Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 1342 entries
Sorted by: Best Match Show Resources per page
A Structure-Activity Relationship for the Hydrolysis of Acetylamino Acids by Porcine Aminoacylase.

Bioorganic chemistry

Denton P.
PMID: 11034782
Bioorg Chem. 2000 Aug;28(4):205-213. doi: 10.1006/bioo.2000.1177.

A structure-activity relationship is presented that satisfactorily predicts the rates of hydrolysis of a series of acetylglycine derivatives by porcine aminoacylase. It is apparent that the substrate specificity of aminoacylase is mainly kinetic in origin, the observed correlation with...

Cite
Denton P. A Structure-Activity Relationship for the Hydrolysis of Acetylamino Acids by Porcine Aminoacylase. Bioorg Chem. 2000;28(4):205-213doi: 10.1006/bioo.2000.1177.
Denton, P. (2000). A Structure-Activity Relationship for the Hydrolysis of Acetylamino Acids by Porcine Aminoacylase. Bioorganic chemistry, 28(4), 205-213. https://doi.org/10.1006/bioo.2000.1177
Denton. "A Structure-Activity Relationship for the Hydrolysis of Acetylamino Acids by Porcine Aminoacylase." Bioorganic chemistry vol. 28,4 (2000): 205-213. doi: https://doi.org/10.1006/bioo.2000.1177
Denton P. A Structure-Activity Relationship for the Hydrolysis of Acetylamino Acids by Porcine Aminoacylase. Bioorg Chem. 2000 Aug;28(4):205-213. doi: 10.1006/bioo.2000.1177. PMID: 11034782.
Copy Download .nbib Format: NLM
Evidence for a 1,2 Shift of a Hydrogen Atom in a Radical Intermediate of the Methylmalonyl-CoA Mutase Reaction.

Bioorganic chemistry

Kunz M, Rétey J.
PMID: 10915551
Bioorg Chem. 2000 Jun;28(3):134-139. doi: 10.1006/bioo.2000.1165.

An excellent substrate of methylmalonyl-CoA mutase, methylmalonyl-carba-(dethia) coenzyme A (methylmalonyl-CH(2)-CoA), was synthesized by a chemoenzymatic method and its alpha-proton was exchanged with deuterium by long-term incubation in deuterium oxide at pH 6.9. After addition of highly purified epimerase-free methylmalonyl-CoA...

Cite
Kunz M, Rétey J. Evidence for a 1,2 Shift of a Hydrogen Atom in a Radical Intermediate of the Methylmalonyl-CoA Mutase Reaction. Bioorg Chem. 2000;28(3):134-139doi: 10.1006/bioo.2000.1165.
Kunz, M., & Rétey, J. (2000). Evidence for a 1,2 Shift of a Hydrogen Atom in a Radical Intermediate of the Methylmalonyl-CoA Mutase Reaction. Bioorganic chemistry, 28(3), 134-139. https://doi.org/10.1006/bioo.2000.1165
Kunz, and Rétey. "Evidence for a 1,2 Shift of a Hydrogen Atom in a Radical Intermediate of the Methylmalonyl-CoA Mutase Reaction." Bioorganic chemistry vol. 28,3 (2000): 134-139. doi: https://doi.org/10.1006/bioo.2000.1165
Kunz M, Rétey J. Evidence for a 1,2 Shift of a Hydrogen Atom in a Radical Intermediate of the Methylmalonyl-CoA Mutase Reaction. Bioorg Chem. 2000 Jun;28(3):134-139. doi: 10.1006/bioo.2000.1165. PMID: 10915551.
Copy Download .nbib Format: NLM
Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors.

Bioorganic chemistry

Maurer K, Tang AH, Kenyon GL, Leavitt AD.
PMID: 10915552
Bioorg Chem. 2000 Jun;28(3):140-155. doi: 10.1006/bioo.2000.1166.

Integration of a DNA copy of the HIV-1 genome is required for viral replication and pathogenicity, and this highly specific molecular process is mediated by the virus-encoded integrase protein. The requirement for integration, combined with the lack of a...

