Portal Investigación UEx

The Regulation Of Glycolysis In The Hepatopancreas Of The Sea Mussel Mytilus Edulis L.

Homozygous Variant In Tkfc Abolishing Triokinase Activities Is Associated With Isolated Immunodeficiency

Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase / Phosphodiesterase Enpp3 Elicited By Edta

Homozygous Variant In Tkfc Abolishing Triokinase Activities Is Associated With Isolated Immunodeficiency

Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase / Phosphodiesterase Enpp3 Elicited By Edta

Alternative Splicing Of The Last Tkfc Intron Yields Transcripts Differentially Expressed In Human Tissues That Code In Vitro For A Protein Devoid Of Triokinase And Fmn Cyclase Activity

Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase / Phosphodiesterase Enpp3 Elicited By Edta

Alternative Splicing Of The Last Tkfc Intron Yields Transcripts Differentially Expressed In Human Tissues That Code In Vitro For A Protein Devoid Of Triokinase And Fmn Cyclase Activity

Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes

Alternative Splicing Of The Last Tkfc Intron Yields Transcripts Differentially Expressed In Human Tissues That Code In Vitro For A Protein Devoid Of Triokinase And Fmn Cyclase Activity

Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes

Genomic Distribution Of Pro-Virulent Cpdb-Like Genes In Eubacteria And Comparison Of The Enzyme Specificity Of Cpdb-Like Proteins From Salmonella Enterica, Escherichia Coli And Streptococcus Suis

Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes

Genomic Distribution Of Pro-Virulent Cpdb-Like Genes In Eubacteria And Comparison Of The Enzyme Specificity Of Cpdb-Like Proteins From Salmonella Enterica, Escherichia Coli And Streptococcus Suis

The Tkfc Ala185thr Variant, Reported As ‘null’ For Fructose Metabolism, Is Fully Active As Triokinase

Genomic Distribution Of Pro-Virulent Cpdb-Like Genes In Eubacteria And Comparison Of The Enzyme Specificity Of Cpdb-Like Proteins From Salmonella Enterica, Escherichia Coli And Streptococcus Suis

The Tkfc Ala185thr Variant, Reported As ‘null’ For Fructose Metabolism, Is Fully Active As Triokinase

Enzyme Characterization Of Pro-Virulent Snta, A Cell Wall-Anchored Protein Of Streptococcus Suis, With Phosphodiesterase Activity On Cyclic-Di-Amp At A Level Suited To Limit The Innate Immune System

The Tkfc Ala185thr Variant, Reported As ‘null’ For Fructose Metabolism, Is Fully Active As Triokinase

Enzyme Characterization Of Pro-Virulent Snta, A Cell Wall-Anchored Protein Of Streptococcus Suis, With Phosphodiesterase Activity On Cyclic-Di-Amp At A Level Suited To Limit The Innate Immune System

Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations*

Enzyme Characterization Of Pro-Virulent Snta, A Cell Wall-Anchored Protein Of Streptococcus Suis, With Phosphodiesterase Activity On Cyclic-Di-Amp At A Level Suited To Limit The Innate Immune System

Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations*

Substrate Specificity Of Chimeric Enzymes Formed By Interchange Of The Catalytic And Specificity Domains Of The 5′-Nucleotidase Usha And The 3′-Nucleotidase Cpdb

Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations*

Substrate Specificity Of Chimeric Enzymes Formed By Interchange Of The Catalytic And Specificity Domains Of The 5′-Nucleotidase Usha And The 3′-Nucleotidase Cpdb

Article Molecular Dissection Of Escherichia Coli Cpdb: Roles Of The N Domain In Catalysis And Phosphate Inhibition, And Of The C Domain In Substrate Specificity And Adenosine Inhibition

Substrate Specificity Of Chimeric Enzymes Formed By Interchange Of The Catalytic And Specificity Domains Of The 5′-Nucleotidase Usha And The 3′-Nucleotidase Cpdb

