PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21193413-0 2011 Structure-activity analysis of cathepsin K/chondroitin 4-sulfate interactions. Chondroitin Sulfates 43-64 cathepsin K Homo sapiens 31-42 28771551-8 2017 Molecular dynamics simulations show that the conformation of cathepsin K is influenced by known allosteric effectors, chondroitin sulfate and the small molecules NSC13345 and NSC94914. Chondroitin Sulfates 118-137 cathepsin K Homo sapiens 61-72 24958728-4 2014 We have demonstrated that chondroitin 4-sulfate (C4-S) promotes autoprocessing of the pro-domain of CatK at pH <= 5, leading to a fully matured enzyme with collagenase and peptidase activities. Chondroitin Sulfates 26-47 cathepsin K Homo sapiens 100-104 24958728-4 2014 We have demonstrated that chondroitin 4-sulfate (C4-S) promotes autoprocessing of the pro-domain of CatK at pH <= 5, leading to a fully matured enzyme with collagenase and peptidase activities. Chondroitin Sulfates 49-53 cathepsin K Homo sapiens 100-104 24958728-6 2014 During bone resorption, CatK and C4-S are co-localized at the ruffled border between osteoclast bone interface, supporting the proposal that CatK activation is accomplished through the combined action of the acidic environment together with the presence of a high concentration of C4-S. Chondroitin Sulfates 33-37 cathepsin K Homo sapiens 141-145 24958728-6 2014 During bone resorption, CatK and C4-S are co-localized at the ruffled border between osteoclast bone interface, supporting the proposal that CatK activation is accomplished through the combined action of the acidic environment together with the presence of a high concentration of C4-S. Chondroitin Sulfates 281-285 cathepsin K Homo sapiens 24-28 24958728-6 2014 During bone resorption, CatK and C4-S are co-localized at the ruffled border between osteoclast bone interface, supporting the proposal that CatK activation is accomplished through the combined action of the acidic environment together with the presence of a high concentration of C4-S. Chondroitin Sulfates 281-285 cathepsin K Homo sapiens 141-145 24958728-7 2014 Formation of a multimeric complex between C4-S and pro-CatK has been speculated to accelerate CatK autoactivation and promote efficient collagen degradation. Chondroitin Sulfates 42-46 cathepsin K Homo sapiens 55-59 24958728-7 2014 Formation of a multimeric complex between C4-S and pro-CatK has been speculated to accelerate CatK autoactivation and promote efficient collagen degradation. Chondroitin Sulfates 42-46 cathepsin K Homo sapiens 94-98 24958728-8 2014 Together, these results demonstrate that CS plays an important role in contributing to the enhanced efficiency of CatK collagenase activity in vivo. Chondroitin Sulfates 41-43 cathepsin K Homo sapiens 114-118 22822386-4 2012 Atomic model assessment of the CTSK gene revealed that the R122P mutant could disrupt hydrogen bonds binding with chondroitin 4-sulfate leading to a decrease in the collagen-degrading activity of cathepsin K. Chondroitin Sulfates 114-135 cathepsin K Homo sapiens 31-35 22822386-4 2012 Atomic model assessment of the CTSK gene revealed that the R122P mutant could disrupt hydrogen bonds binding with chondroitin 4-sulfate leading to a decrease in the collagen-degrading activity of cathepsin K. Chondroitin Sulfates 114-135 cathepsin K Homo sapiens 196-207 24958728-0 2014 Chondroitin sulfate promotes activation of cathepsin K. Chondroitin Sulfates 0-19 cathepsin K Homo sapiens 43-54 24958728-2 2014 Evidence exists that the collagenase activity of CatK is promoted by chondroitin sulfate (CS), a sulfated glycosaminoglycan. Chondroitin Sulfates 69-88 cathepsin K Homo sapiens 49-53 24958728-2 2014 Evidence exists that the collagenase activity of CatK is promoted by chondroitin sulfate (CS), a sulfated glycosaminoglycan. Chondroitin Sulfates 90-92 cathepsin