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Proteinase K

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J Bajorath et al.
Biochimica et biophysica acta, 954(2), 176-182 (1988-05-18)
The activity of proteinase K (EC 3.4.21.14), a subtilisin-related serine proteinase, was assayed with azoalbumin that showed non-expected behavior in substrate saturation curve because of interaction between albumin molecules. Succinyl-(Ala)n-p-nitroanilide with n = 2 and 3, yielded specific activities of...
Dieter Brömme et al.
Expert opinion on investigational drugs, 18(5), 585-600 (2009-04-25)
Cathepsin K is a highly potent collagenase and the predominant papain-like cysteine protease expressed in osteoclasts. Cathepsin K deficiencies in humans and mice have underlined the central role of this protease in bone resorption and, thus, have rendered the enzyme...
Fabien Lecaille et al.
Biochimie, 90(2), 208-226 (2007-10-16)
Cysteine cathepsins (11 in humans) are mostly located in the acidic compartments of cells. They have been known for decades to be involved in intracellular protein degradation as housekeeping proteases. However, the discovery of new cathepsins, including cathepsins K, V...
Atefeh Jafari et al.
International journal of biological macromolecules, 151, 1250-1258 (2019-11-26)
Osmolytes such as sucrose can interact with the proteins. The aim of the present investigation was to characterize how sucrose could affect the structure, thermal stability and the kinetic of proteinase K. UV-vis spectroscopy, fluorescence spectroscopy, circular dichroism, molecular docking...
Mansoore Hosseini-Koupaei et al.
International journal of biological macromolecules, 122, 732-744 (2018-11-09)
Here, CuO nanoparticles were synthesized using Sambucus nigra (elderberry) fruit extract. Further, the binding of proteinase K, as a model enzyme with green synthesized nanoparticles was investigated. The results demonstrated that the structural changes in enzyme were induced by the...
Tiina Laitala-Leinonen et al.
Matrix biology : journal of the International Society for Matrix Biology, 25(3), 149-157 (2005-12-03)
Degradation of organic bone matrix requires proteinase activity. Cathepsin K is a major osteoclast proteinase needed for bone resorption, although osteoclasts also express a variety of other cysteine- and matrix metalloproteinases that are involved in bone remodellation. Cystatin B, an...
Crystal structure of human cathepsin K complexed with a potent inhibitor.
M E McGrath et al.
Nature structural biology, 4(2), 105-109 (1997-02-01)
Arumugam Jayakumar et al.
Archives of biochemistry and biophysics, 409(2), 367-374 (2002-12-31)
Headpin (SERPINB13) is a novel member of the serine proteinase inhibitor (Serpin) gene family that was originally cloned from a keratinocyte cDNA library. Western blot analysis using a headpin-specific antiserum recognized a protein with the predicted M(r) of 44kDa in...
C E Tye et al.
Journal of dental research, 90(4), 489-494 (2010-12-02)
Fluorosed enamel can be porous, mottled, discolored, hypomineralized, and protein-rich if the enamel matrix is not completely removed. Proteolytic processing by matrix metalloproteinase-20 (MMP20) and kallikrein-4 (KLK4) is critical for enamel formation, and homozygous mutation of either protease results in...
Jingjing Cai et al.
Investigative ophthalmology & visual science, 53(9), 5967-5974 (2012-08-11)
Oxidative processes may play important roles in age-related macular degeneration. Previous studies have suggested that enhancing proteasome activity by pretreatment with low doses of proteasome inhibitors reduces injury from oxidative damage in neuronal cultures. The objective of the current study...
S Mischke
Microbios, 87(352), 175-183 (1996-01-01)
Four chromogenic substrates were compared, and methods were developed for measuring protease activity from fungi. Digestion of azoalbumin, a water-soluble substrate, resulted in dye release most closely proportional to enzyme activity. Substrates insoluble in water were advantageous for time-course studies...
Jean-Pierre Falgueyret et al.
Analytical biochemistry, 335(2), 218-227 (2004-11-24)
We describe a novel diazomethylketone-containing irreversible inhibitor (BIL-DMK) which is specific for a subset of pharmaceutically important cysteine cathepsin proteases. BIL-DMK rapidly inactivates cathepsins B, F, K, L, S, and V in isolated enzyme assays and labels cathepsins in whole...
Vincent Everts et al.
Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 21(9), 1399-1408 (2006-08-31)
Osteoclastic bone degradation involves the activity of cathepsin K. We found that in addition to this enzyme other, yet unknown, cysteine proteinases participate in digestion. The results support the notion that osteoclasts from different bone sites use different enzymes to...
L Xia et al.
Biological chemistry, 380(6), 679-687 (1999-08-03)
We have localized cathepsin K in rat osteoclasts and within exposed resorption pits by immuno-fluorescence microscopy. Intracellular staining using an antibody raised against recombinant mouse cathepsin K was vesicular and uniformly distributed throughout the cell. Confocal microscopy analysis did not...
T Moldoveanu et al.
Journal of molecular biology, 343(5), 1313-1326 (2004-10-20)
The endogenous calpain inhibitor, calpastatin, modulates some patho-physiological aspects of calpain signaling. Excess calpain can escape this inhibition and as well, many calpain isoforms and autolytically generated protease core fragments are not inhibited by calpastatin. There is a need, therefore...
Marko Novinec et al.
