PUBLICACIÓN

A program to calculate the isoelectric point of macromolecules

ACCEDER A LA PUBLICACIÓN: Scopus Orcid

Meireles Ribeiro, J., Sillero, A.

1991 Computers in Biology and Medicine

CITAS

30

DOI

10.1016/0010-4825(91)90022-2

EID

2-s2.0-0025833291

ISSN

0010-4825

BIBTEX

@article{Ribeiro1991,title = {A program to calculate the isoelectric point of macromolecules},journal = {Computers in Biology and Medicine},year = {1991},volume = {21},number = {3},pages = {131-141},author = {Meireles Ribeiro, J. and Sillero, A.}}

AUTORES DE LA UEX

Juan Nuno Meireles Da Silva Gonçalves Ribeiro

OTRAS PUBLICACIONES DE INTERÉS

Derivation And Use Of A Formula To Calculate The Net Charge Of Acid-Base Compounds. Its Application To Amino Acids, Proteins And Nucleotides
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Enpp3 Elicited By Edta: Free Amino Acids Accelerate The Time-Dependent Inactivation..: A. Romero Et Al.
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: Free Amino Acids Accelerate The Time-Dependent Inactivation..: A. Romero Et Al.
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
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
Genomic Distribution Of Usha-Like Genes In Bacteria: Comparison To Cpdb-Like Genes
Free Amino Acids Accelerate The Time-Dependent Inactivation Of Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Enpp3 Elicited By Edta
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
Geographical Distribution Of Emergency Services Times In Traffic Accidents In Extremadura
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
Geographical Distribution Of Emergency Services Times In Traffic Accidents In Extremadura
Autosomal Recessive Hypotrichosis With Loose Anagen Hairs Associated With Tkfc Mutations*
Geographical Distribution Of Emergency Services Times In Traffic Accidents In Extremadura
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
Isoelectric Point, Electric Charge, And Nomenclature Of The Acid-Base Residues Of Proteins
Characterization Of Danio Rerio Mn2+-Dependent Adp-Ribose/cdp-Alcohol Diphosphatase, The Structural Prototype Of The Adpribase-Mn-Like Protein Family
Isoelectric Point, Electric Charge, And Nomenclature Of The Acid-Base Residues Of Proteins
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
Isoelectric Point, Electric Charge, And Nomenclature Of The Acid-Base Residues Of Proteins
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
Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase: A Novel Metallophosphoesterase Family Preferentially Expressed In Rodent Immune Cells
Hydrolysis Of The Phosphoanhydride Linkage Of Cyclic Adp-Ribose By The Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase
Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase: A Novel Metallophosphoesterase Family Preferentially Expressed In Rodent Immune Cells
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
Mn2+-Dependent Adp-Ribose/cdp-Alcohol Pyrophosphatase: A Novel Metallophosphoesterase Family Preferentially Expressed In Rodent Immune Cells
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
Human Placenta Hydrolases Active On Free Adp-Ribose: An Adp-Sugar Pyrophosphatase And A Specific Adp-Ribose Pyrophosphatase
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
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
Inhibition And Activation Of Enzymes. The Effect Of A Modifier On The Reaction Rate And On Kinetic Parameters
Nucleotide Ester-Forming Alcoholytic Activities Of Nucleotide Pyrophosphatases: Implications For Practical Biotransformation, Enzyme Mechanisms And Biological Function
Inhibition And Activation Of Enzymes. The Effect Of A Modifier On The Reaction Rate And On Kinetic Parameters
An Easy Procedure To Transform The Ratio Of Two Polynomials Of First Degree Into Michaelis-Menten-Type Equations. Application To The Ordered Uni Bi Enzyme Mechanism
Inhibition And Activation Of Enzymes. The Effect Of A Modifier On The Reaction Rate And On Kinetic Parameters
An Easy Procedure To Transform The Ratio Of Two Polynomials Of First Degree Into Michaelis-Menten-Type Equations. Application To The Ordered Uni Bi Enzyme Mechanism
Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase.
An Easy Procedure To Transform The Ratio Of Two Polynomials Of First Degree Into Michaelis-Menten-Type Equations. Application To The Ordered Uni Bi Enzyme Mechanism
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.
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
Adp-Ribose Pyrophosphatase-I Partially Purified From Livers Of Rats Overdosed With Acetaminophen Reveals Enzyme Inhibition In Vivo Reverted In Vitro By Dithiothreitol
Rat Liver Nucleotide Pyrophosphatase/phosphodiesterase Is An Efficient Adenylyl Transferase
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
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)
A Pharmacokinetic Study Of Peritoneal Absorption Of Glucose And Alanine In Rats: Nutritional Implications
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)
A Pharmacokinetic Study Of Peritoneal Absorption Of Glucose And Alanine In Rats: Nutritional Implications
Rat Liver Adp-Ribose Pyrophosphatase-I As An In Vitro Target Of The Acetaminophen Metabolite N-Acetyl-P-Benzoquinoneimine
A Pharmacokinetic Study Of Peritoneal Absorption Of Glucose And Alanine In Rats: Nutritional Implications
Rat Liver Adp-Ribose Pyrophosphatase-I As An In Vitro Target Of The Acetaminophen Metabolite N-Acetyl-P-Benzoquinoneimine
Specific Adp-Ribose Pyrophosphatase From Artemia Cysts And Rat Liver: Effects Of Nitroprusside, Fluoride And Ionic Strength
Rat Liver Adp-Ribose Pyrophosphatase-I As An In Vitro Target Of The Acetaminophen Metabolite N-Acetyl-P-Benzoquinoneimine
Specific Adp-Ribose Pyrophosphatase From Artemia Cysts And Rat Liver: Effects Of Nitroprusside, Fluoride And Ionic Strength
Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose
Specific Adp-Ribose Pyrophosphatase From Artemia Cysts And Rat Liver: Effects Of Nitroprusside, Fluoride And Ionic Strength
Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose
Enzyme Inhibition As Visualized With The Reservoir Model: Relationships Between I50 And Inhibition Constant(S) Of An Enzyme Inhibitor
Inhibition Of Adp-Ribose Pyrophosphatase-I By Nitric Oxide-Generating Systems: A Mechanism Linking Nitric Oxide To Processes Dependent On Free Adp-Ribose
Enzyme Inhibition As Visualized With The Reservoir Model: Relationships Between I50 And Inhibition Constant(S) Of An Enzyme Inhibitor
A Tridimensional Representation Of Enzyme Inhibition Useful For Diagnostic Purposes
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Ca2+/mg2+-Dependent Endonuclease From Human Spleen: Purification, Properties, And Role In Apoptosis
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Theoretical Isoelectric Points And Electric Charges Of Mutated Human Hemoglobin Subunits
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A Low Km Nucleoside 3′(2′),5′-Biphosphate 3′(2′)-Phosphophydrolase From Rat Liver
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A Low Km Nucleoside 3′(2′),5′-Biphosphate 3′(2′)-Phosphophydrolase From Rat Liver
Computer Program For The Reservoir Model Of Metabolic Crossroads
A Low Km Nucleoside 3′(2′),5′-Biphosphate 3′(2′)-Phosphophydrolase From Rat Liver
Computer Program For The Reservoir Model Of Metabolic Crossroads
An Algorithm For The Computer Calculation Of The Coefficients Of A Polynomial That Allows Determination Of Isoelectric Points Of Proteins And Other Macromolecules
Computer Program For The Reservoir Model Of Metabolic Crossroads
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Hydrolysis Of Bis(5'-Nucleosidyl) Polyphosphates By Escherichia Coli 5'-Nucleotidase
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