Cite
Maurer K, Tang AH, Kenyon GL, et al. Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors. Bioorg Chem. 2000;28(3):140-155doi: 10.1006/bioo.2000.1166.
Maurer, K., Tang, A. H., Kenyon, G. L., & Leavitt, A. D. (2000). Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors. Bioorganic chemistry, 28(3), 140-155. https://doi.org/10.1006/bioo.2000.1166
Maurer, et al. "Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors." Bioorganic chemistry vol. 28,3 (2000): 140-155. doi: https://doi.org/10.1006/bioo.2000.1166
Maurer K, Tang AH, Kenyon GL, Leavitt AD. Carbonyl J Derivatives: A New Class of HIV-1 Integrase Inhibitors. Bioorg Chem. 2000 Jun;28(3):140-155. doi: 10.1006/bioo.2000.1166. PMID: 10915552.
Copy Download .nbib Format: NLM
Different Activities of 5-Hydroxy-dUMP and 5-Hydroxymethyl-dUMP in Thymidylate Synthase-Catalyzed Reaction in View of Molecular Modeling and Structural Studies.

Bioorganic chemistry

Jarmula A, Leś A, Rode W.
PMID: 10915553
Bioorg Chem. 2000 Jun;28(3):156-162. doi: 10.1006/bioo.2000.1172.

In order to explain different activities shown by 5-hydroxy-dUMP (substrate) and its close analogue 5-hydroxymethyl-dUMP (slow-binding inhibitor) in the reaction catalyzed by thymidylate synthase, studies have been undertaken involving (i) ab initio RHF simulations, (ii) comparative analysis of crystallographic...

Cite
Jarmula A, Leś A, Rode W. Different Activities of 5-Hydroxy-dUMP and 5-Hydroxymethyl-dUMP in Thymidylate Synthase-Catalyzed Reaction in View of Molecular Modeling and Structural Studies. Bioorg Chem. 2000;28(3):156-162doi: 10.1006/bioo.2000.1172.
Jarmula, A., Leś, A., & Rode, W. (2000). Different Activities of 5-Hydroxy-dUMP and 5-Hydroxymethyl-dUMP in Thymidylate Synthase-Catalyzed Reaction in View of Molecular Modeling and Structural Studies. Bioorganic chemistry, 28(3), 156-162. https://doi.org/10.1006/bioo.2000.1172
Jarmula, et al. "Different Activities of 5-Hydroxy-dUMP and 5-Hydroxymethyl-dUMP in Thymidylate Synthase-Catalyzed Reaction in View of Molecular Modeling and Structural Studies." Bioorganic chemistry vol. 28,3 (2000): 156-162. doi: https://doi.org/10.1006/bioo.2000.1172
Jarmula A, Leś A, Rode W. Different Activities of 5-Hydroxy-dUMP and 5-Hydroxymethyl-dUMP in Thymidylate Synthase-Catalyzed Reaction in View of Molecular Modeling and Structural Studies. Bioorg Chem. 2000 Jun;28(3):156-162. doi: 10.1006/bioo.2000.1172. PMID: 10915553.
Copy Download .nbib Format: NLM
Introduction.

Bioorganic chemistry

Benkovic SJ, Kenyon GL.
PMID: 11352468
Bioorg Chem. 2000 Dec;28(6):315. doi: 10.1006/bioo.2001.1198.

No abstract available.

Cite
Benkovic SJ, Kenyon GL. Introduction. Bioorg Chem. 2000;28(6):315doi: 10.1006/bioo.2001.1198.
Benkovic, S. J., & Kenyon, G. L. (2000). Introduction. Bioorganic chemistry, 28(6), 315. https://doi.org/10.1006/bioo.2001.1198
Benkovic, S J, and Kenyon, G L. "Introduction." Bioorganic chemistry vol. 28,6 (2000): 315. doi: https://doi.org/10.1006/bioo.2001.1198
Benkovic SJ, Kenyon GL. Introduction. Bioorg Chem. 2000 Dec;28(6):315. doi: 10.1006/bioo.2001.1198. PMID: 11352468.
Copy Download .nbib Format: NLM
The Unexpected Catalytic Properties of a Heterodimer of GAR Transformylase.

Bioorganic chemistry

Liu C, Shim JH, Benkovic SJ.
PMID: 11352469
Bioorg Chem. 2000 Dec;28(6):316-23. doi: 10.1006/bioo.2000.1186.

We have developed an efficient expression and purification protocol for a heterodimer of glycinamide ribonucleotide transformylase that was identified in incremental truncation libraries, a general combinatorial method for protein fragment complementation (M. Ostermeier, A. E. Nixon, J. H. Shim,...