Article Molecular Dissection Of Escherichia Coli Cpdb: Roles Of The N Domain In Catalysis And Phosphate Inhibition, And Of The C Domain In Substrate Specificity And Adenosine Inhibition

Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations

Article Molecular Dissection Of Escherichia Coli Cpdb: Roles Of The N Domain In Catalysis And Phosphate Inhibition, And Of The C Domain In Substrate Specificity And Adenosine Inhibition

Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations

Closure Of The Human Tkfc Active Site: Comparison Of The Apoenzyme And The Complexes Formed With Either Triokinase Or Fmn Cyclase Substrates

Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations

Closure Of The Human Tkfc Active Site: Comparison Of The Apoenzyme And The Complexes Formed With Either Triokinase Or Fmn Cyclase Substrates

Specific Cyclic Adp-Ribose Phosphohydrolase Obtained By Mutagenic Engineering Of Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase

Closure Of The Human Tkfc Active Site: Comparison Of The Apoenzyme And The Complexes Formed With Either Triokinase Or Fmn Cyclase Substrates

Specific Cyclic Adp-Ribose Phosphohydrolase Obtained By Mutagenic Engineering Of Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase

The Characterization Of Escherichia Coli Cpdb As A Recombinant Protein Reveals That, Besides Having The Expected 3-Nucleotidase And 2,3-Cyclic Mononucleotide Phosphodiesterase Activities, It Is Also Active As Cyclic Dinucleotide Phosphodiesterase

Specific Cyclic Adp-Ribose Phosphohydrolase Obtained By Mutagenic Engineering Of Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase

The Characterization Of Escherichia Coli Cpdb As A Recombinant Protein Reveals That, Besides Having The Expected 3-Nucleotidase And 2,3-Cyclic Mononucleotide Phosphodiesterase Activities, It Is Also Active As Cyclic Dinucleotide Phosphodiesterase

Molecular Bases Of Catalysis And Adp-Ribose Preference Of Human Mn2+-Dependent Adpribose/cdp-Alcohol Diphosphatase And Conversion By Mutagenesis To A Preferential Cyclic Adp-Ribose Phosphohydrolase

The Characterization Of Escherichia Coli Cpdb As A Recombinant Protein Reveals That, Besides Having The Expected 3-Nucleotidase And 2,3-Cyclic Mononucleotide Phosphodiesterase Activities, It Is Also Active As Cyclic Dinucleotide Phosphodiesterase

Molecular Bases Of Catalysis And Adp-Ribose Preference Of Human Mn2+-Dependent Adpribose/cdp-Alcohol Diphosphatase And Conversion By Mutagenesis To A Preferential Cyclic Adp-Ribose Phosphohydrolase

Bifunctional Homodimeric Triokinase/fmn Cyclase Contribution Of Protein Domains To The Activities Of The Human Enzyme And Molecular Dynamics Simulation Of Domain Movements

Molecular Bases Of Catalysis And Adp-Ribose Preference Of Human Mn2+-Dependent Adpribose/cdp-Alcohol Diphosphatase And Conversion By Mutagenesis To A Preferential Cyclic Adp-Ribose Phosphohydrolase

Bifunctional Homodimeric Triokinase/fmn Cyclase Contribution Of Protein Domains To The Activities Of The Human Enzyme And Molecular Dynamics Simulation Of Domain Movements

Characterization Of Danio Rerio Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase, The Structural Prototype Of The Adpribase-Mn-Like Protein Family

Bifunctional Homodimeric Triokinase/fmn Cyclase Contribution Of Protein Domains To The Activities Of The Human Enzyme And Molecular Dynamics Simulation Of Domain Movements

Characterization Of Danio Rerio Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase, The Structural Prototype Of The Adpribase-Mn-Like Protein Family