FEBS letters, 586(7), 1062-1066 (2012-05-10)
The cysteine peptidase cathepsin K is a major player in extracellular proteolysis. Here we describe the identification of the multifunctional extracellular chaperone clusterin as a cathepsin K-binding protein. Clusterin increases the stability of cathepsin K in dilute solution and in...
Lykourgos Chiniadis et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 25(4), 635-645 (2020-04-09)
The high-resolution X-ray crystal structures of the adducts formed between the "half sandwich"-type Ru(II) coordination compound [RuII(1,4,7-trithiacyclononane)(ethane-1,2-diamine)Cl]+ and two proteins, namely hen egg-white lysozyme and proteinase K, are presented. The structures unveil that upon reaction with both enzymes the Ru(II)...
S A Niazi et al.
International endodontic journal, 48(12), 1157-1167 (2014-12-09)
To investigate the dynamics of a disinfection regimen using 1% trypsin and 1% proteinase K in combination with 2% chlorhexidine (with or without ultrasonics) using a nutrient-stressed endodontic multispecies model biofilm. Nutrient-stressed biofilms (Propionibacterium acnes, Staphylococcus epidermidis, Actinomyces radicidentis, Streptococcus...
Zoran Rankovic et al.
Bioorganic & medicinal chemistry letters, 20(5), 1524-1527 (2010-02-13)
Morphing structural features of HTS-derived chemotypes led to the discovery of novel 2-cyano-pyrimidine inhibitors of cathepsin K with good pharmacokinetic profiles, for example, compound 20 showed high catK potency (IC(50)=4nM), >580-fold selectivity over catL and catB, and oral bioavailability in...
Min Yang et al.
Arteriosclerosis, thrombosis, and vascular biology, 28(12), 2202-2208 (2008-09-27)
Previous studies demonstrated increased levels of cysteine proteases cathepsins in serum and adipose tissues from obese patients. We now provide evidence from a mouse model of obesity to suggest a direct participation of cathepsin K (CatK) in mouse body weight...
M Motiur Rahman et al.
Biochemical and biophysical research communications, 462(2), 159-164 (2015-05-09)
In an attempt to identify secretory products of osteoclasts that mediate the coupling of bone formation to resorption, we found that along with osteoclast differentiation, PDGF-A gene expression increase occurred first, by 12 h after stimulation of bone marrow macrophages...
Marko Novinec et al.
The Biochemical journal, 429(2), 379-389 (2010-05-11)
The human cysteine peptidase cathepsin K is a key enzyme in bone homoeostasis and other physiological functions. In the present study we investigate the mechanism of cathepsin K action at physiological plasma pH and its regulation by modifiers that bind...
Shun-ichi Tanaka et al.
Biochimica et biophysica acta, 1814(2), 299-307 (2010-11-30)
A serpin homologue (Tk-serpin) from the hyperthermophilic archaeon Thermococcus kodakaraensis was overproduced in E. coli, purified, and characterized. Tk-serpin irreversibly inhibits Tk-subtilisin (TKS) from the same organism with the second-order association rate constants (k(ass)) of 5.2×10³ M⁻¹ s⁻¹ at 40°C...
Yinan Ma et al.
Macromolecular bioscience, 16(1), 151-159 (2015-09-22)
Oligomerization of thiol-unprotected L-cysteine ethyl ester (Cys-OEt) catalyzed by proteinase K in aqueous solution has been used to synthesize oligo(L-cysteine) (OligoCys) with a well-defined chemical structure and relatively large degree of polymerization (DP) up to 16-17 (average 8.8). By using...
Ana-Maria Lennon-Duménil et al.
The Journal of experimental medicine, 196(4), 529-540 (2002-08-21)
Here, we describe a new approach designed to monitor the proteolytic activity of maturing phagosomes in live antigen-presenting cells. We find that an ingested particle sequentially encounters distinct protease activities during phagosomal maturation. Incorporation of active proteases into the phagosome...
Junfeng Han et al.
Endocrine journal, 56(1), 55-63 (2008-10-09)
We previously found that cathepsin K (CTSK) played an important role in adipocyte differentiation. However, the underlying molecular mechanism is not clear. Through the time window study, it was observed that CTSK activities were required mainly in the early phases...
Natasa Obermajer et al.
Experimental cell research, 312(13), 2515-2527 (2006-06-16)
Cathepsin X is a lysosomal carboxypeptidase with a potential role in processes of inflammation and immune response. The integrin-binding motifs RGD and ECD, present in the pro- and in mature forms of cathepsin X, respectively, suggest that this enzyme might...
Emma V Beale et al.
Frontiers in molecular biosciences, 7, 179-179 (2020-08-28)
MicroED has recently emerged as a powerful method for the analysis of biological structures at atomic resolution. This technique has been largely limited to protein nanocrystals which grow either as needles or plates measuring only a few hundred nanometers in...
Vitaly D Samuilov et al.
Bioscience reports, 23(2-3), 103-117 (2003-10-23)
Mitochondria are known to participate in the initiation of programmed cell death (PCD) in animals and in plants. The role of chloroplasts in PCD is still unknown. We describe a new system to study PCD in plants; namely, leaf epidermal...
Tadashi Hayami et al.
Bone, 50(6), 1250-1259 (2012-04-10)
To investigate the disease modifying effects of cathepsin K (CatK) inhibitor L-006235 compared to alendronate (ALN) in two preclinical models of osteoarthritis (OA). Skeletally mature rabbits underwent sham or anterior cruciate ligament transection (ACLT)-surgery and were treated with L-006235 (L-235...
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