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Showing 1 to 12 of 69 entries
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Effects of monocyte-endothelium interactions on the expression of type IV collagenases in monocytes.

Experimental and therapeutic medicine

Li YQ, Liu R, Xue JH, Zhang Y, Gao DF, Wu XS, Wang CX, Yang YB.
PMID: 25574228
Exp Ther Med. 2015 Feb;9(2):527-532. doi: 10.3892/etm.2014.2109. Epub 2014 Dec 05.

The adhesion of monocytes to endothelial cells is one of the early stages in the development of atherosclerosis. The expression of type IV collagenases, which include matrix metalloproteinase (MMP)-2 and MMP-9, in monocytes is hypothesized to play an important...

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Li YQ, Liu R, Xue JH, et al. Effects of monocyte-endothelium interactions on the expression of type IV collagenases in monocytes. Exp Ther Med. 2014;9(2):527-532doi: 10.3892/etm.2014.2109.
Li, Y. Q., Liu, R., Xue, J. H., Zhang, Y., Gao, D. F., Wu, X. S., Wang, C. X., & Yang, Y. B. (2015). Effects of monocyte-endothelium interactions on the expression of type IV collagenases in monocytes. Experimental and therapeutic medicine, 9(2), 527-532. https://doi.org/10.3892/etm.2014.2109
Li, Yong-Qin, et al. "Effects of monocyte-endothelium interactions on the expression of type IV collagenases in monocytes." Experimental and therapeutic medicine vol. 9,2 (2015): 527-532. doi: https://doi.org/10.3892/etm.2014.2109
Li YQ, Liu R, Xue JH, Zhang Y, Gao DF, Wu XS, Wang CX, Yang YB. Effects of monocyte-endothelium interactions on the expression of type IV collagenases in monocytes. Exp Ther Med. 2015 Feb;9(2):527-532. doi: 10.3892/etm.2014.2109. Epub 2014 Dec 05. PMID: 25574228; PMCID: PMC4280919.
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Requirement of mitogen-activated protein kinase for collagenase production by the fibronectin fragment in human articular chondrocytes in culture.

Modern rheumatology

Yasuda T, Julovi SM, Hiramitsu T, Yoshida M, Nakamura T.
PMID: 17028806
Mod Rheumatol. 2004;14(1):54-60. doi: 10.1007/s10165-003-0266-1.

Fibronectin fragments have been shown to up-regulate matrix metalloproteinase production in chondrocytes. We investigated the roles of mitogen-activated protein kinase (MAPK) pathways activated by the COOH-terminal heparin-binding fibronectin fragment (HBFN-f) in collagenase production by human chondrocytes in culture. In...

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Yasuda T, Julovi SM, Hiramitsu T, et al. Requirement of mitogen-activated protein kinase for collagenase production by the fibronectin fragment in human articular chondrocytes in culture. Mod Rheumatol. 2004;14(1):54-60doi: 10.1007/s10165-003-0266-1.
Yasuda, T., Julovi, S. M., Hiramitsu, T., Yoshida, M., & Nakamura, T. (2004). Requirement of mitogen-activated protein kinase for collagenase production by the fibronectin fragment in human articular chondrocytes in culture. Modern rheumatology, 14(1), 54-60. https://doi.org/10.1007/s10165-003-0266-1
Yasuda, Tadashi, et al. "Requirement of mitogen-activated protein kinase for collagenase production by the fibronectin fragment in human articular chondrocytes in culture." Modern rheumatology vol. 14,1 (2004): 54-60. doi: https://doi.org/10.1007/s10165-003-0266-1
Yasuda T, Julovi SM, Hiramitsu T, Yoshida M, Nakamura T. Requirement of mitogen-activated protein kinase for collagenase production by the fibronectin fragment in human articular chondrocytes in culture. Mod Rheumatol. 2004;14(1):54-60. doi: 10.1007/s10165-003-0266-1. PMID: 17028806.
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Matrix metalloproteinases in corneal inflammation.

