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Showing 1 to 12 of 46 entries
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New cytotoxics and non-cytotoxics in epithelial ovarian cancer.

International journal of gynecological cancer : official journal of the International Gynecological Cancer Society

Eisenhauer EA.
PMID: 11240731
Int J Gynecol Cancer. 2000 Jan;10:38-43. doi: 10.1046/j.1525-1438.2000.99509.x.

Several new cytotoxic agents with activity in relapsed ovarian cancer are being combined with paclitaxel plus platinum as the first step to assess their impact in randomized trials against the standard treatment. These include topotecan, gemcitabine, epirubicin, and liposomal...

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Eisenhauer EA. New cytotoxics and non-cytotoxics in epithelial ovarian cancer. Int J Gynecol Cancer. 2000;10:38-43doi: 10.1046/j.1525-1438.2000.99509.x.
Eisenhauer, E. A. (2000). New cytotoxics and non-cytotoxics in epithelial ovarian cancer. International journal of gynecological cancer : official journal of the International Gynecological Cancer Society, 1038-43. https://doi.org/10.1046/j.1525-1438.2000.99509.x
Eisenhauer, E. A.. "New cytotoxics and non-cytotoxics in epithelial ovarian cancer." International journal of gynecological cancer : official journal of the International Gynecological Cancer Society vol. 10 (2000): 38-43. doi: https://doi.org/10.1046/j.1525-1438.2000.99509.x
Eisenhauer EA. New cytotoxics and non-cytotoxics in epithelial ovarian cancer. Int J Gynecol Cancer. 2000 Jan;10:38-43. doi: 10.1046/j.1525-1438.2000.99509.x. PMID: 11240731.
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Enhancement of fibrinogen-triggered pro-coagulant activation of monocytes in vitro by matrix metalloproteinase-9.

Thrombosis journal

Kaneider NC, Mosheimer B, Günther A, Feistritzer C, Wiedermann CJ.
PMID: 20181055
Thromb J. 2010 Jan 29;8(1):2. doi: 10.1186/1477-9560-8-2.

BACKGROUND: Interaction of fibrinogen with specific leukocyte integrins of monocytes may link coagulation and inflammation, however, the precise mechanism of fibrinogen leading to the pro-inflammatory and pro-coagulatory response on monocytes is yet unknown.RESULTS: Fibrinogen and its digestion fragment D...

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Kaneider NC, Mosheimer B, Günther A, et al. Enhancement of fibrinogen-triggered pro-coagulant activation of monocytes in vitro by matrix metalloproteinase-9. Thromb J. 2010;8(1):2doi: 10.1186/1477-9560-8-2.
Kaneider, N. C., Mosheimer, B., Günther, A., Feistritzer, C., & Wiedermann, C. J. (2010). Enhancement of fibrinogen-triggered pro-coagulant activation of monocytes in vitro by matrix metalloproteinase-9. Thrombosis journal, 8(1), 2. https://doi.org/10.1186/1477-9560-8-2
Kaneider, Nicole C, et al. "Enhancement of fibrinogen-triggered pro-coagulant activation of monocytes in vitro by matrix metalloproteinase-9." Thrombosis journal vol. 8,1 (2010): 2. doi: https://doi.org/10.1186/1477-9560-8-2
Kaneider NC, Mosheimer B, Günther A, Feistritzer C, Wiedermann CJ. Enhancement of fibrinogen-triggered pro-coagulant activation of monocytes in vitro by matrix metalloproteinase-9. Thromb J. 2010 Jan 29;8(1):2. doi: 10.1186/1477-9560-8-2. PMID: 20181055; PMCID: PMC2837620.
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Effect of Doxycycline Microencapsulation on Buccal Films: Stability, Mucoadhesion and In Vitro Drug Release.

Gels (Basel, Switzerland)

Patlolla VGR, Popovic N, Peter Holbrook W, Kristmundsdottir T, Gizurarson S.
PMID: 33924744
Gels. 2021 Apr 28;7(2). doi: 10.3390/gels7020051.

The aim of this work was to stabilize doxycycline in mucoadhesive buccal films at room temperature (25 °C). Since doxycycline is susceptible to degradation such as oxidation and epimerization, tablets are currently the only formulation that can keep the...

