scholarly journals Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis

1999 ◽  
Vol 103 (5) ◽  
pp. 731-738 ◽  
Author(s):  
Wu-Shiun Hou ◽  
Dieter Brömme ◽  
Yingming Zhao ◽  
Ernest Mehler ◽  
Craig Dushey ◽  
...  
Keyword(s):  
Cathepsin K ◽  
Mature Polypeptide

scholarly journals Characterization of lysosomal acid lipase mutations in the signal peptide and mature polypeptide region causing Wolman disease

2001 ◽  
Vol 42 (7) ◽  
pp. 1033-1040 ◽  
Author(s):  
Oliver Zschenker ◽  
Nikola Jung ◽  
Julia Rethmeier ◽  
Sabine Trautwein ◽  
Stefanie Hertel ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Acid Lipase ◽  
Wolman Disease ◽  
Lysosomal Acid ◽  
Lysosomal Acid Lipase ◽  
Mature Polypeptide

The development and characterization of an ELISA specifically detecting the active form of cathepsin K

2013 ◽  
Vol 46 (15) ◽  
pp. 1601-1606 ◽  
Author(s):  
S. Sun ◽  
M.A. Karsdal ◽  
A.C. Bay-Jensen ◽  
M.G. Sørensen ◽  
Q. Zheng ◽  
...  
Keyword(s):  
Active Form ◽  
Cathepsin K

scholarly journals A composite docking approach for the identification and characterization of ectosteric inhibitors of cathepsin K

PLoS ONE ◽  
2017 ◽  
Vol 12 (10) ◽  
pp. e0186869 ◽  
Author(s):  
Simon Law ◽  
Preety Panwar ◽  
Jody Li ◽  
Adeleke H. Aguda ◽  
Andrew Jamroz ◽  
...  
Keyword(s):  
Cathepsin K ◽  
Docking Approach ◽  
Identification And Characterization

scholarly journals Nonclinical and clinical pharmacological characterization of the potent and selective cathepsin K inhibitor MIV-711

2018 ◽  
Vol 16 (1) ◽  
Author(s):  
Erik Lindström ◽  
Biljana Rizoska ◽  
Ian Henderson ◽  
Ylva Terelius ◽  
Markus Jerling ◽  
...  
Keyword(s):  
Cathepsin K ◽  
Pharmacological Characterization ◽  
Cathepsin K Inhibitor

Pharmacological characterization of the potent, selective and orally active cathepsin K inhibitor MIV-711

Bone ◽  
2012 ◽  
Vol 50 ◽  
pp. S164-S165 ◽  
Author(s):  
U. Grabowska⁎ ◽  
I. Henderson ◽  
M. Edlund ◽  
L. Vrang ◽  
S. Sedig ◽  
...  
Keyword(s):  
Cathepsin K ◽  
Pharmacological Characterization ◽  
Cathepsin K Inhibitor ◽  
Orally Active

Cathepsin K: Isolation and Characterization of the Murine cDNA and Genomic Sequence, the Homologue of the Human Pycnodysostosis Gene

1996 ◽  
Vol 59 (2) ◽  
pp. 200-206 ◽  
Author(s):  
Bruce D. Gelb ◽  
Konstadinos Moissoglu ◽  
Jian Zhang ◽  
John A. Martignetti ◽  
Dieter Brömme ◽  
...  
Keyword(s):  
Genomic Sequence ◽  
Cathepsin K ◽  
Isolation And Characterization

scholarly journals Molecular and Biochemical Characterization of a β-Fructofuranosidase from Xanthophyllomyces dendrorhous

2008 ◽  
Vol 75 (4) ◽  
pp. 1065-1073 ◽  
Author(s):  
Dolores Linde ◽  
Isabel Macias ◽  
Luc�a Fern�ndez-Arrojo ◽  
Francisco J. Plou ◽  
Antonio Jim�nez ◽  
...  
Keyword(s):  
Total Mass ◽  
Structural Model ◽  
Biochemical Characterization ◽  
Sucrose Solution ◽  
Catalytic Efficiency ◽  
Maximum Activity ◽  
Xanthophyllomyces Dendrorhous ◽  
Glycosyl Hydrolases ◽  
Mature Polypeptide

ABSTRACT An extracellular β-fructofuranosidase from the yeast Xanthophyllomyces dendrorhous was characterized biochemically, molecularly, and phylogenetically. This enzyme is a glycoprotein with an estimated molecular mass of 160 kDa, of which the N-linked carbohydrate accounts for 60% of the total mass. It displays optimum activity at pH 5.0 to 6.5, and its thermophilicity (with maximum activity at 65 to 70�C) and thermostability (with a T 50 in the range 66 to 71�C) is higher than that exhibited by most yeast invertases. The enzyme was able to hydrolyze fructosyl-β-(2→1)-linked carbohydrates such as sucrose, 1-kestose, or nystose, although its catalytic efficiency, defined by the k cat/Km ratio, indicates that it hydrolyzes sucrose approximately 4.2 times more efficiently than 1-kestose. Unlike other microbial β-fructofuranosidases, the enzyme from X. dendrorhous produces neokestose as the main transglycosylation product, a potentially novel bifidogenic trisaccharide. Using a 41% (wt/vol) sucrose solution, the maximum fructooligosaccharide concentration reached was 65.9 g liter−1. In addition, we isolated and sequenced the X. dendrorhous β-fructofuranosidase gene (Xd-INV), showing that it encodes a putative mature polypeptide of 595 amino acids and that it shares significant identity with other fungal, yeast, and plant β-fructofuranosidases, all members of family 32 of the glycosyl-hydrolases. We demonstrate that the Xd-INV could functionally complement the suc2 mutation of Saccharomyces cerevisiae and, finally, a structural model of the new enzyme based on the homologous invertase from Arabidopsis thaliana has also been obtained.

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