Cite
Liu C, Shim JH, Benkovic SJ. The Unexpected Catalytic Properties of a Heterodimer of GAR Transformylase. Bioorg Chem. 2000;28(6):316-23doi: 10.1006/bioo.2000.1186.
Liu, C., Shim, J. H., & Benkovic, S. J. (2000). The Unexpected Catalytic Properties of a Heterodimer of GAR Transformylase. Bioorganic chemistry, 28(6), 316-23. https://doi.org/10.1006/bioo.2000.1186
Liu, C, et al. "The Unexpected Catalytic Properties of a Heterodimer of GAR Transformylase." Bioorganic chemistry vol. 28,6 (2000): 316-23. doi: https://doi.org/10.1006/bioo.2000.1186
Liu C, Shim JH, Benkovic SJ. The Unexpected Catalytic Properties of a Heterodimer of GAR Transformylase. Bioorg Chem. 2000 Dec;28(6):316-23. doi: 10.1006/bioo.2000.1186. PMID: 11352469.
Copy Download .nbib Format: NLM
Rational design of pyrrolo.

Bioorganic chemistry

Huang X, Suleman A, Skibo EB.
PMID: 11352470
Bioorg Chem. 2000 Dec;28(6):324-37. doi: 10.1006/bioo.2000.1183.

Models have been developed for the interaction of the pyrrolo[1,2-a]benzimidazole (PBI) antitumor agents with the two-electron activating enzyme DT-diaphorase and the DNA major groove. The DT-diaphorase model and experimental results indicate that the S-enantiomer of 3-carbamido PBI can enantioselect...

Cite
Huang X, Suleman A, Skibo EB. Rational design of pyrrolo. Bioorg Chem. 2000;28(6):324-37doi: 10.1006/bioo.2000.1183.
Huang, X., Suleman, A., & Skibo, E. B. (2000). Rational design of pyrrolo. Bioorganic chemistry, 28(6), 324-37. https://doi.org/10.1006/bioo.2000.1183
Huang, X, et al. "Rational design of pyrrolo." Bioorganic chemistry vol. 28,6 (2000): 324-37. doi: https://doi.org/10.1006/bioo.2000.1183
Huang X, Suleman A, Skibo EB. Rational design of pyrrolo. Bioorg Chem. 2000 Dec;28(6):324-37. doi: 10.1006/bioo.2000.1183. PMID: 11352470.
Copy Download .nbib Format: NLM
Analysis of claims of enhanced enzyme catalysis by inorganic colloidosomes.

Bioorganic chemistry

Kluger R.
PMID: 23886373
Bioorg Chem. 2013 Aug;49:59-60. doi: 10.1016/j.bioorg.2013.06.004. Epub 2013 Jun 20.

Ester hydrolysis reactions in the presence of enzymes have been reported to occur within inorganic colloidsomes that contain water in organic solvents. Analysis of reported data plots that were used to obtain values for Km and Vmax that led...

Cite
Kluger R. Analysis of claims of enhanced enzyme catalysis by inorganic colloidosomes. Bioorg Chem. 2013;49:59-60doi: 10.1016/j.bioorg.2013.06.004.
Kluger, R. (2013). Analysis of claims of enhanced enzyme catalysis by inorganic colloidosomes. Bioorganic chemistry, 4959-60. https://doi.org/10.1016/j.bioorg.2013.06.004
Kluger, Ronald. "Analysis of claims of enhanced enzyme catalysis by inorganic colloidosomes." Bioorganic chemistry vol. 49 (2013): 59-60. doi: https://doi.org/10.1016/j.bioorg.2013.06.004
Kluger R. Analysis of claims of enhanced enzyme catalysis by inorganic colloidosomes. Bioorg Chem. 2013 Aug;49:59-60. doi: 10.1016/j.bioorg.2013.06.004. Epub 2013 Jun 20. PMID: 23886373.
Copy Download .nbib Format: NLM
Discovery of the PARP (poly ADP-ribose polymerase) inhibitor 2-(1-(4,4-difluorocyclohexyl)piperidin-4-yl)-1H-benzo[d]imidazole-4-carboxamide for the treatment of cancer.

Bioorganic chemistry

Tang L, Wu W, Zhang C, Shi Z, Chen D, Zhai X, Jiang Y.
PMID: 34186467
Bioorg Chem. 2021 Sep;114:105026. doi: 10.1016/j.bioorg.2021.105026. Epub 2021 May 26.

In this work, two series of cyclic amine-containing benzimidazole carboxamide derivatives were designed and synthesized as potent anticancer agents. PARP1/2 inhibitory activity assays indicated that most of the compounds showed significant activity. The in vitro antiproliferative activity of these...