The ocular surface

Li DQ, Pflugfelder SC.
PMID: 17216119
Ocul Surf. 2005 Oct;3(4):S198-202. doi: 10.1016/s1542-0124(12)70255-0.

Matrix metalloproteinases (MMPs) are a family of calcium-dependent, zinc-containing endoproteinases capable of degrading the extracellular matrix and basement membrane. Many inflammatory stimuli, such as wound healing, ultraviolet, hyperosmolarity, and stress, can stimulate production of inflammatory cytokines and a variety...

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Li DQ, Pflugfelder SC. Matrix metalloproteinases in corneal inflammation. Ocul Surf. 2005;3(4):S198-202doi: 10.1016/s1542-0124(12)70255-0.
Li, D. Q., & Pflugfelder, S. C. (2005). Matrix metalloproteinases in corneal inflammation. The ocular surface, 3(4), S198-202. https://doi.org/10.1016/s1542-0124(12)70255-0
Li, De-Quan, and Pflugfelder, Stephen C. "Matrix metalloproteinases in corneal inflammation." The ocular surface vol. 3,4 (2005): S198-202. doi: https://doi.org/10.1016/s1542-0124(12)70255-0
Li DQ, Pflugfelder SC. Matrix metalloproteinases in corneal inflammation. Ocul Surf. 2005 Oct;3(4):S198-202. doi: 10.1016/s1542-0124(12)70255-0. PMID: 17216119.
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Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells.

Anemia

Keegan PM, Surapaneni S, Platt MO.
PMID: 22550569
Anemia. 2012;2012:201781. doi: 10.1155/2012/201781. Epub 2012 Apr 09.

Sickle cell disease is a genetic disease that increases systemic inflammation as well as the risk of pediatric strokes, but links between sickle-induced inflammation and arterial remodeling are not clear. Cathepsins are powerful elastases and collagenases secreted by endothelial...

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Keegan PM, Surapaneni S, Platt MO. Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells. Anemia. 2012;2012:201781doi: 10.1155/2012/201781.
Keegan, P. M., Surapaneni, S., & Platt, M. O. (2012). Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells. Anemia, 2012201781. https://doi.org/10.1155/2012/201781
Keegan, Philip M, et al. "Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells." Anemia vol. 2012 (2012): 201781. doi: https://doi.org/10.1155/2012/201781
Keegan PM, Surapaneni S, Platt MO. Sickle cell disease activates peripheral blood mononuclear cells to induce cathepsins k and v activity in endothelial cells. Anemia. 2012;2012:201781. doi: 10.1155/2012/201781. Epub 2012 Apr 09. PMID: 22550569; PMCID: PMC3328887.
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Urinary matrix metalloproteinase activity in diabetic kidney disease: a potential marker of disease progression.

Nephron extra

Altemtam N, Nahas ME, Johnson T.
PMID: 22949917
Nephron Extra. 2012 Jan;2:219-32. doi: 10.1159/000339645. Epub 2012 Aug 09.

BACKGROUND: Progressive kidney fibrosis, associated with chronic kidney disease (CKD), results from an imbalance in extracellular matrix (ECM) homeostasis. Reduced matrix metalloproteinases (MMP) activity causing lower clearance of ECM proteins has been implicated mainly through an overproduction of tissue...

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Altemtam N, Nahas ME, Johnson T. Urinary matrix metalloproteinase activity in diabetic kidney disease: a potential marker of disease progression. Nephron Extra. 2012;2:219-32doi: 10.1159/000339645.
Altemtam, N., Nahas, M. E., & Johnson, T. (2012). Urinary matrix metalloproteinase activity in diabetic kidney disease: a potential marker of disease progression. Nephron extra, 2219-32. https://doi.org/10.1159/000339645
Altemtam, Nagi, et al. "Urinary matrix metalloproteinase activity in diabetic kidney disease: a potential marker of disease progression." Nephron extra vol. 2 (2012): 219-32. doi: https://doi.org/10.1159/000339645
Altemtam N, Nahas ME, Johnson T. Urinary matrix metalloproteinase activity in diabetic kidney disease: a potential marker of disease progression. Nephron Extra. 2012 Jan;2:219-32. doi: 10.1159/000339645. Epub 2012 Aug 09. PMID: 22949917; PMCID: PMC3433015.
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Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro.

