10358084
https://pubmed.ncbi.nlm.nih.gov/10358084
Publikováno v:
Glycoconjugate journal. 15(5)
In the carbohydrate deficient glycoprotein syndrome (CDGS) type 1 glycoproteins with less and shorter N-linked oligosaccharides are synthesized due to a deficiency of phosphomannomutase. Glucose deprivation or mannose addition are shown to partially
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9ea955d9c7df0bb5491b545b705eada4
https://pubmed.ncbi.nlm.nih.gov/9881752
https://pubmed.ncbi.nlm.nih.gov/9881752
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 95(22)
Deficiency of dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase is the cause of an additional type of carbohydrate-deficient glycoprotein syndrome (CDGS type V). Clinically this type resembles the classical type Ia of CDGS caused by the defi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::499c73a4faa1d1306e649a0485f227f5
https://pubmed.ncbi.nlm.nih.gov/9789065
https://pubmed.ncbi.nlm.nih.gov/9789065
Publisher Summary This chapter discusses the protein glycosylation in yeast. Glycosylated proteins are found in all eukaryotes, in many archaebacteria, and exceptionally in eubacteria. The glycosylation of proteins is the most complex type of protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb9e33cb1eb744a73a8f64143d4fbbc6
https://doi.org/10.1016/s0167-7306(08)60601-8
https://doi.org/10.1016/s0167-7306(08)60601-8
Autor:
B Janetzky, L Lehle
Publikováno v:
Scopus-Elsevier
We have isolated and sequenced a genomic clone from Saccharomyces cerevisiae that shows structural features of a novel retrotransposon, designated Ty4. The element is 6.2 kilobases in length, and its genetic organization of the deduced functional dom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::214cceb32c364c582aa557d25b65ad27
https://pubmed.ncbi.nlm.nih.gov/1328182
https://pubmed.ncbi.nlm.nih.gov/1328182
Publikováno v:
The Journal of biological chemistry. 266(36)
We have isolated and mapped to the left end of chromosome III a single-copy gene (TRG1) encoding a 72-kDa glycoprotein, by screening a yeast genomic library with a DNA probe specifying the catalytic center (APWCGHCK) of thioredoxin-related proteins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::28555f48b41062178942abd56f67a749
https://pubmed.ncbi.nlm.nih.gov/1761554
https://pubmed.ncbi.nlm.nih.gov/1761554
Publikováno v:
Journal of Biological Chemistry. 254:12209-12218
Invertase, extracted from broken cells of Saccharomyces cerevisiae X-2180 mm2 mannan mutant, was separated into a fraction insoluble in 75% ammonium sulfate (P75 invertase, 36% carbohydrate) and a soluble fraction (S75 invertase, 53% carbohydrate). T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ed5c37805fbb8bb4a8774cb98eb4560
https://doi.org/10.1016/s0021-9258(19)86451-7
https://doi.org/10.1016/s0021-9258(19)86451-7