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Patlolla VGR, Popovic N, Peter Holbrook W, et al. Effect of Doxycycline Microencapsulation on Buccal Films: Stability, Mucoadhesion and In Vitro Drug Release. Gels. 2021;7(2)doi: 10.3390/gels7020051.
Patlolla, V. G. R., Popovic, N., Peter Holbrook, W., Kristmundsdottir, T., & Gizurarson, S. (2021). Effect of Doxycycline Microencapsulation on Buccal Films: Stability, Mucoadhesion and In Vitro Drug Release. Gels (Basel, Switzerland), 7(2), . https://doi.org/10.3390/gels7020051
Patlolla, Venu Gopal Reddy, et al. "Effect of Doxycycline Microencapsulation on Buccal Films: Stability, Mucoadhesion and In Vitro Drug Release." Gels (Basel, Switzerland) vol. 7,2 (2021). doi: https://doi.org/10.3390/gels7020051
Patlolla VGR, Popovic N, Peter Holbrook W, Kristmundsdottir T, Gizurarson S. Effect of Doxycycline Microencapsulation on Buccal Films: Stability, Mucoadhesion and In Vitro Drug Release. Gels. 2021 Apr 28;7(2). doi: 10.3390/gels7020051. PMID: 33924744; PMCID: PMC8167737.
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Does Chemically Modified Curcumin Control the Progression of Periodontitis? A Systematic Review.

Journal of experimental pharmacology

Dhaifullah E, Seayed HS, Mostafa D, Alharbi AMM, Alotaibi WM.
PMID: 34135646
J Exp Pharmacol. 2021 Jun 09;13:565-575. doi: 10.2147/JEP.S313192. eCollection 2021.

BACKGROUND: Recently, pharmacologic approaches have been seen in utilizing matrix metalloproteinase inhibitors (MMP-I) to prohibit the destruction of connective tissue accompanied by erythrogenic inflammatory diseases such as periodontitis. However, curcumin characteristics have been described to be effective in reducing...

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Dhaifullah E, Seayed HS, Mostafa D, et al. Does Chemically Modified Curcumin Control the Progression of Periodontitis? A Systematic Review. J Exp Pharmacol. 2021;13:565-575doi: 10.2147/JEP.S313192.
Dhaifullah, E., Seayed, H. S., Mostafa, D., Alharbi, A. M. M., & Alotaibi, W. M. (2021). Does Chemically Modified Curcumin Control the Progression of Periodontitis? A Systematic Review. Journal of experimental pharmacology, 13565-575. https://doi.org/10.2147/JEP.S313192
Dhaifullah, Esam, et al. "Does Chemically Modified Curcumin Control the Progression of Periodontitis? A Systematic Review." Journal of experimental pharmacology vol. 13 (2021): 565-575. doi: https://doi.org/10.2147/JEP.S313192
Dhaifullah E, Seayed HS, Mostafa D, Alharbi AMM, Alotaibi WM. Does Chemically Modified Curcumin Control the Progression of Periodontitis? A Systematic Review. J Exp Pharmacol. 2021 Jun 09;13:565-575. doi: 10.2147/JEP.S313192. eCollection 2021. PMID: 34135646; PMCID: PMC8200174.
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Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin.

Current tissue engineering

Tsunenaga M.
PMID: 27853671
Curr Tissue Eng. 2016 Aug;5(2):113-122. doi: 10.2174/2211542005666160725154356.

Recent research suggests that the basement membrane at the dermal-epidermal junction of the skin plays an important role in maintaining a healthy epidermis and dermis, and repeated damage to the skin can destabilize the skin and accelerate the aging...

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Tsunenaga M. Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin. Curr Tissue Eng. 2016;5(2):113-122doi: 10.2174/2211542005666160725154356.
Tsunenaga, M. (2016). Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin. Current tissue engineering, 5(2), 113-122. https://doi.org/10.2174/2211542005666160725154356
Tsunenaga, Makoto. "Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin." Current tissue engineering vol. 5,2 (2016): 113-122. doi: https://doi.org/10.2174/2211542005666160725154356
Tsunenaga M. Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin. Curr Tissue Eng. 2016 Aug;5(2):113-122. doi: 10.2174/2211542005666160725154356. PMID: 27853671; PMCID: PMC5070419.
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New hope for matrix metalloproteinase inhibitors in cancer therapy.

Drug discovery today

Brown PD.
PMID: 11408196
Drug Discov Today. 2001 Jun 01;6(12):615. doi: 10.1016/s1359-6446(01)01845-1.

No abstract available.

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Brown PD. New hope for matrix metalloproteinase inhibitors in cancer therapy. Drug Discov Today. 2001;6(12):615doi: 10.1016/s1359-6446(01)01845-1.
Brown, P. D. (2001). New hope for matrix metalloproteinase inhibitors in cancer therapy. Drug discovery today, 6(12), 615. https://doi.org/10.1016/s1359-6446(01)01845-1
Brown, P D.. "New hope for matrix metalloproteinase inhibitors in cancer therapy." Drug discovery today vol. 6,12 (2001): 615. doi: https://doi.org/10.1016/s1359-6446(01)01845-1
Brown PD. New hope for matrix metalloproteinase inhibitors in cancer therapy. Drug Discov Today. 2001 Jun 01;6(12):615. doi: 10.1016/s1359-6446(01)01845-1. PMID: 11408196.
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Matrix metalloproteinase inhibitors.