Cells

Ibrahim WN, Doolaanea AA, Bin Abdull Rasad MSB.
PMID: 29320405
Cells. 2018 Jan 10;7(1). doi: 10.3390/cells7010007.

No abstract available.

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Ibrahim WN, Doolaanea AA, Bin Abdull Rasad MSB. Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro. Cells. 2018;7(1)doi: 10.3390/cells7010007.
Ibrahim, W. N., Doolaanea, A. A., & Bin Abdull Rasad, M. S. B. (2018). Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro. Cells, 7(1), . https://doi.org/10.3390/cells7010007
Ibrahim, Wisam Nabeel, et al. "Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro." Cells vol. 7,1 (2018). doi: https://doi.org/10.3390/cells7010007
Ibrahim WN, Doolaanea AA, Bin Abdull Rasad MSB. Effect of shRNA Mediated Silencing of YB-1 Protein on the Expression of Matrix Collagenases in Malignant Melanoma Cell In Vitro. Cells. 2018 Jan 10;7(1). doi: 10.3390/cells7010007. PMID: 29320405; PMCID: PMC5789280.
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Tetracyclines Inhibit Tissue Collagenases: Effects of Ingested Low-Dose and Local Delivery Systems.

Journal of periodontology

Golub LM, Goodson JM, Lee HM, Vidal AM, McNamara TF, Ramamurthy NS.
PMID: 29538954
J Periodontol. 1985 Nov;56:93-97. doi: 10.1902/jop.1985.56.11s.93.

In a series of experiments, Golub et al. demonstrated that tetracyclines, but not other antibiotics, can inhibit mammalian collagenases and proposed that this property could be useful in treating diseases, such as periodontal disease (but also included certain medical...

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Golub LM, Goodson JM, Lee HM, et al. Tetracyclines Inhibit Tissue Collagenases: Effects of Ingested Low-Dose and Local Delivery Systems. J Periodontol. 1985;56:93-97doi: 10.1902/jop.1985.56.11s.93.
Golub, L. M., Goodson, J. M., Lee, H. M., Vidal, A. M., McNamara, T. F., & Ramamurthy, N. S. (1985). Tetracyclines Inhibit Tissue Collagenases: Effects of Ingested Low-Dose and Local Delivery Systems. Journal of periodontology, 5693-97. https://doi.org/10.1902/jop.1985.56.11s.93
Golub, L M, et al. "Tetracyclines Inhibit Tissue Collagenases: Effects of Ingested Low-Dose and Local Delivery Systems." Journal of periodontology vol. 56 (1985): 93-97. doi: https://doi.org/10.1902/jop.1985.56.11s.93
Golub LM, Goodson JM, Lee HM, Vidal AM, McNamara TF, Ramamurthy NS. Tetracyclines Inhibit Tissue Collagenases: Effects of Ingested Low-Dose and Local Delivery Systems. J Periodontol. 1985 Nov;56:93-97. doi: 10.1902/jop.1985.56.11s.93. PMID: 29538954.
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Virulence Factors of the Periodontopathogen Actinobacillus actinomycetemcomitans.

Journal of periodontology

Fives-Taylor P, Meyer D, Mintz K.
PMID: 29539842
J Periodontol. 1996 Mar;67:291-297. doi: 10.1902/jop.1996.67.3s.291.

Actinobacillus actinomycetemcomitans is an important periodontopathogen that has been implicated in juvenile and adult periodontitis. This capnophilic coccobacillus elaborates a number of virulence factors such as a bacteriocin, chemotaxis-inhibiting factor, immunosuppressive factors, cytotoxic factors, Fc binding proteins, lipopolysaccharide (LPS),...