Cgdease, A Pseudomonas Fluorescens Protein Of The Plc/apase Superfamily With Cdp-Ethanolamine And (Dihexanoyl)glycerophosphoethanolamine Hydrolase Activity Induced By Osmoprotectants Under Phosphate-Deficient Conditions

Characterization Of Danio Rerio Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase, The Structural Prototype Of The Adpribase-Mn-Like Protein Family

Cgdease, A Pseudomonas Fluorescens Protein Of The Plc/apase Superfamily With Cdp-Ethanolamine And (Dihexanoyl)glycerophosphoethanolamine Hydrolase Activity Induced By Osmoprotectants Under Phosphate-Deficient Conditions

Hydrolysis Of The Phosphoanhydride Linkage Of Cyclic Adp-Ribose By The Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase

Cgdease, A Pseudomonas Fluorescens Protein Of The Plc/apase Superfamily With Cdp-Ethanolamine And (Dihexanoyl)glycerophosphoethanolamine Hydrolase Activity Induced By Osmoprotectants Under Phosphate-Deficient Conditions

Hydrolysis Of The Phosphoanhydride Linkage Of Cyclic Adp-Ribose By The Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase

A Bifunctional Molecule As An Artificial Flavin Mononucleotide Cyclase And A Chemosensor For Selective Fluorescent Detection Of Flavins

Hydrolysis Of The Phosphoanhydride Linkage Of Cyclic Adp-Ribose By The Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase

A Bifunctional Molecule As An Artificial Flavin Mononucleotide Cyclase And A Chemosensor For Selective Fluorescent Detection Of Flavins

Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase: A Novel Metallophosphoesterase Family Preferentially Expressed In Rodent Immune Cells

A Bifunctional Molecule As An Artificial Flavin Mononucleotide Cyclase And A Chemosensor For Selective Fluorescent Detection Of Flavins

Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase: A Novel Metallophosphoesterase Family Preferentially Expressed In Rodent Immune Cells

Cdp-Alcohol Hydrolase, A Very Efficient Activity Of The 5′-Nucleotidase/udp-Sugar Hydrolase Encoded By The Usha Gene Of Yersinia Intermedia And Escherichia Coli

Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase: A Novel Metallophosphoesterase Family Preferentially Expressed In Rodent Immune Cells

Cdp-Alcohol Hydrolase, A Very Efficient Activity Of The 5′-Nucleotidase/udp-Sugar Hydrolase Encoded By The Usha Gene Of Yersinia Intermedia And Escherichia Coli

The Specific, Submicromolar-Km Adp-Ribose Pyrophosphatase Purified From Human Placenta Is Enzymically Indistinguishable From Recombinant Nudt9 Protein, Including A Selectivity For Mn2+ As Activating Cation And Increase In Km For Adp-Ribose, Both Elicited By H2o2

Cdp-Alcohol Hydrolase, A Very Efficient Activity Of The 5′-Nucleotidase/udp-Sugar Hydrolase Encoded By The Usha Gene Of Yersinia Intermedia And Escherichia Coli

The Specific, Submicromolar-Km Adp-Ribose Pyrophosphatase Purified From Human Placenta Is Enzymically Indistinguishable From Recombinant Nudt9 Protein, Including A Selectivity For Mn2+ As Activating Cation And Increase In Km For Adp-Ribose, Both Elicited By H2o2

Identification Of Human And Rat Fad-Amp Lyase (Cyclic Fmn Forming) As Atp-Dependent Dihydroxyacetone Kinases

The Specific, Submicromolar-Km Adp-Ribose Pyrophosphatase Purified From Human Placenta Is Enzymically Indistinguishable From Recombinant Nudt9 Protein, Including A Selectivity For Mn2+ As Activating Cation And Increase In Km For Adp-Ribose, Both Elicited By H2o2

Identification Of Human And Rat Fad-Amp Lyase (Cyclic Fmn Forming) As Atp-Dependent Dihydroxyacetone Kinases

