Transition state analog (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Transition state analog" in English language version.

refsWebsite

Global rank English rank

15nih.gov

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11doi.org

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1archive.org

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1harvard.edu

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archive.org

Silverman RB (2004). The Organic Chemistry of Drug Design and Drug Action. San Diego, CA: Elsevier Academic Press. ISBN 0-12-643732-7.

doi.org

Davis JP, Cain GA, Pitts WJ, Magolda RL, Copeland RA (January 1996). "The immunosuppressive metabolite of leflunomide is a potent inhibitor of human dihydroorotate dehydrogenase". Biochemistry. 35 (4): 1270–1273. doi:10.1021/bi952168g. PMID 8573583.
Schramm VL (2011). "Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes". Annual Review of Biochemistry. 80 (1): 703–732. doi:10.1146/annurev-biochem-061809-100742. PMC 5502542. PMID 21675920.
Kollman P, Kuhn B, Peräkylä M (2002). "Computational Studies of Enzyme-Catalyzed Reactions: Where Are We in Predicting Mechanisms and in Understanding the Nature of Enzyme Catalysis?". J. Phys. Chem. B. 106 (7): 1537–1542. doi:10.1021/jp012017p.
Hou G, Cui Q (January 2012). "QM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP superfamily". Journal of the American Chemical Society. 134 (1): 229–246. doi:10.1021/ja205226d. PMC 3257412. PMID 22097879.
Saen-Oon S, Quaytman-Machleder S, Schramm VL, Schwartz SD (October 2008). "Atomic detail of chemical transformation at the transition state of an enzymatic reaction". Proceedings of the National Academy of Sciences of the United States of America. 105 (43): 16543–16548. Bibcode:2008PNAS..10516543S. doi:10.1073/pnas.0808413105. PMC 2575456. PMID 18946041.
Singh V, Lee JE, Núñez S, Howell PL, Schramm VL (September 2005). "Transition state structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues". Biochemistry. 44 (35): 11647–11659. doi:10.1021/bi050863a. PMID 16128565.
Gutierrez JA, Luo M, Singh V, Li L, Brown RL, Norris GE, et al. (November 2007). "Picomolar inhibitors as transition-state probes of 5'-methylthioadenosine nucleosidases". ACS Chemical Biology. 2 (11): 725–734. doi:10.1021/cb700166z. PMID 18030989.
Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW (December 1987). "Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues". Biochemistry. 26 (26): 8542–8553. doi:10.1021/bi00400a008. PMID 3442675.
Maarsingh H, Zaagsma J, Meurs H (October 2009). "Arginase: a key enzyme in the pathophysiology of allergic asthma opening novel therapeutic perspectives". British Journal of Pharmacology. 158 (3): 652–664. doi:10.1111/j.1476-5381.2009.00374.x. PMC 2765587. PMID 19703164.
Cama E, Shin H, Christianson DW (October 2003). "Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase". Journal of the American Chemical Society. 125 (43): 13052–13057. doi:10.1021/ja036365b. PMID 14570477.
Shishova EY, Di Costanzo L, Emig FA, Ash DE, Christianson DW (January 2009). "Probing the specificity determinants of amino acid recognition by arginase". Biochemistry. 48 (1): 121–131. doi:10.1021/bi801911v. PMC 2665027. PMID 19093830.

harvard.edu

ui.adsabs.harvard.edu

Saen-Oon S, Quaytman-Machleder S, Schramm VL, Schwartz SD (October 2008). "Atomic detail of chemical transformation at the transition state of an enzymatic reaction". Proceedings of the National Academy of Sciences of the United States of America. 105 (43): 16543–16548. Bibcode:2008PNAS..10516543S. doi:10.1073/pnas.0808413105. PMC 2575456. PMID 18946041.

