Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Salit Tzaban"'
Autor:
Nadia Fiks, Yoseph Shaaltiel, Yoram Tekoah, Salit Tzaban, Svetlana Gingis-Velitski, David Aviezer
Publikováno v:
Plant Biotechnology Journal. 13:1033-1040
Summary Gaucher's disease (GD), a lysosomal storage disorder caused by mutations in the gene encoding glucocerebrosidase (GCD), is currently treated by enzyme replacement therapy (ERT) using recombinant GCD that is administered intravenously every 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00ea353b8406e8e9de28ae5b3a573c2f
https://doi.org/10.1111/pbi.12366
https://doi.org/10.1111/pbi.12366
Autor:
Steen H. Hansen, Salit Tzaban, Wendy Hamman, Richard S. Blumberg, Scott R. Frank, Lynne A. Lapierre, Ramiro Massol, James R. Goldenring, Wayne I. Lencer, Elizabeth H. Yen
Publikováno v:
The Journal of Cell Biology
The Fc receptor FcRn traffics immunoglobulin G (IgG) in both directions across polarized epithelial cells that line mucosal surfaces, contributing to host defense. We show that FcRn traffics IgG from either apical or basolateral membranes into the re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b7a0820c0c17097abf964ea3d913651
http://europepmc.org/articles/PMC2711563
http://europepmc.org/articles/PMC2711563
Autor:
Olga Ben-Zaken, Salit Tzaban, Yuval Tal, Israel Vlodavsky, Lior Horonchik, Jeffrey D. Esko, Albert Taraboulos
Publikováno v:
Journal of Biological Chemistry. 278:40041-40049
During prion diseases, the host protein PrPC is refolded into an abnormal conformer "prion" PrPSc. Histological and pharmacological data have suggested that glycosaminoglycans may be involved in the development of prion diseases. Here we present the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e1dc8bd06125342d242ee5d5a078117
https://doi.org/10.1074/jbc.m301152200
https://doi.org/10.1074/jbc.m301152200
Publikováno v:
The EMBO Journal. 20:5383-5391
Prion diseases propagate by converting a normal glycoprotein of the host, PrP(C), into a pathogenic "prion" conformation. Several misfolding mutants of PrP(C) are degraded through the ER-associated degradation (ERAD)-proteasome pathway. In their infe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed3be94ed8ed220b86da15743f30e5a8
https://doi.org/10.1093/emboj/20.19.5383
https://doi.org/10.1093/emboj/20.19.5383
Publikováno v:
Phytochemistry. 45:1115-1121
The presence of at least three distinct polygalacturonases (PGase) in callus of Orobanche was demonstrated. The PGase activity is labile and at pH 4.5 does not require activation by cations. It can be partially purified on Biogel P 100 columns and ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bba4433fdbd4c8826d12ce39d512b01
https://doi.org/10.1016/s0031-9422(97)00134-9
https://doi.org/10.1016/s0031-9422(97)00134-9
Autor:
Tali Kizhner, Myriam Golembo, David Aviezer, Anna Gantman, Mariana Hainrichson, Salit Tzaban, Yoseph Shaaltiel, Yoram Tekoah
Publikováno v:
Bioscience Reports
The glycosylation of recombinant β-glucocerebrosidase, and in particular the exposure of mannose residues, has been shown to be a key factor in the success of ERT (enzyme replacement therapy) for the treatment of GD (Gaucher disease). Macrophages, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::527bd80496225889294d6a891656a3bb
https://doi.org/10.1042/bsr20130081
https://doi.org/10.1042/bsr20130081
Autor:
Myriam Golembo, Yoseph Shaaltiel, David Aviezer, Anna Gantman, Mariana Hainrichson, Tali Kizhner, Yoram Tekoah, Salit Tzaban
Publikováno v:
Bioscience Reports, Vol 33, Iss 5, p e00071 (2013)
The glycosylation of recombinant β-glucocerebrosidase, and in particular the exposure of mannose residues, has been shown to be a key factor in the success of ERT (enzyme replacement therapy) for the treatment of GD (Gaucher disease). Macrophages, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doajarticles::658de7738d8d0000ecd474f99d915328
http://www.bioscirep.org/bsr/033/e071/bsr033e071.htm
http://www.bioscirep.org/bsr/033/e071/bsr033e071.htm
Autor:
Olga Ben-Zaken, Lior Horonchik, Salit Tzaban, Yifat Yedidia, Alexander Rouvinski, Dulce Papy-Garcia, Denis Barritault, Albert Taraboulos, Israel Vlodavsky
Publikováno v:
The Journal of biological chemistry. 280(17)
Prions replicate in the host cell by the self-propagating refolding of the normal cell surface protein, PrP(C), into a beta-sheet-rich conformer, PrP(Sc). Exposure of cells to prion-infected material and subsequent endocytosis can sometimes result in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffab7256defff569dde8f3345c7258f1
https://pubmed.ncbi.nlm.nih.gov/15668247
https://pubmed.ncbi.nlm.nih.gov/15668247
Autor:
Gilgi Friedlander, Albert Taraboulos, Salit Tzaban, Gideon M. Shaked, Oshrat Schonberger, Ruth Gabizon, Lior Horonchik, Yifat Yedidia
Publikováno v:
Biochemistry. 41(42)
The pathological prion protein PrP(Sc) is the only known component of the infectious prion. In cells infected with prions, PrP(Sc) is formed posttranslationally by the refolding of the benign cell surface glycoprotein PrP(C) into an aberrant conforma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::846e2f40c2218054eacb3b8622464bea
https://pubmed.ncbi.nlm.nih.gov/12379130
https://pubmed.ncbi.nlm.nih.gov/12379130
Autor:
David Aviezer, Mariana Hainrichson, Anna Gantman, Yoseph Shaaltiel, Salit Tzaban, Yoram Tekoa
Publikováno v:
Molecular Genetics and Metabolism. 111:S95
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::977bc34ef97fe6dfa898a209dad125e1
https://doi.org/10.1016/j.ymgme.2013.12.233
https://doi.org/10.1016/j.ymgme.2013.12.233