Fluorimetric Hplc Detection Of Endogenous Riboflavin 4′,5′- Cyclic Phosphate In Rat Liver At Nanomolar Concentrations

Identification Of Human And Rat Fad-Amp Lyase (Cyclic Fmn Forming) As Atp-Dependent Dihydroxyacetone Kinases

Fluorimetric Hplc Detection Of Endogenous Riboflavin 4′,5′- Cyclic Phosphate In Rat Liver At Nanomolar Concentrations

Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase

Fluorimetric Hplc Detection Of Endogenous Riboflavin 4′,5′- Cyclic Phosphate In Rat Liver At Nanomolar Concentrations

Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase

Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function

Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase

Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function

Purification, Characterization, And Substrate And Inhibitor Structure-Activity Studies Of Rat Liver Fad-Amp Lyase (Cyclizing): Preference For Fad And Specificity For Splitting Ribonucleoside Diphosphate-X Into Ribonucleotide And A Five-Atom Cyclic Phosphodiester Of X, Either A Monocyclic Compound Or A Cis-Bicyclic Phosphodiester-Pyranose Fusion

Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function

Purification, Characterization, And Substrate And Inhibitor Structure-Activity Studies Of Rat Liver Fad-Amp Lyase (Cyclizing): Preference For Fad And Specificity For Splitting Ribonucleoside Diphosphate-X Into Ribonucleotide And A Five-Atom Cyclic Phosphodiester Of X, Either A Monocyclic Compound Or A Cis-Bicyclic Phosphodiester-Pyranose Fusion

The Simulated Purification Of An Enzyme As A 'dry' Practical Within An Introductory Course Of Biochemistry

Purification, Characterization, And Substrate And Inhibitor Structure-Activity Studies Of Rat Liver Fad-Amp Lyase (Cyclizing): Preference For Fad And Specificity For Splitting Ribonucleoside Diphosphate-X Into Ribonucleotide And A Five-Atom Cyclic Phosphodiester Of X, Either A Monocyclic Compound Or A Cis-Bicyclic Phosphodiester-Pyranose Fusion

The Simulated Purification Of An Enzyme As A 'dry' Practical Within An Introductory Course Of Biochemistry

Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase

The Simulated Purification Of An Enzyme As A 'dry' Practical Within An Introductory Course Of Biochemistry

Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase

Preparation Of Riboflavin 4',5'-Cyclic Phosphate By Incubation Of Flavin-Adenine Dinucleotide With Mn2+ In The Absence Of Riboflavin 5'- Phosphate Cyclase

Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase

Preparation Of Riboflavin 4',5'-Cyclic Phosphate By Incubation Of Flavin-Adenine Dinucleotide With Mn2+ In The Absence Of Riboflavin 5'- Phosphate Cyclase

Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol

Preparation Of Riboflavin 4',5'-Cyclic Phosphate By Incubation Of Flavin-Adenine Dinucleotide With Mn2+ In The Absence Of Riboflavin 5'- Phosphate Cyclase

Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol

Use Of Potato Tuber Nucleotide Pyrophosphatase To Synthesize Adenosine 5 '-Monophosphate Methyl Ester: Evidence That The Solvolytic Preferences Of The Enzyme Are Regulated By Ph And Temperature

Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol

Use Of Potato Tuber Nucleotide Pyrophosphatase To Synthesize Adenosine 5 '-Monophosphate Methyl Ester: Evidence That The Solvolytic Preferences Of The Enzyme Are Regulated By Ph And Temperature

Enzymic Formation Of Riboflavin 4′,5′-Cyclic Phosphate From Fad: Evidence For A Specific Low-Km Fmn Cyclase In Rat Liver

Use Of Potato Tuber Nucleotide Pyrophosphatase To Synthesize Adenosine 5 '-Monophosphate Methyl Ester: Evidence That The Solvolytic Preferences Of The Enzyme Are Regulated By Ph And Temperature