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Fives-Taylor P, Meyer D, Mintz K. Virulence Factors of the Periodontopathogen Actinobacillus actinomycetemcomitans. J Periodontol. 1996;67:291-297doi: 10.1902/jop.1996.67.3s.291.
Fives-Taylor, P., Meyer, D., & Mintz, K. (1996). Virulence Factors of the Periodontopathogen Actinobacillus actinomycetemcomitans. Journal of periodontology, 67291-297. https://doi.org/10.1902/jop.1996.67.3s.291
Fives-Taylor, P, et al. "Virulence Factors of the Periodontopathogen Actinobacillus actinomycetemcomitans." Journal of periodontology vol. 67 (1996): 291-297. doi: https://doi.org/10.1902/jop.1996.67.3s.291
Fives-Taylor P, Meyer D, Mintz K. Virulence Factors of the Periodontopathogen Actinobacillus actinomycetemcomitans. J Periodontol. 1996 Mar;67:291-297. doi: 10.1902/jop.1996.67.3s.291. PMID: 29539842.
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Lead identification and optimization of novel collagenase inhibitors; pharmacophore and structure based studies.

Bioinformation

Kalva S, Vadivelan S, Sanam R, Jagarlapudi SA, Saleena LM.
PMID: 22553386
Bioinformation. 2012;8(7):301-8. doi: 10.6026/97320630008301. Epub 2012 Apr 13.

In this study, chemical feature based pharmacophore models of MMP-1, MMP-8 and MMP-13 inhibitors have been developed with the aid of HypoGen module within Catalyst program package. In MMP-1 and MMP-13, all the compounds in the training set mapped...

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Kalva S, Vadivelan S, Sanam R, et al. Lead identification and optimization of novel collagenase inhibitors; pharmacophore and structure based studies. Bioinformation. 2012;8(7):301-8doi: 10.6026/97320630008301.
Kalva, S., Vadivelan, S., Sanam, R., Jagarlapudi, S. A., & Saleena, L. M. (2012). Lead identification and optimization of novel collagenase inhibitors; pharmacophore and structure based studies. Bioinformation, 8(7), 301-8. https://doi.org/10.6026/97320630008301
Kalva, Sukesh, et al. "Lead identification and optimization of novel collagenase inhibitors; pharmacophore and structure based studies." Bioinformation vol. 8,7 (2012): 301-8. doi: https://doi.org/10.6026/97320630008301
Kalva S, Vadivelan S, Sanam R, Jagarlapudi SA, Saleena LM. Lead identification and optimization of novel collagenase inhibitors; pharmacophore and structure based studies. Bioinformation. 2012;8(7):301-8. doi: 10.6026/97320630008301. Epub 2012 Apr 13. PMID: 22553386; PMCID: PMC3338973.
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[No title available]

Microorganisms

Salamone M, Nicosia A, Ghersi G, Tagliavia M.
PMID: 31554228
Microorganisms. 2019 Sep 24;7(10). doi: 10.3390/microorganisms7100387.

Proteolytic enzymes are of great interest for biotechnological purposes, and their large-scale production, as well as the discovery of strains producing new molecules, is a relevant issue. Collagenases are employed for biomedical and pharmaceutical purposes. The high specificity of...

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Salamone M, Nicosia A, Ghersi G, et al. . Microorganisms. 2019;7(10)doi: 10.3390/microorganisms7100387.
Salamone, M., Nicosia, A., Ghersi, G., & Tagliavia, M. (2019). . Microorganisms, 7(10), . https://doi.org/10.3390/microorganisms7100387
Salamone, Monica, et al. "." Microorganisms vol. 7,10 (2019). doi: https://doi.org/10.3390/microorganisms7100387
Salamone M, Nicosia A, Ghersi G, Tagliavia M. . Microorganisms. 2019 Sep 24;7(10). doi: 10.3390/microorganisms7100387. PMID: 31554228; PMCID: PMC6843219.
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Dentin degradonomics - The potential role of salivary MMP-8 in dentin caries.

