Zobrazeno 1 - 10
of 293
pro vyhledávání: '"B. Wiederanders"'
Autor:
U. Claussen, B. Wiederanders, R.-A. Venbrocks, C. Müller, R. Fuhrmann, Jürgen Mollenhauer, A. Rüttger
Publikováno v:
Zeitschrift für Orthopädie und Unfallchirurgie. 145:313-316
Aim and background Cysteine proteases as cathepsins K and L as well as matrix metalloproteases are considered to be basically involved in collagen turnover. Degenerative joint diseases such as gonarthrosis are characterised by massive cartilage degra
Autor:
Peter Hortschansky, Frank Layher, Jürgen Mollenhauer, W.-D. Wetzel, A. Sachse, Andreas Wagner, Jörg Bossert, R. Venbrocks, B. Wiederanders, M. Keller, J. Horn, K. Schmuck, O. Wagner, H.J. Hempel, M. Pietraszczyk
Publikováno v:
Bone. 37:699-710
Osteointegration of metal implants into aged organisms can be severely compromised due to reduced healing capacity of bone, lack of precursor cells for new bone formation, or osteoporosis. Here, we report on successful implant healing in a novel mode
Publikováno v:
bchm. 382:859-866
Folding of cathepsins L and S depend upon their proregion which extends the enzyme part by about 100 amino acids. Only a minority of the prosequence follows the structural template provided by the enzyme part; the majority forms an autonomous minidom
Autor:
Klaus Schilling, Ying Lan Guo, Joachim E. Schultz, B Wiederanders, Ursula Kurz, Chin Chia Lim
Publikováno v:
FEBS Letters. 469:203-207
Proregions of papain-like cysteine proteases are potent and often highly selective inhibitors of their parental enzymes. The molecular basis of their selectivity is poorly understood. For two closely related members of the cathepsin L-like subfamily
Publikováno v:
Journal of Biological Chemistry. 268:19690-19696
Chinese hamster ovary cells transfected with human lysozyme cDNA encoding Asn instead of Gly22 synthesize a mutant lysozyme, [Asn22]lysozyme, with about 60% of the molecules bearing carbohydrate. This carbohydrate is predominantly of the complex type
Autor:
B. Wiederanders, Dieter Brömme, David Y. Thomas, Andrew C. Storer, H. Kirschke, P.R. Bonneau, Thierry Vernet, Christoph Peters, Paule Lachance
Publikováno v:
Scopus-Elsevier
A cDNA encoding the human lysosomal cysteine proteinase cathepsin S precursor has been expressed in yeast using the pVT100-U expression vector containing the alpha-factor promoter. The procathepsin S gene was expressed either as a fusion protein with
Publikováno v:
Infection and Immunity. 58:1730-1737
In mammalian hosts, Leishmania amastigotes are obligatory intracellular parasites of macrophages and multiply within parasitophorous vacuoles of phagolysosomal origin. To understand how they escape the harmful strategies developed by macrophages to k
Publikováno v:
Brain Research Bulletin. 24:543-549
The lysosomal thiol proteinase, cathepsin B, has been localized in different regions of aged human brain by use of the peroxidase-antiperoxidase technique. Cathepsin B-immunoreactive material was detected in multiple neurons of human hippocampus, neo
Autor:
C, Müller, B, Wiederanders, R, Fuhrmann, R-A, Venbrocks, J, Mollenhauer, U, Claussen, A, Rüttger
Publikováno v:
Zeitschrift fur Orthopadie und Unfallchirurgie. 145(3)
Cysteine proteases as cathepsins K and L as well as matrix metalloproteases are considered to be basically involved in collagen turnover. Degenerative joint diseases such as gonarthrosis are characterised by massive cartilage degradation mediated by