nih.gov

pubmed.ncbi.nlm.nih.gov

Davis JP, Cain GA, Pitts WJ, Magolda RL, Copeland RA (January 1996). "The immunosuppressive metabolite of leflunomide is a potent inhibitor of human dihydroorotate dehydrogenase". Biochemistry. 35 (4): 1270–1273. doi:10.1021/bi952168g. PMID 8573583.
Schramm VL (2011). "Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes". Annual Review of Biochemistry. 80 (1): 703–732. doi:10.1146/annurev-biochem-061809-100742. PMC 5502542. PMID 21675920.
Hou G, Cui Q (January 2012). "QM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP superfamily". Journal of the American Chemical Society. 134 (1): 229–246. doi:10.1021/ja205226d. PMC 3257412. PMID 22097879.
Saen-Oon S, Quaytman-Machleder S, Schramm VL, Schwartz SD (October 2008). "Atomic detail of chemical transformation at the transition state of an enzymatic reaction". Proceedings of the National Academy of Sciences of the United States of America. 105 (43): 16543–16548. Bibcode:2008PNAS..10516543S. doi:10.1073/pnas.0808413105. PMC 2575456. PMID 18946041.
Singh V, Lee JE, Núñez S, Howell PL, Schramm VL (September 2005). "Transition state structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues". Biochemistry. 44 (35): 11647–11659. doi:10.1021/bi050863a. PMID 16128565.
Gutierrez JA, Luo M, Singh V, Li L, Brown RL, Norris GE, et al. (November 2007). "Picomolar inhibitors as transition-state probes of 5'-methylthioadenosine nucleosidases". ACS Chemical Biology. 2 (11): 725–734. doi:10.1021/cb700166z. PMID 18030989.
Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW (December 1987). "Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues". Biochemistry. 26 (26): 8542–8553. doi:10.1021/bi00400a008. PMID 3442675.
Maarsingh H, Zaagsma J, Meurs H (October 2009). "Arginase: a key enzyme in the pathophysiology of allergic asthma opening novel therapeutic perspectives". British Journal of Pharmacology. 158 (3): 652–664. doi:10.1111/j.1476-5381.2009.00374.x. PMC 2765587. PMID 19703164.
Cama E, Shin H, Christianson DW (October 2003). "Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase". Journal of the American Chemical Society. 125 (43): 13052–13057. doi:10.1021/ja036365b. PMID 14570477.
Shishova EY, Di Costanzo L, Emig FA, Ash DE, Christianson DW (January 2009). "Probing the specificity determinants of amino acid recognition by arginase". Biochemistry. 48 (1): 121–131. doi:10.1021/bi801911v. PMC 2665027. PMID 19093830.

ncbi.nlm.nih.gov

Schramm VL (2011). "Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes". Annual Review of Biochemistry. 80 (1): 703–732. doi:10.1146/annurev-biochem-061809-100742. PMC 5502542. PMID 21675920.
Hou G, Cui Q (January 2012). "QM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP superfamily". Journal of the American Chemical Society. 134 (1): 229–246. doi:10.1021/ja205226d. PMC 3257412. PMID 22097879.
Saen-Oon S, Quaytman-Machleder S, Schramm VL, Schwartz SD (October 2008). "Atomic detail of chemical transformation at the transition state of an enzymatic reaction". Proceedings of the National Academy of Sciences of the United States of America. 105 (43): 16543–16548. Bibcode:2008PNAS..10516543S. doi:10.1073/pnas.0808413105. PMC 2575456. PMID 18946041.
Maarsingh H, Zaagsma J, Meurs H (October 2009). "Arginase: a key enzyme in the pathophysiology of allergic asthma opening novel therapeutic perspectives". British Journal of Pharmacology. 158 (3): 652–664. doi:10.1111/j.1476-5381.2009.00374.x. PMC 2765587. PMID 19703164.
Shishova EY, Di Costanzo L, Emig FA, Ash DE, Christianson DW (January 2009). "Probing the specificity determinants of amino acid recognition by arginase". Biochemistry. 48 (1): 121–131. doi:10.1021/bi801911v. PMC 2665027. PMID 19093830.