PUBLICACIÓN

Identification of two types of Ca2+ transport ATPases in pig brain by specific antibodies

ACCEDER A LA PUBLICACIÓN: Scopus Orcid

Salvador, J.M.; Mata, A.M.

1995 Biochemical Society Transactions

CITAS

3

DOI

10.1042/bst023571s

EID

2-s2.0-0028804171

ISSN

0300-5127

BIBTEX

@article{Mata1995,title = {Identification of two types of Ca2+ transport ATPases in pig brain by specific antibodies},journal = {Biochemical Society Transactions},year = {1995},volume = {23},number = {4},pages = {571},author = {Salvador, J.M. and Mata, A.M.}}

AUTORES DE LA UEX

Ana María Mata Durán

OTRAS PUBLICACIONES DE INTERÉS

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Unveiling The Agonistic Properties Of Preyssler-Type Polyoxotungstates On Purinergic P2 Receptors
The Plasma Membrane Ca2+-Atpase, A Molecular Target For Tau-Induced Cytosolic Calcium Dysregulation
Unveiling The Agonistic Properties Of Preyssler-Type Polyoxotungstates On Purinergic P2 Receptors
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Inhibition Of Serca And Pmca Ca2+-Atpase Activities By Polyoxotungstates
Internalized Amyloid-Β (1-42) Peptide Inhibits The Store-Operated Calcium Entry In Ht-22 Cells
Inhibition Of Serca And Pmca Ca2+-Atpase Activities By Polyoxotungstates
Internalized Amyloid-Β (1-42) Peptide Inhibits The Store-Operated Calcium Entry In Ht-22 Cells
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Internalized Amyloid-Β (1-42) Peptide Inhibits The Store-Operated Calcium Entry In Ht-22 Cells
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Design And Experimental Evaluation Of A Peptide Antagonist Against Amyloid Β(1–42) Interactions With Calmodulin And Calbindin-D28k
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Methylene Blue Blocks And Reverses The Inhibitory Effect Of Tau On Pmca Function
Correction To: Stim1 Deficiency Is Linked To Alzheimer’s Disease And Triggers Cell Death In Sh-Sy5y Cells By Upregulation Of L-Type Voltage-Operated Ca2+ Entry (Journal Of Molecular Medicine, (2018), 96, 10, (1061-1079), 10.1007/s00109-018-1677-Y)
Methylene Blue Blocks And Reverses The Inhibitory Effect Of Tau On Pmca Function
Correction To: Stim1 Deficiency Is Linked To Alzheimer’s Disease And Triggers Cell Death In Sh-Sy5y Cells By Upregulation Of L-Type Voltage-Operated Ca2+ Entry (Journal Of Molecular Medicine, (2018), 96, 10, (1061-1079), 10.1007/s00109-018-1677-Y)
Methylene Blue Activates The Pmca Activity And Cross-Interacts With Amyloid Β-Peptide, Blocking Aβ-Mediated Pmca Inhibition
Correction To: Stim1 Deficiency Is Linked To Alzheimer’s Disease And Triggers Cell Death In Sh-Sy5y Cells By Upregulation Of L-Type Voltage-Operated Ca2+ Entry (Journal Of Molecular Medicine, (2018), 96, 10, (1061-1079), 10.1007/s00109-018-1677-Y)
Methylene Blue Activates The Pmca Activity And Cross-Interacts With Amyloid Β-Peptide, Blocking Aβ-Mediated Pmca Inhibition
Functional Interplay Between Plasma Membrane Ca2+-Atpase, Amyloid Β-Peptide And Tau
Methylene Blue Activates The Pmca Activity And Cross-Interacts With Amyloid Β-Peptide, Blocking Aβ-Mediated Pmca Inhibition
Functional Interplay Between Plasma Membrane Ca2+-Atpase, Amyloid Β-Peptide And Tau
Stim1 Deficiency Is Linked To Alzheimer’s Disease And Triggers Cell Death In Sh-Sy5y Cells By Upregulation Of L-Type Voltage-Operated Ca2+ Entry
Functional Interplay Between Plasma Membrane Ca2+-Atpase, Amyloid Β-Peptide And Tau
Stim1 Deficiency Is Linked To Alzheimer’s Disease And Triggers Cell Death In Sh-Sy5y Cells By Upregulation Of L-Type Voltage-Operated Ca2+ Entry
Phospholipids And Calmodulin Modulate The Inhibition Of Pmca Activity By Tau
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Phospholipids And Calmodulin Modulate The Inhibition Of Pmca Activity By Tau
