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Thiazolium C(2)-proton exchange: structure-reactivity correlations and the pKa of thiamin C(2)-H revisited
Thiazolium C(2)-proton exchange: structure-reactivity correlations and the pKa of thiamin C(2)-H revisited
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Thiazolium C(2)-proton exchange: structure-reactivity correlations and the pKa of thiamin C(2)-H revisited

Washabaugh, Michael W ; Jencks, William P

Biochemistry (Easton), 1988-07, Vol.27 (14), p.5044-5053 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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2
Role of Binding Energy with Coenzyme A in Catalysis by 3-Oxoacid Coenzyme A Transferase
Role of Binding Energy with Coenzyme A in Catalysis by 3-Oxoacid Coenzyme A Transferase
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Role of Binding Energy with Coenzyme A in Catalysis by 3-Oxoacid Coenzyme A Transferase

Whitty, Adrian ; Fierke, Carol A ; Jencks, William P

Biochemistry (Easton), 1995-09, Vol.34 (37), p.11678-11689 [Periódico revisado por pares]

United States: American Chemical Society

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3
Alkaline Phosphatase Is an Almost Perfect Enzyme
Alkaline Phosphatase Is an Almost Perfect Enzyme
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Alkaline Phosphatase Is an Almost Perfect Enzyme

Simopoulos, Thomas T ; Jencks, William P

Biochemistry (Easton), 1994-08, Vol.33 (34), p.10375-10380 [Periódico revisado por pares]

United States: American Chemical Society

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4
Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH)+ : a possible model for enzymatic phosphoryl transfer
Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH)+ : a possible model for enzymatic phosphoryl transfer
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Catalysis of the hydrolysis of phosphorylated pyridines by Mg(OH)+ : a possible model for enzymatic phosphoryl transfer

HERSCHLAG, D ; JENCKS, W. P

Biochemistry (Easton), 1990-05, Vol.29 (21), p.5172-5179 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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5
Dissociation of calcium from the phosphorylated calcium-transporting adenosine triphosphatase of sarcoplasmic reticulum: kinetic equivalence of the calcium ions bound to the phosphorylated enzyme
Dissociation of calcium from the phosphorylated calcium-transporting adenosine triphosphatase of sarcoplasmic reticulum: kinetic equivalence of the calcium ions bound to the phosphorylated enzyme
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Dissociation of calcium from the phosphorylated calcium-transporting adenosine triphosphatase of sarcoplasmic reticulum: kinetic equivalence of the calcium ions bound to the phosphorylated enzyme

Hanel, Arthur M ; Jencks, William P

Biochemistry (Easton), 1991-11, Vol.30 (47), p.11320-11330 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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6
There Is Only One Phosphoenzyme Intermediate with Bound Calcium on the Reaction Pathway of the Sarcoplasmic Reticulum Calcium ATPase
There Is Only One Phosphoenzyme Intermediate with Bound Calcium on the Reaction Pathway of the Sarcoplasmic Reticulum Calcium ATPase
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There Is Only One Phosphoenzyme Intermediate with Bound Calcium on the Reaction Pathway of the Sarcoplasmic Reticulum Calcium ATPase

Myung, Jayhyuk ; Jencks, William P

Biochemistry (Easton), 1995-03, Vol.34 (9), p.3077-3083 [Periódico revisado por pares]

United States: American Chemical Society

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7
Phosphorylation of the Sodium−Potassium Adenosinetriphosphatase Proceeds through a Rate-Limiting Conformational Change Followed by Rapid Phosphoryl Transfer
Phosphorylation of the Sodium−Potassium Adenosinetriphosphatase Proceeds through a Rate-Limiting Conformational Change Followed by Rapid Phosphoryl Transfer
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Phosphorylation of the Sodium−Potassium Adenosinetriphosphatase Proceeds through a Rate-Limiting Conformational Change Followed by Rapid Phosphoryl Transfer

Keillor, Jeffrey W ; Jencks, William P

Biochemistry (Easton), 1996-02, Vol.35 (8), p.2750-2753 [Periódico revisado por pares]

United States: American Chemical Society

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8
Lumenal and Cytoplasmic Binding Sites for Calcium on the Calcium ATPase of Sarcoplasmic Reticulum Are Different and Independent
Lumenal and Cytoplasmic Binding Sites for Calcium on the Calcium ATPase of Sarcoplasmic Reticulum Are Different and Independent
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Lumenal and Cytoplasmic Binding Sites for Calcium on the Calcium ATPase of Sarcoplasmic Reticulum Are Different and Independent

Myung, Jayhyuk ; Jencks, William P

Biochemistry (Easton), 1994-07, Vol.33 (29), p.8775-8785 [Periódico revisado por pares]

United States: American Chemical Society

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9
Phosphorylation of the calcium adenosine triphosphatase of sarcoplasmic reticulum: rate-limiting conformational change followed by rapid phosphoryl transfer
Phosphorylation of the calcium adenosine triphosphatase of sarcoplasmic reticulum: rate-limiting conformational change followed by rapid phosphoryl transfer
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Phosphorylation of the calcium adenosine triphosphatase of sarcoplasmic reticulum: rate-limiting conformational change followed by rapid phosphoryl transfer

Petithory, Joanne R ; Jencks, William P

Biochemistry (Easton), 1986-08, Vol.25 (16), p.4493-4497 [Periódico revisado por pares]

American Chemical Society

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10
Optical properties of astaxanthin solutions and aggregates
Optical properties of astaxanthin solutions and aggregates
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Optical properties of astaxanthin solutions and aggregates

Buchwald, Manuel ; Jencks, William P

Biochemistry (Easton), 1968-02, Vol.7 (2), p.834-843 [Periódico revisado por pares]

United States: American Chemical Society

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