K Homo sapiens 49-53 24958728-3 2014 This study examines the role of CS in facilitating CatK activation. Chondroitin Sulfates 32-34 cathepsin K Homo sapiens 51-55 21193413-1 2011 In the presence of oligomeric chondroitin 4-sulfate (C4-S), cathepsin K (catK) forms a specific complex that was shown to be the source of the major collagenolytic activity in bone osteoclasts. Chondroitin Sulfates 30-51 cathepsin K Homo sapiens 60-71 21193413-1 2011 In the presence of oligomeric chondroitin 4-sulfate (C4-S), cathepsin K (catK) forms a specific complex that was shown to be the source of the major collagenolytic activity in bone osteoclasts. Chondroitin Sulfates 30-51 cathepsin K Homo sapiens 73-77 21193413-1 2011 In the presence of oligomeric chondroitin 4-sulfate (C4-S), cathepsin K (catK) forms a specific complex that was shown to be the source of the major collagenolytic activity in bone osteoclasts. Chondroitin Sulfates 53-57 cathepsin K Homo sapiens 60-71 21193413-1 2011 In the presence of oligomeric chondroitin 4-sulfate (C4-S), cathepsin K (catK) forms a specific complex that was shown to be the source of the major collagenolytic activity in bone osteoclasts. Chondroitin Sulfates 53-57 cathepsin K Homo sapiens 73-77 21193413-2 2011 C4-S forms multiple contacts with amino acid residues on the backside of the catK molecule that help to facilitate complex formation. Chondroitin Sulfates 0-4 cathepsin K Homo sapiens 77-81 21193413-3 2011 As cathepsin L does not exhibit a significant collagenase activity in the presence or in the absence of C4-S, we substituted the C4-S interacting residues in catK with those of cathepsin L. Chondroitin Sulfates 129-133 cathepsin K Homo sapiens 158-162 21193413-7 2011 C4-S is not continuously ordered as it is in the wild-type catK C4-S complex. Chondroitin Sulfates 0-4 cathepsin K Homo sapiens 59-63 21193413-7 2011 C4-S is not continuously ordered as it is in the wild-type catK C4-S complex. Chondroitin Sulfates 64-68 cathepsin K Homo sapiens 59-63 21193413-10 2011 These substitutions have changed the mode of catK binding to C4-S and, as a result, have likely affected the collagenolytic potential of the variant. Chondroitin Sulfates 61-65 cathepsin K Homo sapiens 45-49 18692071-3 2008 Here, we describe the crystal structure of a 1:n complex of cathepsin K:C4-S inhibited by E64 at a resolution of 1.8 A. Chondroitin Sulfates 72-76 cathepsin K Homo sapiens 60-71 18692071-0 2008 The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex. Chondroitin Sulfates 54-73 cathepsin K Homo sapiens 42-53 18692071-2 2008 We showed earlier that the unique triple-helical collagen-degrading activity of cathepsin K depends on the formation of complexes with bone-or cartilage-resident glycosaminoglycans, such as chondroitin 4-sulfate (C4-S). Chondroitin Sulfates 190-211 cathepsin K Homo sapiens 80-91 18692071-2 2008 We showed earlier that the unique triple-helical collagen-degrading activity of cathepsin K depends on the formation of complexes with bone-or cartilage-resident glycosaminoglycans, such as chondroitin 4-sulfate (C4-S). Chondroitin Sulfates 213-217 cathepsin K Homo sapiens 80-91 18692071-8 2008 Biochemical analyses of cathepsin K and C4-S mixtures support the presence of a 1:n complex in solution; a dissociation constant, K(d), of about 10 nM was determined for the interaction between cathepsin K and C4-S. Chondroitin Sulfates 40-44 cathepsin K Homo sapiens 194-205 18692071-8 2008 Biochemical analyses of cathepsin K and C4-S mixtures support the presence of a 1:n complex in solution; a dissociation constant, K(d), of about 10 nM was determined for the interaction between cathepsin K and C4-S. Chondroitin Sulfates 210-214 cathepsin K Homo sapiens 24-35 18692071-8 2008 Biochemical analyses of cathepsin K and C4-S mixtures support the presence of a 1:n complex in solution; a