High Affinity Binding Of Amyloid Β-Peptide To Calmodulin: Structural And Functional Implications
Phospholipids And Calmodulin Modulate The Inhibition Of Pmca Activity By Tau
High Affinity Binding Of Amyloid Β-Peptide To Calmodulin: Structural And Functional Implications
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High Affinity Binding Of Amyloid Β-Peptide To Calmodulin: Structural And Functional Implications
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High Levels Of Mn2+ Inhibit Secretory Pathway Ca 2+/mn2+-Atpase (Spca) Activity And Cause Golgi Fragmentation In Neurons And Glia
Evaluation Of Manganese Uptake And Toxicity In Mouse Brain During Continuous Mncl2 Administration Using Osmotic Pumps
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Evaluation Of Manganese Uptake And Toxicity In Mouse Brain During Continuous Mncl2 Administration Using Osmotic Pumps
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Impairment Of The Activity Of The Plasma Membrane Ca2+-Atpase In Alzheimer's Disease
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Silencing The Spca1 (Secretory Pathway Ca2+-Atpase Isoform 1) Impairs Ca2+ Homeostasis In The Golgi And Disturbs Neural Polarity
Impairment Of The Activity Of The Plasma Membrane Ca2+-Atpase In Alzheimer's Disease
Silencing The Spca1 (Secretory Pathway Ca2+-Atpase Isoform 1) Impairs Ca2+ Homeostasis In The Golgi And Disturbs Neural Polarity
Ontogeny Of Atp Hydrolysis And Isoform Expression Of The Plasma Membrane Ca2+-Atpase In Mouse Brain
Silencing The Spca1 (Secretory Pathway Ca2+-Atpase Isoform 1) Impairs Ca2+ Homeostasis In The Golgi And Disturbs Neural Polarity
Ontogeny Of Atp Hydrolysis And Isoform Expression Of The Plasma Membrane Ca2+-Atpase In Mouse Brain
Altered Ca2+ Dependence Of Synaptosomal Plasma Membrane Ca 2+-Atpase In Human Brain Affected By Alzheimer's Disease
Ontogeny Of Atp Hydrolysis And Isoform Expression Of The Plasma Membrane Ca2+-Atpase In Mouse Brain
Altered Ca2+ Dependence Of Synaptosomal Plasma Membrane Ca 2+-Atpase In Human Brain Affected By Alzheimer's Disease
Activity And Localization Of The Secretory Pathway Ca2+-Atpase Isoform 1 (Spca1) In Different Areas Of The Mouse Brain During Postnatal Development
Altered Ca2+ Dependence Of Synaptosomal Plasma Membrane Ca 2+-Atpase In Human Brain Affected By Alzheimer's Disease
Activity And Localization Of The Secretory Pathway Ca2+-Atpase Isoform 1 (Spca1) In Different Areas Of The Mouse Brain During Postnatal Development
Functional And Immunocytochemical Evidence For The Expression And Localization Of The Secretory Pathway Ca2+-Atpase Isoform 1 (Spca1) In Cerebellum Relative To Other Ca2+ Pumps
Activity And Localization Of The Secretory Pathway Ca2+-Atpase Isoform 1 (Spca1) In Different Areas Of The Mouse Brain During Postnatal Development
Functional And Immunocytochemical Evidence For The Expression And Localization Of The Secretory Pathway Ca2+-Atpase Isoform 1 (Spca1) In Cerebellum Relative To Other Ca2+ Pumps
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Functional And Immunocytochemical Evidence For The Expression And Localization Of The Secretory Pathway Ca2+-Atpase Isoform 1 (Spca1) In Cerebellum Relative To Other Ca2+ Pumps
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Developmental Distribution Of Plasma Membrane Ca2+-Atpase Isoforms In Chick Cerebellum
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The Plasma Membrane Ca2+-Atpase Isoform 4 Is Localized In Lipid Rafts Of Cerebellum Synaptic Plasma Membranes
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Calcium Pumps In The Central Nervous System
Localization Of Intracellular And Plasma Membrane Ca2+-Atpases In The Cerebellum
Calcium Pumps In The Central Nervous System
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The Interaction Of Ethanol With Reconstituted Synaptosomal Plasma Membrane Ca 2+-Atpase
