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Andrew Brunskill

Showing results (1-10 of 16) with videos related to

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AAPS Pharmscitech|February 23, 2024
Using Dry Dispersion Laser Diffraction to Assess Dispersibility in Spheronized Agglomerate FormulationsFaustin Arevalo, Steven Tignor, Andrew Brunskill, et al.
Pharmaceutical Research|December 1, 2023
Impact of Processing Methods on the Physico-chemical Properties of Posaconazole Amorphous Solid DispersionsRu He, Matthew S Lamm, Andrew Brunskill, et al.
Artificial Intelligence in Medicine|October 1, 2011
Incorporating expert knowledge when learning Bayesian network structure: a medical case studyM Julia Flores, Ann E Nicholson, Andrew Brunskill, et al.
The Journal of Organic Chemistry|December 15, 2015
Promotion of a Ti-Mediated Mannich Reaction by a Proton SourceJohn Limanto, Naoki Yoshikawa, Robert A Reamer, et al.
Biochemistry|March 3, 2004
Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphatePalaniappa Arjunan, Krishnamoorthy Chandrasekhar, Martin Sax, et al.
Organic Letters|April 29, 2016
The Discovery of Quinoxaline-Based Metathesis Catalysts from Synthesis of Grazoprevir (MK-5172)Michael J Williams, Jongrock Kong, Cheol K Chung, et al.
The Journal of Biological Chemistry|March 15, 2006
A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adductPalaniappa Arjunan, Martin Sax, Andrew Brunskill, et al.
Biochemistry|December 27, 2002
Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolaseNatalia Nemeria, Palaniappa Arjunan, Andrew Brunskill, et al.
Biochemistry|April 17, 2002
Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolutionPalaniappa Arjunan, Natalia Nemeria, Andrew Brunskill, et al.
Organic Letters|May 24, 2019
<sup>13</sup>C NMR-Based Approaches for Solving Challenging Stereochemical ProblemsIkenna E Ndukwe, Andrew Brunskill, Donald R Gauthier, et al.
Pageof 2

Showing results (1-10 of 16) with videos related to

Sort By:
Pageof 2
AAPS Pharmscitech|February 23, 2024
Using Dry Dispersion Laser Diffraction to Assess Dispersibility in Spheronized Agglomerate FormulationsFaustin Arevalo, Steven Tignor, Andrew Brunskill, et al.
Pharmaceutical Research|December 1, 2023
Impact of Processing Methods on the Physico-chemical Properties of Posaconazole Amorphous Solid DispersionsRu He, Matthew S Lamm, Andrew Brunskill, et al.
Artificial Intelligence in Medicine|October 1, 2011
Incorporating expert knowledge when learning Bayesian network structure: a medical case studyM Julia Flores, Ann E Nicholson, Andrew Brunskill, et al.
The Journal of Organic Chemistry|December 15, 2015
Promotion of a Ti-Mediated Mannich Reaction by a Proton SourceJohn Limanto, Naoki Yoshikawa, Robert A Reamer, et al.
Biochemistry|March 3, 2004
Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphatePalaniappa Arjunan, Krishnamoorthy Chandrasekhar, Martin Sax, et al.
Organic Letters|April 29, 2016
The Discovery of Quinoxaline-Based Metathesis Catalysts from Synthesis of Grazoprevir (MK-5172)Michael J Williams, Jongrock Kong, Cheol K Chung, et al.
The Journal of Biological Chemistry|March 15, 2006
A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adductPalaniappa Arjunan, Martin Sax, Andrew Brunskill, et al.
Biochemistry|December 27, 2002
Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolaseNatalia Nemeria, Palaniappa Arjunan, Andrew Brunskill, et al.
Biochemistry|April 17, 2002
Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolutionPalaniappa Arjunan, Natalia Nemeria, Andrew Brunskill, et al.
Organic Letters|May 24, 2019
<sup>13</sup>C NMR-Based Approaches for Solving Challenging Stereochemical ProblemsIkenna E Ndukwe, Andrew Brunskill, Donald R Gauthier, et al.
Pageof 2