Cite
Tang L, Wu W, Zhang C, et al. Discovery of the PARP (poly ADP-ribose polymerase) inhibitor 2-(1-(4,4-difluorocyclohexyl)piperidin-4-yl)-1H-benzo[d]imidazole-4-carboxamide for the treatment of cancer. Bioorg Chem. 2021;114:105026doi: 10.1016/j.bioorg.2021.105026.
Tang, L., Wu, W., Zhang, C., Shi, Z., Chen, D., Zhai, X., & Jiang, Y. (2021). Discovery of the PARP (poly ADP-ribose polymerase) inhibitor 2-(1-(4,4-difluorocyclohexyl)piperidin-4-yl)-1H-benzo[d]imidazole-4-carboxamide for the treatment of cancer. Bioorganic chemistry, 114105026. https://doi.org/10.1016/j.bioorg.2021.105026
Tang, Lin, et al. "Discovery of the PARP (poly ADP-ribose polymerase) inhibitor 2-(1-(4,4-difluorocyclohexyl)piperidin-4-yl)-1H-benzo[d]imidazole-4-carboxamide for the treatment of cancer." Bioorganic chemistry vol. 114 (2021): 105026. doi: https://doi.org/10.1016/j.bioorg.2021.105026
Tang L, Wu W, Zhang C, Shi Z, Chen D, Zhai X, Jiang Y. Discovery of the PARP (poly ADP-ribose polymerase) inhibitor 2-(1-(4,4-difluorocyclohexyl)piperidin-4-yl)-1H-benzo[d]imidazole-4-carboxamide for the treatment of cancer. Bioorg Chem. 2021 Sep;114:105026. doi: 10.1016/j.bioorg.2021.105026. Epub 2021 May 26. PMID: 34186467.
Copy Download .nbib Format: NLM
Computational studies and sever apoptotic bioactivity of new heterocyclic cyanoacrylamide based p-fluorophenyl and p-phenolic compounds against liver carcinoma (Hepg2).

Bioorganic chemistry

Mohamed MF, Saddiq AA, Al-Shaikh TM, Ibrahim NS, Abdelhamid IA.
PMID: 34246114
Bioorg Chem. 2021 Sep;114:105147. doi: 10.1016/j.bioorg.2021.105147. Epub 2021 Jul 05.

An efficient route for the preparation of new heterocyclic cyanoacrylamides based p-fluorophenyl and p-phenolic compounds was depicted. All structures were confirmed based on the different spectral tools and elemental analyses. MTT assay for the novel synthesized series was performed...

Cite
Mohamed MF, Saddiq AA, Al-Shaikh TM, et al. Computational studies and sever apoptotic bioactivity of new heterocyclic cyanoacrylamide based p-fluorophenyl and p-phenolic compounds against liver carcinoma (Hepg2). Bioorg Chem. 2021;114:105147doi: 10.1016/j.bioorg.2021.105147.
Mohamed, M. F., Saddiq, A. A., Al-Shaikh, T. M., Ibrahim, N. S., & Abdelhamid, I. A. (2021). Computational studies and sever apoptotic bioactivity of new heterocyclic cyanoacrylamide based p-fluorophenyl and p-phenolic compounds against liver carcinoma (Hepg2). Bioorganic chemistry, 114105147. https://doi.org/10.1016/j.bioorg.2021.105147
Mohamed, Magda F, et al. "Computational studies and sever apoptotic bioactivity of new heterocyclic cyanoacrylamide based p-fluorophenyl and p-phenolic compounds against liver carcinoma (Hepg2)." Bioorganic chemistry vol. 114 (2021): 105147. doi: https://doi.org/10.1016/j.bioorg.2021.105147
Mohamed MF, Saddiq AA, Al-Shaikh TM, Ibrahim NS, Abdelhamid IA. Computational studies and sever apoptotic bioactivity of new heterocyclic cyanoacrylamide based p-fluorophenyl and p-phenolic compounds against liver carcinoma (Hepg2). Bioorg Chem. 2021 Sep;114:105147. doi: 10.1016/j.bioorg.2021.105147. Epub 2021 Jul 05. PMID: 34246114.
Copy Download .nbib Format: NLM
New pyrimidine and pyrazole-based compounds as potential EGFR inhibitors: Synthesis, anticancer, antimicrobial evaluation and computational studies.

