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1
The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition
The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition
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The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition

Gill, Harindarpal S ; Eisenberg, David

Biochemistry (Easton), 2001-02, Vol.40 (7), p.1903-1912 [Periódico revisado por pares]

United States: American Chemical Society

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2
Crystal Structure of Diphtheria Toxin Bound to Nicotinamide Adenine Dinucleotide
Crystal Structure of Diphtheria Toxin Bound to Nicotinamide Adenine Dinucleotide
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Crystal Structure of Diphtheria Toxin Bound to Nicotinamide Adenine Dinucleotide

Bell, Charles E ; Eisenberg, David

Biochemistry (Easton), 1996-01, Vol.35 (4), p.1137-1149 [Periódico revisado por pares]

United States: American Chemical Society

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3
Characterization of High-Order Diphtheria Toxin Oligomers
Characterization of High-Order Diphtheria Toxin Oligomers
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Characterization of High-Order Diphtheria Toxin Oligomers

Steere, Boyd ; Eisenberg, David

Biochemistry (Easton), 2000-12, Vol.39 (51), p.15901-15909 [Periódico revisado por pares]

United States: American Chemical Society

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4
3D Structure and Significance of the GΦXXG Helix Packing Motif in Tetramers of the E1β Subunit of Pyruvate Dehydrogenase from the Archeon Pyrobaculum aerophilum
3D Structure and Significance of the GΦXXG Helix Packing Motif in Tetramers of the E1β Subunit of Pyruvate Dehydrogenase from the Archeon Pyrobaculum aerophilum
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3D Structure and Significance of the GΦXXG Helix Packing Motif in Tetramers of the E1β Subunit of Pyruvate Dehydrogenase from the Archeon Pyrobaculum aerophilum

Kleiger, Gary ; Perry, Jeanne ; Eisenberg, David

Biochemistry (Easton), 2001-12, Vol.40 (48), p.14484-14492 [Periódico revisado por pares]

American Chemical Society

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5
GXXXG and AXXXA:  Common α-Helical Interaction Motifs in Proteins, Particularly in Extremophiles
GXXXG and AXXXA:  Common α-Helical Interaction Motifs in Proteins, Particularly in Extremophiles
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GXXXG and AXXXA:  Common α-Helical Interaction Motifs in Proteins, Particularly in Extremophiles

Kleiger, Gary ; Grothe, Robert ; Mallick, Parag ; Eisenberg, David

Biochemistry (Easton), 2002-05, Vol.41 (19), p.5990-5997 [Periódico revisado por pares]

United States: American Chemical Society

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6
Crystal Structure of the Pantothenate Synthetase from Mycobacterium tuberculosis, Snapshots of the Enzyme in Action
Crystal Structure of the Pantothenate Synthetase from Mycobacterium tuberculosis, Snapshots of the Enzyme in Action
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Crystal Structure of the Pantothenate Synthetase from Mycobacterium tuberculosis, Snapshots of the Enzyme in Action

Wang, Shuishu ; Eisenberg, David

Biochemistry (Easton), 2006-02, Vol.45 (6), p.1554-1561 [Periódico revisado por pares]

United States: American Chemical Society

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7
A Structure-Based Mechanism for Copper−Zinc Superoxide Dismutase
A Structure-Based Mechanism for Copper−Zinc Superoxide Dismutase
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A Structure-Based Mechanism for Copper−Zinc Superoxide Dismutase

Hart, P. John ; Balbirnie, Melinda M ; Ogihara, Nancy L ; Nersissian, Aram M ; Weiss, Manfred S ; Valentine, Joan Selverstone ; Eisenberg, David

Biochemistry (Easton), 1999-02, Vol.38 (7), p.2167-2178 [Periódico revisado por pares]

United States: American Chemical Society

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8
Multicopy Crystallographic Refinement of a Relaxed Glutamine Synthetase from Mycobacterium tuberculosis Highlights Flexible Loops in the Enzymatic Mechanism and Its Regulation
Multicopy Crystallographic Refinement of a Relaxed Glutamine Synthetase from Mycobacterium tuberculosis Highlights Flexible Loops in the Enzymatic Mechanism and Its Regulation
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Multicopy Crystallographic Refinement of a Relaxed Glutamine Synthetase from Mycobacterium tuberculosis Highlights Flexible Loops in the Enzymatic Mechanism and Its Regulation

Gill, Harindarpal S ; Pfluegl, Gaston M. U ; Eisenberg, David

Biochemistry (Easton), 2002-08, Vol.41 (31), p.9863-9872 [Periódico revisado por pares]

United States: American Chemical Society

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9
Heregulin Reverses the Oligomerization of HER3
Heregulin Reverses the Oligomerization of HER3
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Heregulin Reverses the Oligomerization of HER3

Landgraf, Ralf ; Eisenberg, David

Biochemistry (Easton), 2000-07, Vol.39 (29), p.8503-8511 [Periódico revisado por pares]

United States: American Chemical Society

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10
Thiol−Disulfide Exchange in an Immunoglobulin-like Fold:  Structure of the N-Terminal Domain of DsbD
Thiol−Disulfide Exchange in an Immunoglobulin-like Fold:  Structure of the N-Terminal Domain of DsbD
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Thiol−Disulfide Exchange in an Immunoglobulin-like Fold:  Structure of the N-Terminal Domain of DsbD

Goulding, Celia W ; Sawaya, Michael R ; Parseghian, Angineh ; Lim, Vincent ; Eisenberg, David ; Missiakas, Dominique

Biochemistry (Easton), 2002-06, Vol.41 (22), p.6920-6927 [Periódico revisado por pares]

United States: American Chemical Society

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