Journal of clinical and experimental dentistry

Ashwini A, Dineshkumar T, Rameshkumar A, Swarnalakshmi R, Shahnaz A, Nagarathinam AE, Rajkumar K.
PMID: 32071691
J Clin Exp Dent. 2020 Feb 01;12(2):e108-e115. doi: 10.4317/jced.56144. eCollection 2020 Feb.

BACKGROUND: Dentin caries involves dissolution of minerals which eventually leads to degradation of organic matrix. This degradation which was thought to be by bacterial proteases is now considered to be orchestrated by endogenous collagenases such as Matrix Metalloproteinases (MMPs)....

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Ashwini A, Dineshkumar T, Rameshkumar A, et al. Dentin degradonomics - The potential role of salivary MMP-8 in dentin caries. J Clin Exp Dent. 2020;12(2):e108-e115doi: 10.4317/jced.56144.
Ashwini, A., Dineshkumar, T., Rameshkumar, A., Swarnalakshmi, R., Shahnaz, A., Nagarathinam, A. E., & Rajkumar, K. (2020). Dentin degradonomics - The potential role of salivary MMP-8 in dentin caries. Journal of clinical and experimental dentistry, 12(2), e108-e115. https://doi.org/10.4317/jced.56144
Ashwini, Ajay, et al. "Dentin degradonomics - The potential role of salivary MMP-8 in dentin caries." Journal of clinical and experimental dentistry vol. 12,2 (2020): e108-e115. doi: https://doi.org/10.4317/jced.56144
Ashwini A, Dineshkumar T, Rameshkumar A, Swarnalakshmi R, Shahnaz A, Nagarathinam AE, Rajkumar K. Dentin degradonomics - The potential role of salivary MMP-8 in dentin caries. J Clin Exp Dent. 2020 Feb 01;12(2):e108-e115. doi: 10.4317/jced.56144. eCollection 2020 Feb. PMID: 32071691; PMCID: PMC7018481.
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An in vitro evaluation of the Native American ethnomedicinal plant Eryngium yuccifolium as a treatment for snakebite envenomation.

Journal of intercultural ethnopharmacology

Price JA.
PMID: 27366346
J Intercult Ethnopharmacol. 2016 May 04;5(3):219-25. doi: 10.5455/jice.20160421070136. eCollection 2016.

AIM: At least seven North American tribes specifically mention the use of Eryngium (typically roots) as an anti-snake venom therapy. As snake envenomation is an endemic, life-threatening medical risk, is there a scientific basis for the Native American ethnomedicine?...

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Price JA. An in vitro evaluation of the Native American ethnomedicinal plant Eryngium yuccifolium as a treatment for snakebite envenomation. J Intercult Ethnopharmacol. 2016;5(3):219-25doi: 10.5455/jice.20160421070136.
Price, J. A. (2016). An in vitro evaluation of the Native American ethnomedicinal plant Eryngium yuccifolium as a treatment for snakebite envenomation. Journal of intercultural ethnopharmacology, 5(3), 219-25. https://doi.org/10.5455/jice.20160421070136
Price, Joseph A. "An in vitro evaluation of the Native American ethnomedicinal plant Eryngium yuccifolium as a treatment for snakebite envenomation." Journal of intercultural ethnopharmacology vol. 5,3 (2016): 219-25. doi: https://doi.org/10.5455/jice.20160421070136
Price JA. An in vitro evaluation of the Native American ethnomedicinal plant Eryngium yuccifolium as a treatment for snakebite envenomation. J Intercult Ethnopharmacol. 2016 May 04;5(3):219-25. doi: 10.5455/jice.20160421070136. eCollection 2016. PMID: 27366346; PMCID: PMC4927125.
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Showing 1 to 12 of 69 entries