Angiogenesis

Brown PD.
PMID: 14517381
Angiogenesis. 1998;1(2):142-54. doi: 10.1023/A:1018373520193.

Matrix metalloproteinases (MMPs) are a family of structurally related enzymes that are capable of degrading a wide variety of extracellular matrix proteins. In addition to the role played by these enzymes in normal tissue remodeling, MMPs have been implicted...

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Brown PD. Matrix metalloproteinase inhibitors. Angiogenesis. 1998;1(2):142-54doi: 10.1023/A:1018373520193.
Brown, P. D. (1998). Matrix metalloproteinase inhibitors. Angiogenesis, 1(2), 142-54. https://doi.org/10.1023/A:1018373520193
Brown, P D. "Matrix metalloproteinase inhibitors." Angiogenesis vol. 1,2 (1998): 142-54. doi: https://doi.org/10.1023/A:1018373520193
Brown PD. Matrix metalloproteinase inhibitors. Angiogenesis. 1998;1(2):142-54. doi: 10.1023/A:1018373520193. PMID: 14517381.
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Recent Advances in Adhesive Bonding - The Role of Biomolecules, Nanocompounds, and Bonding Strategies in Enhancing Resin Bonding to Dental Substrates.

Current oral health reports

Münchow EA, Bottino MC.
PMID: 29177123
Curr Oral Health Rep. 2017 Sep;4(3):215-227. doi: 10.1007/s40496-017-0146-y. Epub 2017 Jul 10.

PURPOSE OF REVIEW: To present an overview on the main agents (i.e., biomolecules and nanocompounds) and/or strategies currently available to amplify or stabilize resin-dentin bonding.RECENT FINDINGS: According to studies retrieved for full text reading (2014-2017), there are currently six...

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Münchow EA, Bottino MC. Recent Advances in Adhesive Bonding - The Role of Biomolecules, Nanocompounds, and Bonding Strategies in Enhancing Resin Bonding to Dental Substrates. Curr Oral Health Rep. 2017;4(3):215-227doi: 10.1007/s40496-017-0146-y.
Münchow, E. A., & Bottino, M. C. (2017). Recent Advances in Adhesive Bonding - The Role of Biomolecules, Nanocompounds, and Bonding Strategies in Enhancing Resin Bonding to Dental Substrates. Current oral health reports, 4(3), 215-227. https://doi.org/10.1007/s40496-017-0146-y
Münchow, Eliseu A, and Bottino, Marco C. "Recent Advances in Adhesive Bonding - The Role of Biomolecules, Nanocompounds, and Bonding Strategies in Enhancing Resin Bonding to Dental Substrates." Current oral health reports vol. 4,3 (2017): 215-227. doi: https://doi.org/10.1007/s40496-017-0146-y
Münchow EA, Bottino MC. Recent Advances in Adhesive Bonding - The Role of Biomolecules, Nanocompounds, and Bonding Strategies in Enhancing Resin Bonding to Dental Substrates. Curr Oral Health Rep. 2017 Sep;4(3):215-227. doi: 10.1007/s40496-017-0146-y. Epub 2017 Jul 10. PMID: 29177123; PMCID: PMC5697773.
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Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks.

International journal of peptide research and therapeutics

Bhowmick M, Fields GB.
PMID: 24496015
Int J Pept Res Ther. 2012 Dec;18(4):335-339. doi: 10.1007/s10989-012-9307-y.

The efficient synthesis of an Fmoc-Gly-Ile phosphinic pseudodipeptide was desired as an eventual building block for construction of matrix metalloproteinase inhibitors. A Michael-type addition reaction of bis(tri-methylsilyl) phosphonite with the appropriate acrylate generated the pseudodipeptide bond. Additional of adamantyl...

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Bhowmick M, Fields GB. Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks. Int J Pept Res Ther. 2012;18(4):335-339doi: 10.1007/s10989-012-9307-y.
Bhowmick, M., & Fields, G. B. (2012). Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks. International journal of peptide research and therapeutics, 18(4), 335-339. https://doi.org/10.1007/s10989-012-9307-y
Bhowmick, Manishabrata, and Fields, Gregg B. "Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks." International journal of peptide research and therapeutics vol. 18,4 (2012): 335-339. doi: https://doi.org/10.1007/s10989-012-9307-y
Bhowmick M, Fields GB. Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks. Int J Pept Res Ther. 2012 Dec;18(4):335-339. doi: 10.1007/s10989-012-9307-y. PMID: 24496015; PMCID: PMC3564550.
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Design, synthesis, and primary activity evaluation of pyrrolidine derivatives as matrix metalloproteinase inhibitors.

Drug discoveries & therapeutics

Zhang J, Li X, Zhu HW, Wang Q, Feng JH, Mou JJ, Li YG, Fang H, Xu WF.
PMID: 22491146
Drug Discov Ther. 2010 Feb;4(1):5-12.