Enzymic Formation Of Riboflavin 4′,5′-Cyclic Phosphate From Fad: Evidence For A Specific Low-Km Fmn Cyclase In Rat Liver

Use Of Potato Tuber Nucleotide Pyrophosphatase To Synthesize Adenosine 5'-Monophosphate Methyl Ester: Evidence That The Solvolytic Preferences Of The Enzyme Are Regulated By Ph And Temperature

Enzymic Formation Of Riboflavin 4′,5′-Cyclic Phosphate From Fad: Evidence For A Specific Low-Km Fmn Cyclase In Rat Liver

Use Of Potato Tuber Nucleotide Pyrophosphatase To Synthesize Adenosine 5'-Monophosphate Methyl Ester: Evidence That The Solvolytic Preferences Of The Enzyme Are Regulated By Ph And Temperature

Glycine-Enhanced Inhibition Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase-I By Edta: A Full Account Of The Reported Inhibition By Commercial Preparations Of Acidic Fibroblast Growth Factor (Fgf-1)

Use Of Potato Tuber Nucleotide Pyrophosphatase To Synthesize Adenosine 5'-Monophosphate Methyl Ester: Evidence That The Solvolytic Preferences Of The Enzyme Are Regulated By Ph And Temperature

Glycine-Enhanced Inhibition Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase-I By Edta: A Full Account Of The Reported Inhibition By Commercial Preparations Of Acidic Fibroblast Growth Factor (Fgf-1)

Identification Of Rat Liver Glucose-3-Phosphatase As An Inositol Monophosphatase Inhibited By Lithium

Glycine-Enhanced Inhibition Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase-I By Edta: A Full Account Of The Reported Inhibition By Commercial Preparations Of Acidic Fibroblast Growth Factor (Fgf-1)

Identification Of Rat Liver Glucose-3-Phosphatase As An Inositol Monophosphatase Inhibited By Lithium

Rat Liver Adp-Ribose Pyrophosphatase-I As An In Vitro Target Of The Acetaminophen Metabolite N-Acetyl-P-Benzoquinoneimine

Identification Of Rat Liver Glucose-3-Phosphatase As An Inositol Monophosphatase Inhibited By Lithium

Rat Liver Adp-Ribose Pyrophosphatase-I As An In Vitro Target Of The Acetaminophen Metabolite N-Acetyl-P-Benzoquinoneimine

Interaction Of Divalent Metal Ions With Fructose 2,6-Bisphosphate And Analogs

Rat Liver Adp-Ribose Pyrophosphatase-I As An In Vitro Target Of The Acetaminophen Metabolite N-Acetyl-P-Benzoquinoneimine

Interaction Of Divalent Metal Ions With Fructose 2,6-Bisphosphate And Analogs

Specific Adp-Ribose Pyrophosphatase From Artemia Cysts And Rat Liver: Effects Of Nitroprusside, Fluoride And Ionic Strength

Interaction Of Divalent Metal Ions With Fructose 2,6-Bisphosphate And Analogs

Specific Adp-Ribose Pyrophosphatase From Artemia Cysts And Rat Liver: Effects Of Nitroprusside, Fluoride And Ionic Strength

High Efficiency Of Glycerol 2‐phosphate And Sn ‐glycerol 3‐phosphate As Nucleotidyl Acceptors In Snake Venom Phosphodiesterase Esterifications: Formation Of Primary And Secondary Amp‐o‐glyceryl And Amp‐o‐glycerophosphoryl Esters And Evidence For An Acceptor‐binding Enzyme Site

Specific Adp-Ribose Pyrophosphatase From Artemia Cysts And Rat Liver: Effects Of Nitroprusside, Fluoride And Ionic Strength

