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Enzyme Inhibitors as the Attractive Targets for the Treatment of Various Diseases.

Current medicinal chemistry

Orhan IE.
PMID: 31526340
Curr Med Chem. 2019;26(18):3206-3207. doi: 10.2174/092986732618190821115641.

No abstract available.

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Orhan IE. Enzyme Inhibitors as the Attractive Targets for the Treatment of Various Diseases. Curr Med Chem. 2019;26(18):3206-3207doi: 10.2174/092986732618190821115641.
Orhan, I. E. (2019). Enzyme Inhibitors as the Attractive Targets for the Treatment of Various Diseases. Current medicinal chemistry, 26(18), 3206-3207. https://doi.org/10.2174/092986732618190821115641
Orhan, Ilkay Erdogan. "Enzyme Inhibitors as the Attractive Targets for the Treatment of Various Diseases." Current medicinal chemistry vol. 26,18 (2019): 3206-3207. doi: https://doi.org/10.2174/092986732618190821115641
Orhan IE. Enzyme Inhibitors as the Attractive Targets for the Treatment of Various Diseases. Curr Med Chem. 2019;26(18):3206-3207. doi: 10.2174/092986732618190821115641. PMID: 31526340.
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In silico identification of potential inhibitors against human 2'-5'- oligoadenylate synthetase (OAS) proteins.

Computational biology and chemistry

Gonzalez KJ, Moncada-Giraldo DM, Gutierrez JB.
PMID: 32004971
Comput Biol Chem. 2020 Apr;85:107211. doi: 10.1016/j.compbiolchem.2020.107211. Epub 2020 Jan 22.

As part of the type I IFN signaling, the 2'-5'- oligoadenylate synthetase (OAS) proteins have been involved in the progression of several non-viral diseases. Notably, OAS has been correlated with immune-modulatory functions that promote chronic inflammatory conditions, autoimmune disorders,...

Cite
Gonzalez KJ, Moncada-Giraldo DM, Gutierrez JB. In silico identification of potential inhibitors against human 2'-5'- oligoadenylate synthetase (OAS) proteins. Comput Biol Chem. 2020;85:107211doi: 10.1016/j.compbiolchem.2020.107211.
Gonzalez, K. J., Moncada-Giraldo, D. M., & Gutierrez, J. B. (2020). In silico identification of potential inhibitors against human 2'-5'- oligoadenylate synthetase (OAS) proteins. Computational biology and chemistry, 85107211. https://doi.org/10.1016/j.compbiolchem.2020.107211
Gonzalez, Karen J, et al. "In silico identification of potential inhibitors against human 2'-5'- oligoadenylate synthetase (OAS) proteins." Computational biology and chemistry vol. 85 (2020): 107211. doi: https://doi.org/10.1016/j.compbiolchem.2020.107211
Gonzalez KJ, Moncada-Giraldo DM, Gutierrez JB. In silico identification of potential inhibitors against human 2'-5'- oligoadenylate synthetase (OAS) proteins. Comput Biol Chem. 2020 Apr;85:107211. doi: 10.1016/j.compbiolchem.2020.107211. Epub 2020 Jan 22. PMID: 32004971.
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Structure-based drug design.

Current opinion in structural biology

Colman PM.
PMID: 7712290
Curr Opin Struct Biol. 1994 Dec;4(6):868-74. doi: 10.1016/0959-440x(94)90268-2.

There are now many successful examples of the design of new ligands based on knowledge of target protein structures. In most cases those ligands are unsuitable as drugs because of problems of toxicity, stability or bioavailability. The past twelve...

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Colman PM. Structure-based drug design. Curr Opin Struct Biol. 1994;4(6):868-74doi: 10.1016/0959-440x(94)90268-2.
Colman, P. M. (1994). Structure-based drug design. Current opinion in structural biology, 4(6), 868-74. https://doi.org/10.1016/0959-440x(94)90268-2
Colman, P M. "Structure-based drug design." Current opinion in structural biology vol. 4,6 (1994): 868-74. doi: https://doi.org/10.1016/0959-440x(94)90268-2
Colman PM. Structure-based drug design. Curr Opin Struct Biol. 1994 Dec;4(6):868-74. doi: 10.1016/0959-440x(94)90268-2. PMID: 7712290.
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Anti-CRISPR AcrIIA5 Potently Inhibits All Cas9 Homologs Used for Genome Editing.