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Ca2+ Transport By The Synaptosomal Plasma Membrane Ca 2+-Atpase And The Effect Of Thioridazinet
Localization Of Endoplasmic Reticulum And Plasma Membrane Ca 2+-Atpases In Subcellular Fractions And Sections Of Pig Cerebellum
Ca2+ Transport By The Synaptosomal Plasma Membrane Ca 2+-Atpase And The Effect Of Thioridazinet
Localization Of Endoplasmic Reticulum And Plasma Membrane Ca 2+-Atpases In Subcellular Fractions And Sections Of Pig Cerebellum
Erratum: Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids (Biochimica Et Biophysica Acta (2003) 1611 (197-203))
Localization Of Endoplasmic Reticulum And Plasma Membrane Ca 2+-Atpases In Subcellular Fractions And Sections Of Pig Cerebellum
Erratum: Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids (Biochimica Et Biophysica Acta (2003) 1611 (197-203))
Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids
Erratum: Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids (Biochimica Et Biophysica Acta (2003) 1611 (197-203))
Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids
Distribution Of The Intracellular Ca2+-Atpase Isoform 2b In Pig Brain Subcellular Fractions And Cross-Reaction With A Monoclonal Antibody Raised Against The Enzyme Isoform 1
Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids
Distribution Of The Intracellular Ca2+-Atpase Isoform 2b In Pig Brain Subcellular Fractions And Cross-Reaction With A Monoclonal Antibody Raised Against The Enzyme Isoform 1
Ca2+ Transport By Reconstituted Synaptosomal Atpase Is Associated With H+ Countertransport And Net Charge Displacement
Distribution Of The Intracellular Ca2+-Atpase Isoform 2b In Pig Brain Subcellular Fractions And Cross-Reaction With A Monoclonal Antibody Raised Against The Enzyme Isoform 1
Ca2+ Transport By Reconstituted Synaptosomal Atpase Is Associated With H+ Countertransport And Net Charge Displacement
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Ca2+ Transport By Reconstituted Synaptosomal Atpase Is Associated With H+ Countertransport And Net Charge Displacement
Characterization Of The Intracellular And The Plasma Membrane Ca2+- Atpases In Fractionated Pig Brain Membranes Using Calcium Pump Inhibitors
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Characterization Of The Intracellular And The Plasma Membrane Ca2+- Atpases In Fractionated Pig Brain Membranes Using Calcium Pump Inhibitors
Evidence That An Ant1-Serca1 Monoclonal Antibody Recognizes The Serca2b Calcium Pump In Pig Brain
Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain
Evidence That An Ant1-Serca1 Monoclonal Antibody Recognizes The Serca2b Calcium Pump In Pig Brain
Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain
Correction: Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain (Biochemical Journal (1996) 315 (183-187))
Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain
Correction: Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain (Biochemical Journal (1996) 315 (183-187))
The Modulation Of Ca2+ Binding To Sarcoplasmic Reticulum Atpase By Atp Analogues Is Ph-Dependent
Correction: Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain (Biochemical Journal (1996) 315 (183-187))
The Modulation Of Ca2+ Binding To Sarcoplasmic Reticulum Atpase By Atp Analogues Is Ph-Dependent
Identification Of Two Types Of Ca2+ Transport Atpases In Pig Brain By Specific Antibodies
The Modulation Of Ca2+ Binding To Sarcoplasmic Reticulum Atpase By Atp Analogues Is Ph-Dependent
Identification Of Two Types Of Ca2+ Transport Atpases In Pig Brain By Specific Antibodies
Evidence For The Lumenal Location Of The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum
Identification Of Two Types Of Ca2+ Transport Atpases In Pig Brain By Specific Antibodies