High Efficiency Of Glycerol 2‐phosphate And Sn ‐glycerol 3‐phosphate As Nucleotidyl Acceptors In Snake Venom Phosphodiesterase Esterifications: Formation Of Primary And Secondary Amp‐o‐glyceryl And Amp‐o‐glycerophosphoryl Esters And Evidence For An Acceptor‐binding Enzyme Site

Rat Liver Nucleoside Diphosphosugar Or Diphosphoalcohol Pyrophosphatases Different From Nucleotide Pyrophosphatase Or Phosphodiesterase I: Substrate Specificities Of Mg2+- And/or Mn2+-Dependent Hydrolases Acting On Adp-Ribose

High Efficiency Of Glycerol 2‐phosphate And Sn ‐glycerol 3‐phosphate As Nucleotidyl Acceptors In Snake Venom Phosphodiesterase Esterifications: Formation Of Primary And Secondary Amp‐o‐glyceryl And Amp‐o‐glycerophosphoryl Esters And Evidence For An Acceptor‐binding Enzyme Site

Rat Liver Nucleoside Diphosphosugar Or Diphosphoalcohol Pyrophosphatases Different From Nucleotide Pyrophosphatase Or Phosphodiesterase I: Substrate Specificities Of Mg2+- And/or Mn2+-Dependent Hydrolases Acting On Adp-Ribose

Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose

Rat Liver Nucleoside Diphosphosugar Or Diphosphoalcohol Pyrophosphatases Different From Nucleotide Pyrophosphatase Or Phosphodiesterase I: Substrate Specificities Of Mg2+- And/or Mn2+-Dependent Hydrolases Acting On Adp-Ribose

Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose

Detection Of Specific Glucose-3-Phosphatase Activity In Rat Liver

Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose

Detection Of Specific Glucose-3-Phosphatase Activity In Rat Liver

Rat Liver Mitochondrial Adp-Ribose Pyrophosphatase In The Matrix Space With Low K(M) For Free Adp-Ribose

Detection Of Specific Glucose-3-Phosphatase Activity In Rat Liver

Rat Liver Mitochondrial Adp-Ribose Pyrophosphatase In The Matrix Space With Low K(M) For Free Adp-Ribose

Alcohol Esterification Reactions And Mechanisms Of Snake Venom 5′‐nucleotide Phosphodiesterase

Rat Liver Mitochondrial Adp-Ribose Pyrophosphatase In The Matrix Space With Low K(M) For Free Adp-Ribose

Alcohol Esterification Reactions And Mechanisms Of Snake Venom 5′‐nucleotide Phosphodiesterase

Enzyme Saturation And Inhibition Kinetics Studied From Multiple Progress Curves Recorded Spectrophotometrically From Single Reaction Mixtures For Adp-Ribose Pyrophosphatase

Alcohol Esterification Reactions And Mechanisms Of Snake Venom 5′‐nucleotide Phosphodiesterase

Enzyme Saturation And Inhibition Kinetics Studied From Multiple Progress Curves Recorded Spectrophotometrically From Single Reaction Mixtures For Adp-Ribose Pyrophosphatase

Dinucleoside Tetraphosphatase From Human Blood Cells. Purification And Characterization As A High Specific Activity Enzyme Recognized By An Anti-Rat Tetraphosphatase Antibody

Enzyme Saturation And Inhibition Kinetics Studied From Multiple Progress Curves Recorded Spectrophotometrically From Single Reaction Mixtures For Adp-Ribose Pyrophosphatase

Dinucleoside Tetraphosphatase From Human Blood Cells. Purification And Characterization As A High Specific Activity Enzyme Recognized By An Anti-Rat Tetraphosphatase Antibody

Location Of Dinucleoside Triphosphatase In The Matrix Space Of Rat Liver Mitochondria

Dinucleoside Tetraphosphatase From Human Blood Cells. Purification And Characterization As A High Specific Activity Enzyme Recognized By An Anti-Rat Tetraphosphatase Antibody