dissociation constant, K(d), of about 10 nM was determined for the interaction between cathepsin K and C4-S. Chondroitin Sulfates 210-214 cathepsin K Homo sapiens 194-205 17426030-3 2007 Three different mechanisms to interfere with cathepsin-catalyzed collagen degradation are discussed: 1) inhibition of the formation of the cathepsin K/C4-S complex, 2) inhibition of the attachment of C4-S to collagen, and 3) masking of the collagenase cleavage sites in collagen. Chondroitin Sulfates 151-155 cathepsin K Homo sapiens 139-150 17426030-5 2007 The main inhibitory effect on collagen degradation is due to the impeding effect on the active cathepsin K/C4-S complex. Chondroitin Sulfates 107-111 cathepsin K Homo sapiens 95-106 17426030-6 2007 Essential structural elements in the inhibitor molecules are negative charges which compete with the sulfate groups of C4-S in the cathepsin K/C4-S complex. Chondroitin Sulfates 119-123 cathepsin K Homo sapiens 131-142 17426030-6 2007 Essential structural elements in the inhibitor molecules are negative charges which compete with the sulfate groups of C4-S in the cathepsin K/C4-S complex. Chondroitin Sulfates 143-147 cathepsin K Homo sapiens 131-142 17426030-8 2007 Longer negatively charged polymers (e.g. polyglutamates, oligonucleotides) tend to inhibit all three mechanisms, whereas shorter ones preferentially affect the cathepsin K/C4-S complex. Chondroitin Sulfates 172-176 cathepsin K Homo sapiens 160-171 14645229-1 2004 Cathepsin K, a lysosomal papain-like cysteine protease, forms collagenolytically highly active complexes with chondroitin sulfate and represents the most potent mammalian collagenase. Chondroitin Sulfates 110-129 cathepsin K Homo sapiens 0-11 12039963-0 2002 Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. Chondroitin Sulfates 70-89 cathepsin K Homo sapiens 24-35 12039963-4 2002 Here, we report a cathepsin K-specific complex with chondroitin sulfate, which is essential for the collagenolytic activity of the enzyme. Chondroitin Sulfates 52-71 cathepsin K Homo sapiens 18-29 12039963-7 2002 The primary substrate specificity of cathepsin K is not altered by complex formation, suggesting that the protease-chondroitin sulfate complex primarily facilitates the destabilization and/or the specific binding of the triple helical collagen structure. Chondroitin Sulfates 115-134 cathepsin K Homo sapiens 37-48 12039963-9 2002 The physiological relevance of cathepsin K complexes is supported by the findings that (i) the content of chondroitin sulfate present in bone and accessible to cathepsin K activity is sufficient for complex formation and (ii) Y212C, a cathepsin K mutant that causes pycnodysostosis (a bone sclerosing disorder) and that has no collagenase activity but remains potent as a gelatinase, is unable to form complexes. Chondroitin Sulfates 106-125 cathepsin K Homo sapiens 31-42 12039963-9 2002 The physiological relevance of cathepsin K complexes is supported by the findings that (i) the content of chondroitin sulfate present in bone and accessible to cathepsin K activity is sufficient for complex formation and (ii) Y212C, a cathepsin K mutant that causes pycnodysostosis (a bone sclerosing disorder) and that has no collagenase activity but remains potent as a gelatinase, is unable to form complexes. Chondroitin Sulfates 106-125 cathepsin K Homo sapiens 160-171 12039963-9 2002 The physiological relevance of cathepsin K complexes is supported by the findings that (i) the content of chondroitin sulfate present in bone and accessible to cathepsin K activity is sufficient for complex formation and (ii) Y212C, a cathepsin K mutant that causes pycnodysostosis (a bone sclerosing disorder) and that has no collagenase activity but remains potent as a gelatinase, is unable to form complexes. Chondroitin Sulfates 106-125 cathepsin K Homo sapiens 160-171