Bioorganic chemistry

Othman IMM, Alamshany ZM, Tashkandi NY, Gad-Elkareem MAM, Anwar MM, Nossier ES.
PMID: 34161878
Bioorg Chem. 2021 Sep;114:105078. doi: 10.1016/j.bioorg.2021.105078. Epub 2021 Jun 10.

This study was focused on the synthesis of new pyrimidines 4a,b, 5a,b and pyrazoles 6a, b as ATP mimicking tyrosine kinase inhibitors of the epidermal growth factor receptor (EGFR). The new compounds were assessed as cytotoxic candidates against human...

Cite
Othman IMM, Alamshany ZM, Tashkandi NY, et al. New pyrimidine and pyrazole-based compounds as potential EGFR inhibitors: Synthesis, anticancer, antimicrobial evaluation and computational studies. Bioorg Chem. 2021;114:105078doi: 10.1016/j.bioorg.2021.105078.
Othman, I. M. M., Alamshany, Z. M., Tashkandi, N. Y., Gad-Elkareem, M. A. M., Anwar, M. M., & Nossier, E. S. (2021). New pyrimidine and pyrazole-based compounds as potential EGFR inhibitors: Synthesis, anticancer, antimicrobial evaluation and computational studies. Bioorganic chemistry, 114105078. https://doi.org/10.1016/j.bioorg.2021.105078
Othman, Ismail M M, et al. "New pyrimidine and pyrazole-based compounds as potential EGFR inhibitors: Synthesis, anticancer, antimicrobial evaluation and computational studies." Bioorganic chemistry vol. 114 (2021): 105078. doi: https://doi.org/10.1016/j.bioorg.2021.105078
Othman IMM, Alamshany ZM, Tashkandi NY, Gad-Elkareem MAM, Anwar MM, Nossier ES. New pyrimidine and pyrazole-based compounds as potential EGFR inhibitors: Synthesis, anticancer, antimicrobial evaluation and computational studies. Bioorg Chem. 2021 Sep;114:105078. doi: 10.1016/j.bioorg.2021.105078. Epub 2021 Jun 10. PMID: 34161878.
Copy Download .nbib Format: NLM
Design, synthesis, and biological evaluation of hydroxamic acid-substituted 2,4-diaryl aminopyrimidines as potent EGFRT790M/L858R inhibitors for the treatment of NSCLC.

Bioorganic chemistry

Chen L, Zhang Y, Wang C, Tang Z, Meng Q, Sun H, Qi Y, Ma X, Li L, Li Y, Xu Y.
PMID: 34161879
Bioorg Chem. 2021 Sep;114:105045. doi: 10.1016/j.bioorg.2021.105045. Epub 2021 May 31.

A series of 2,4-diarylaminopyrimidine derivatives bearing hydrophilic hydroxamic acids were designed and synthesized as potent EGFR

Cite
Chen L, Zhang Y, Wang C, et al. Design, synthesis, and biological evaluation of hydroxamic acid-substituted 2,4-diaryl aminopyrimidines as potent EGFRT790M/L858R inhibitors for the treatment of NSCLC. Bioorg Chem. 2021;114:105045doi: 10.1016/j.bioorg.2021.105045.
Chen, L., Zhang, Y., Wang, C., Tang, Z., Meng, Q., Sun, H., Qi, Y., Ma, X., Li, L., Li, Y., & Xu, Y. (2021). Design, synthesis, and biological evaluation of hydroxamic acid-substituted 2,4-diaryl aminopyrimidines as potent EGFRT790M/L858R inhibitors for the treatment of NSCLC. Bioorganic chemistry, 114105045. https://doi.org/10.1016/j.bioorg.2021.105045
Chen, Lixue, et al. "Design, synthesis, and biological evaluation of hydroxamic acid-substituted 2,4-diaryl aminopyrimidines as potent EGFRT790M/L858R inhibitors for the treatment of NSCLC." Bioorganic chemistry vol. 114 (2021): 105045. doi: https://doi.org/10.1016/j.bioorg.2021.105045
Chen L, Zhang Y, Wang C, Tang Z, Meng Q, Sun H, Qi Y, Ma X, Li L, Li Y, Xu Y. Design, synthesis, and biological evaluation of hydroxamic acid-substituted 2,4-diaryl aminopyrimidines as potent EGFRT790M/L858R inhibitors for the treatment of NSCLC. Bioorg Chem. 2021 Sep;114:105045. doi: 10.1016/j.bioorg.2021.105045. Epub 2021 May 31. PMID: 34161879.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 1342 entries