Location Of Dinucleoside Triphosphatase In The Matrix Space Of Rat Liver Mitochondria

Methanol Esterification Reactions Catalyzed By Snake Venom And Bovine Intestinal 5′‐nucleotide Phosphodiesterases: Formation Of Nucleoside 5′‐monophosphate Methyl Esters From Guanosine 5′‐triphosphate And Other Nucleoside 5′‐polyphosphates

Location Of Dinucleoside Triphosphatase In The Matrix Space Of Rat Liver Mitochondria

Methanol Esterification Reactions Catalyzed By Snake Venom And Bovine Intestinal 5′‐nucleotide Phosphodiesterases: Formation Of Nucleoside 5′‐monophosphate Methyl Esters From Guanosine 5′‐triphosphate And Other Nucleoside 5′‐polyphosphates

Particulate Diadenosine 5′,5‴-P1,p3-Triphosphate Hydrolases In Rat Brain: Two Specific Dinucleoside Triphosphatases And Two Phosphodiesterase I-Like Hydrolases

Methanol Esterification Reactions Catalyzed By Snake Venom And Bovine Intestinal 5′‐nucleotide Phosphodiesterases: Formation Of Nucleoside 5′‐monophosphate Methyl Esters From Guanosine 5′‐triphosphate And Other Nucleoside 5′‐polyphosphates

Particulate Diadenosine 5′,5‴-P1,p3-Triphosphate Hydrolases In Rat Brain: Two Specific Dinucleoside Triphosphatases And Two Phosphodiesterase I-Like Hydrolases

Purification To Homogeneity Of Rat Liver Dinucleoside Tetraphosphatase By Affinity Elution With Adenosine 5′-Tetraphosphate

Particulate Diadenosine 5′,5‴-P1,p3-Triphosphate Hydrolases In Rat Brain: Two Specific Dinucleoside Triphosphatases And Two Phosphodiesterase I-Like Hydrolases

Purification To Homogeneity Of Rat Liver Dinucleoside Tetraphosphatase By Affinity Elution With Adenosine 5′-Tetraphosphate

A Specific, Low Km Adp-Ribose Pyrophosphatase From Rat Liver

Purification To Homogeneity Of Rat Liver Dinucleoside Tetraphosphatase By Affinity Elution With Adenosine 5′-Tetraphosphate

A Specific, Low Km Adp-Ribose Pyrophosphatase From Rat Liver

Phosphoglycerate Kinase From Yeast Synthesizes Guanosine 5'-Tetraphosphate

A Specific, Low Km Adp-Ribose Pyrophosphatase From Rat Liver

Phosphoglycerate Kinase From Yeast Synthesizes Guanosine 5'-Tetraphosphate

The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)

Phosphoglycerate Kinase From Yeast Synthesizes Guanosine 5'-Tetraphosphate

The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)

Cytosol 5′-Nucleotidase From Artemia Embryos. Purification And Properties

The Inhibition Of Fructose 1,6-Bisphosphatase By Fructose 2,6-Biphosphate Is Enhanced By Edta And Diminished By Zinc(Ii)

Cytosol 5′-Nucleotidase From Artemia Embryos. Purification And Properties

Binding Of Zinc(Ii) To Β-D-Fructose 2,6-Bisphosphate

Cytosol 5′-Nucleotidase From Artemia Embryos. Purification And Properties

Binding Of Zinc(Ii) To Β-D-Fructose 2,6-Bisphosphate

Gasolines As Primary Solvents In Liquid Scintillation Counting

Binding Of Zinc(Ii) To Β-D-Fructose 2,6-Bisphosphate

Gasolines As Primary Solvents In Liquid Scintillation Counting

Diadenosine Tetraphosphate Activates Cytosol 5′-Nucleotidase

Gasolines As Primary Solvents In Liquid Scintillation Counting

Diadenosine Tetraphosphate Activates Cytosol 5′-Nucleotidase

Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides

Diadenosine Tetraphosphate Activates Cytosol 5′-Nucleotidase

Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides

Mitochondrial Location Of Rat Liver Dinucleoside Triphosphatase

Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides

Mitochondrial Location Of Rat Liver Dinucleoside Triphosphatase

Imp Dehydrogenase From Artemia Embryos: Molecular Forms, Purification And Properties