A series of novel pyrrolidine derivatives was designed, synthesized, and assayed to determine the derivatives' activity against matrix metalloproteinase-2 (MMP-2) and aminopeptidase N (APN)/CD13. Preliminary biological tests showed that most compounds inhibit MMP-2 in a highly selective manner compared...

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Zhang J, Li X, Zhu HW, et al. Design, synthesis, and primary activity evaluation of pyrrolidine derivatives as matrix metalloproteinase inhibitors. Drug Discov Ther. 2010;4(1):5-12
Zhang, J., Li, X., Zhu, H. W., Wang, Q., Feng, J. H., Mou, J. J., Li, Y. G., Fang, H., & Xu, W. F. (2010). Design, synthesis, and primary activity evaluation of pyrrolidine derivatives as matrix metalloproteinase inhibitors. Drug discoveries & therapeutics, 4(1), 5-12.
Zhang, J, et al. "Design, synthesis, and primary activity evaluation of pyrrolidine derivatives as matrix metalloproteinase inhibitors." Drug discoveries & therapeutics vol. 4,1 (2010): 5-12.
Zhang J, Li X, Zhu HW, Wang Q, Feng JH, Mou JJ, Li YG, Fang H, Xu WF. Design, synthesis, and primary activity evaluation of pyrrolidine derivatives as matrix metalloproteinase inhibitors. Drug Discov Ther. 2010 Feb;4(1):5-12. PMID: 22491146.
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Two matrix metalloproteinase inhibitors from scrophularia striata boiss.

Iranian journal of pharmaceutical research : IJPR

Monsef-Esfahani HR, Shahverdi AR, Khorramizadeh MR, Amini M, Hajiaghaee R.
PMID: 24734066
Iran J Pharm Res. 2014;13(1):149-55.

Many species belonging to the Scrophularia genus have been used since ancient times as folk remedies for many medical conditions such as scrofulas, scabies, tumors, eczema, psoriasis, inflammations. The aim of this study was to characterize the matrix metalloproteinases...

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Monsef-Esfahani HR, Shahverdi AR, Khorramizadeh MR, et al. Two matrix metalloproteinase inhibitors from scrophularia striata boiss. Iran J Pharm Res. 2014;13(1):149-55
Monsef-Esfahani, H. R., Shahverdi, A. R., Khorramizadeh, M. R., Amini, M., & Hajiaghaee, R. (2014). Two matrix metalloproteinase inhibitors from scrophularia striata boiss. Iranian journal of pharmaceutical research : IJPR, 13(1), 149-55.
Monsef-Esfahani, Hamid Reza, et al. "Two matrix metalloproteinase inhibitors from scrophularia striata boiss." Iranian journal of pharmaceutical research : IJPR vol. 13,1 (2014): 149-55.
Monsef-Esfahani HR, Shahverdi AR, Khorramizadeh MR, Amini M, Hajiaghaee R. Two matrix metalloproteinase inhibitors from scrophularia striata boiss. Iran J Pharm Res. 2014;13(1):149-55. PMID: 24734066; PMCID: PMC3985265.
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Structure-based molecular insights into matrix metalloproteinase inhibitors in cancer treatments.

Future medicinal chemistry

Lin H, Xu P, Huang M.
PMID: 34779649
Future Med Chem. 2022 Jan;14(1):35-51. doi: 10.4155/fmc-2021-0246. Epub 2021 Nov 15.

Protease inhibitors are of considerable interest as anticancer agents. Matrix metalloproteinases (MMPs) were the earliest type of proteases considered as anticancer targets. The developments of MMP inhibitors (MMPIs) by pharmaceutical companies can be dated from the early 1980s. Thus...

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Lin H, Xu P, Huang M. Structure-based molecular insights into matrix metalloproteinase inhibitors in cancer treatments. Future Med Chem. 2021;14(1):35-51doi: 10.4155/fmc-2021-0246.
Lin, H., Xu, P., & Huang, M. (2022). Structure-based molecular insights into matrix metalloproteinase inhibitors in cancer treatments. Future medicinal chemistry, 14(1), 35-51. https://doi.org/10.4155/fmc-2021-0246
Lin, Haili, et al. "Structure-based molecular insights into matrix metalloproteinase inhibitors in cancer treatments." Future medicinal chemistry vol. 14,1 (2022): 35-51. doi: https://doi.org/10.4155/fmc-2021-0246
Lin H, Xu P, Huang M. Structure-based molecular insights into matrix metalloproteinase inhibitors in cancer treatments. Future Med Chem. 2022 Jan;14(1):35-51. doi: 10.4155/fmc-2021-0246. Epub 2021 Nov 15. PMID: 34779649.
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Showing 1 to 12 of 46 entries