Cell reports

Garcia B, Lee J, Edraki A, Hidalgo-Reyes Y, Erwood S, Mir A, Trost CN, Seroussi U, Stanley SY, Cohn RD, Claycomb JM, Sontheimer EJ, Maxwell KL, Davidson AR.
PMID: 31722192
Cell Rep. 2019 Nov 12;29(7):1739-1746.e5. doi: 10.1016/j.celrep.2019.10.017.

CRISPR-Cas9 systems provide powerful tools for genome editing. However, optimal employment of this technology will require control of Cas9 activity so that the timing, tissue specificity, and accuracy of editing may be precisely modulated. Anti-CRISPR proteins, which are small,...

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Garcia B, Lee J, Edraki A, et al. Anti-CRISPR AcrIIA5 Potently Inhibits All Cas9 Homologs Used for Genome Editing. Cell Rep. 2019;29(7):1739-1746.e5doi: 10.1016/j.celrep.2019.10.017.
Garcia, B., Lee, J., Edraki, A., Hidalgo-Reyes, Y., Erwood, S., Mir, A., Trost, C. N., Seroussi, U., Stanley, S. Y., Cohn, R. D., Claycomb, J. M., Sontheimer, E. J., Maxwell, K. L., & Davidson, A. R. (2019). Anti-CRISPR AcrIIA5 Potently Inhibits All Cas9 Homologs Used for Genome Editing. Cell reports, 29(7), 1739-1746.e5. https://doi.org/10.1016/j.celrep.2019.10.017
Garcia, Bianca, et al. "Anti-CRISPR AcrIIA5 Potently Inhibits All Cas9 Homologs Used for Genome Editing." Cell reports vol. 29,7 (2019): 1739-1746.e5. doi: https://doi.org/10.1016/j.celrep.2019.10.017
Garcia B, Lee J, Edraki A, Hidalgo-Reyes Y, Erwood S, Mir A, Trost CN, Seroussi U, Stanley SY, Cohn RD, Claycomb JM, Sontheimer EJ, Maxwell KL, Davidson AR. Anti-CRISPR AcrIIA5 Potently Inhibits All Cas9 Homologs Used for Genome Editing. Cell Rep. 2019 Nov 12;29(7):1739-1746.e5. doi: 10.1016/j.celrep.2019.10.017. PMID: 31722192; PMCID: PMC6910239.
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Development of 11beta-HSD1 inhibitors for the treatment of type 2 diabetes.

Mini reviews in medicinal chemistry

Hale C, Wang M.
PMID: 18537725
Mini Rev Med Chem. 2008 Jun;8(7):702-10. doi: 10.2174/138955708784567421.

Glucocorticoid action is linked to the development of obesity and insulin resistance. Inhibition of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) has been proposed as a strategy to suppress glucocorticoid action in a tissue-specific manner. A large variety of 11beta-HSD1 inhibitor...

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Hale C, Wang M. Development of 11beta-HSD1 inhibitors for the treatment of type 2 diabetes. Mini Rev Med Chem. 2008;8(7):702-10doi: 10.2174/138955708784567421.
Hale, C., & Wang, M. (2008). Development of 11beta-HSD1 inhibitors for the treatment of type 2 diabetes. Mini reviews in medicinal chemistry, 8(7), 702-10. https://doi.org/10.2174/138955708784567421
Hale, Clarence, and Wang, Minghan. "Development of 11beta-HSD1 inhibitors for the treatment of type 2 diabetes." Mini reviews in medicinal chemistry vol. 8,7 (2008): 702-10. doi: https://doi.org/10.2174/138955708784567421
Hale C, Wang M. Development of 11beta-HSD1 inhibitors for the treatment of type 2 diabetes. Mini Rev Med Chem. 2008 Jun;8(7):702-10. doi: 10.2174/138955708784567421. PMID: 18537725.
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