Mitochondrial Location Of Rat Liver Dinucleoside Triphosphatase

Imp Dehydrogenase From Artemia Embryos: Molecular Forms, Purification And Properties

Occurrence Of Dinucleosidetriphosphatase In The Cytosol And Particulate Fractions From Rat Liver

Imp Dehydrogenase From Artemia Embryos: Molecular Forms, Purification And Properties

Occurrence Of Dinucleosidetriphosphatase In The Cytosol And Particulate Fractions From Rat Liver

Adenosine Deaminase Isozymes In Artemia

Occurrence Of Dinucleosidetriphosphatase In The Cytosol And Particulate Fractions From Rat Liver

Adenosine Deaminase Isozymes In Artemia

Dinucleosidetriphosphatase From Rat Brain

Adenosine Deaminase Isozymes In Artemia

Dinucleosidetriphosphatase From Rat Brain

Two Low K(M) Hydrolytic Activities On Dinucleoside 5',5'''-P1,p4-Tetraphosphates In Rat Liver. Characterization As The Specific Dinucleoside Tetraphosphatase And A Phosphodiesterase I-Like Enzyme

Dinucleosidetriphosphatase From Rat Brain

Two Low K(M) Hydrolytic Activities On Dinucleoside 5',5'''-P1,p4-Tetraphosphates In Rat Liver. Characterization As The Specific Dinucleoside Tetraphosphatase And A Phosphodiesterase I-Like Enzyme

Presence Of Two Isozymes Of Adenylosuccinate Synthetase In Artemia Salina Embryos. Purification And Properties

Two Low K(M) Hydrolytic Activities On Dinucleoside 5',5'''-P1,p4-Tetraphosphates In Rat Liver. Characterization As The Specific Dinucleoside Tetraphosphatase And A Phosphodiesterase I-Like Enzyme

Presence Of Two Isozymes Of Adenylosuccinate Synthetase In Artemia Salina Embryos. Purification And Properties

Presence Of Cytidine 5′-Tetraphosphate In Commercial Samples Of Cytidine 5′-Triphosphate

Presence Of Two Isozymes Of Adenylosuccinate Synthetase In Artemia Salina Embryos. Purification And Properties

Presence Of Cytidine 5′-Tetraphosphate In Commercial Samples Of Cytidine 5′-Triphosphate

Dinucleosidetetraphosphatase Inhibition By Zn(Ii)

Presence Of Cytidine 5′-Tetraphosphate In Commercial Samples Of Cytidine 5′-Triphosphate

Dinucleosidetetraphosphatase Inhibition By Zn(Ii)

Adenylosuccinate Lyase From Artemia Embryos. Purification And Properties.

Dinucleosidetetraphosphatase Inhibition By Zn(Ii)

Adenylosuccinate Lyase From Artemia Embryos. Purification And Properties.

A Cut-Out Model Of The Α-Helix For Student Use

Adenylosuccinate Lyase From Artemia Embryos. Purification And Properties.

A Cut-Out Model Of The Α-Helix For Student Use

Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.

A Cut-Out Model Of The Α-Helix For Student Use

Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.

The Regulation Of Glycolysis In The Hepatopancreas Of The Sea Mussel Mytilus Edulis L.

Bis-(5'-Guanosyl) Tetraphosphatase In Rat Tissues.

The Regulation Of Glycolysis In The Hepatopancreas Of The Sea Mussel Mytilus Edulis L.

Homozygous Variant In Tkfc Abolishing Triokinase Activities Is Associated With Isolated Immunodeficiency