Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Hasilik, A"'
Autor:
Eva Smolenova, Norbert Werth, Konrad Sandhoff, Andrej Hasilik, Hans-Wilhelm Grosch, Madanan Madathiparambil Gopalakrishnan, Silvia Locatelli-Hoops, Michael Nettersheim
Publikováno v:
Biochemical Journal. 383:507-515
Before delivery to endosomes, portions of proCD (procathepsin D) and proSAP (prosaposin) are assembled into complexes. We demonstrate that such complexes are also present in secretions of cultured cells. To study the formation and properties of the c
Autor:
Markus Schwarz, Kurt von Figura, Ulrike Grieben, Martin Hasilik, Christian Körner, Christian Thiel, Folker Hanefeld, Ludwig Lehle
Publikováno v:
Biochemical Journal. 367:195-201
Deficiency of the endoplasmic reticulum enzyme dolichyl-phosphate mannose (Dol-P-Man):Man(7)GlcNAc(2)-PP-dolichyl mannosyltransferase leads to a new type of congenital disorder of glycosylation, designated type Ig. The patient 1 presented with a mult
Publikováno v:
Biochemical Journal. 348:507-515
We have studied the elongation of oligosaccharides containing N-acetyl-lactosamine repeats using glycosylated human lysozyme mutants as a model. We reported previously that a combination of glycosylation sites at the 49th (site IV) and 68th (site II)
Publikováno v:
Scopus-Elsevier
The segregation of human cathepsin D, studied in baby-hamster kidney cells (BHK) transfected with human cathepsin D cDNA and compared with that of hamster cathepsin D in the same cells, showed that, in cells that expressed human cathepsin D at a low
Autor:
Andrej Hasilik, M Horst
Publikováno v:
Biochemical Journal. 273:355-361
In medium and in homogenates from baby-hamster kidney cells (BHK) transfected with human cathepsin D cDNA, an elevated activity of cathepsin D was found as compared to non-transfected cells. The elevated activity was removed by titrating the homogena
Autor:
Stephan Storch, Thomas Braulke, Andrej Hasilik, Hans-Gerhard Löffler, Sanna Partanen, Jaana Tyynelä
The substitution of an active-site aspartic acid residue by asparagine in the lysosomal protease cathepsin D (CTSD) results in a loss of enzyme activity and severe cerebrocortical atrophy in a novel form of neuronal ceroid lipofuscinosis in sheep [Ty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f26e85f8cf593645e65b5fb484aa6b00
https://europepmc.org/articles/PMC1223066/
https://europepmc.org/articles/PMC1223066/
Autor:
Gordon Alton, H. K. Harms, K. Reiter, Klaus-Peter Zimmer, Martin Hasilik, Hans Georg Koch, Rongrong Wu, Erik Harms, Hudson H. Freeze, Christian Körner, M. Schiebe-Sukumar, Thorsten Marquardt, R. Niehues, K von Figura
Phosphomannose isomerase (PMI) deficiency is the cause of a new type of carbohydrate-deficient glycoprotein syndrome (CDGS). The disorder is caused by mutations in the PMI1 gene. The clinical phenotype is characterized by protein-losing enteropathy,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cde2874d94fa8306d86e739d27978cc
https://europepmc.org/articles/PMC508719/
https://europepmc.org/articles/PMC508719/
Morphological and biochemical evidence indicates that in several cell types, lysozyme is found in both lysosomes and the medium. Here we report that in calcitriol-treated human promonocytes U937, in which approx. two-thirds of the synthesized lysozym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae8cbadd0de5257836feeec267b11fdd
https://europepmc.org/articles/PMC1137267/
https://europepmc.org/articles/PMC1137267/
Autor:
Ake Engstrom, Evelyn Plümper, Frank Meyer, Klaus Heckmann, Andrej Hasilik, Helmut J. Schmidt, Helmut E. Meyer, Günther Mersmann
Pheromone 3 mRNA of the ciliate Euplotes octocarinatus contains three in-frame UGA codons that are translated as cysteines. This was revealed from cDNA sequencing and from plasma desorption mass spectrometry of cleaved pheromone 3 in connection with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e45a75a583d3f4400ca3feb9466ed7b
https://europepmc.org/articles/PMC51532/
https://europepmc.org/articles/PMC51532/
Publikováno v:
Proceedings of the National Academy of Sciences. 77:7074-7078
In human fibroblasts, the recognition of lysosomal enzymes by cell surface receptors is mediated by mannose 6-phosphate residues located on oligosaccharides that can be cleaved by endo-beta-N-acetylglucosaminidase H. About half of these oligosacchari