Evidence For The Lumenal Location Of The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum
Reactivity Of Lysyl Residues On The (Ca2+-Mg2+)-Atpase To 7-Amino-4-Methylcoumarin-3-Acetic Acid Succinimidyl Ester
Evidence For The Lumenal Location Of The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum
Reactivity Of Lysyl Residues On The (Ca2+-Mg2+)-Atpase To 7-Amino-4-Methylcoumarin-3-Acetic Acid Succinimidyl Ester
Labeling The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum At Glu-439 With 5-(Bromomethyl)fluorescein
Reactivity Of Lysyl Residues On The (Ca2+-Mg2+)-Atpase To 7-Amino-4-Methylcoumarin-3-Acetic Acid Succinimidyl Ester
Labeling The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum At Glu-439 With 5-(Bromomethyl)fluorescein
Localization Of Cys-344 On The (Ca2+ -Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Resonance Energy Transfer
Labeling The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum At Glu-439 With 5-(Bromomethyl)fluorescein
Localization Of Cys-344 On The (Ca2+ -Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Resonance Energy Transfer
Definition Of Surface-Exposed And Trans-Membranous Regions Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Anti-Peptide Antibodies
Localization Of Cys-344 On The (Ca2+ -Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Resonance Energy Transfer
Definition Of Surface-Exposed And Trans-Membranous Regions Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Anti-Peptide Antibodies
Studies Of The Structure And Function Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Immunological Approaches
Definition Of Surface-Exposed And Trans-Membranous Regions Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Anti-Peptide Antibodies
Studies Of The Structure And Function Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Immunological Approaches
An Examination Of The Transmembranous Organisation Of The Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Antipeptide Antibodies
Studies Of The Structure And Function Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Immunological Approaches
An Examination Of The Transmembranous Organisation Of The Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Antipeptide Antibodies
Definition Of An Epitope At The Nucleotide Binding Site Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum By Fluorescein Labelling
An Examination Of The Transmembranous Organisation Of The Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Antipeptide Antibodies
Definition Of An Epitope At The Nucleotide Binding Site Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum By Fluorescein Labelling
Chemical Crosslinking And Enzyme Kinetics Provide No Evidence For A Regulatory Role For The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum In Calcium Transport
Definition Of An Epitope At The Nucleotide Binding Site Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum By Fluorescein Labelling
Chemical Crosslinking And Enzyme Kinetics Provide No Evidence For A Regulatory Role For The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum In Calcium Transport
Mapping Epitopes On The (Ca2+mg2+)-Atpase Of Sarcoplasmic Reticulum Using Fusion Proteins
Chemical Crosslinking And Enzyme Kinetics Provide No Evidence For A Regulatory Role For The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum In Calcium Transport
Mapping Epitopes On The (Ca2+mg2+)-Atpase Of Sarcoplasmic Reticulum Using Fusion Proteins
The Effect Of A Monoclonal Antibody On Specific Steps Of The Reaction Sequence Of The (Ca2+-Mg2+)-Atpase From Sarcoplasmic Reticulum
Mapping Epitopes On The (Ca2+mg2+)-Atpase Of Sarcoplasmic Reticulum Using Fusion Proteins
The Effect Of A Monoclonal Antibody On Specific Steps Of The Reaction Sequence Of The (Ca2+-Mg2+)-Atpase From Sarcoplasmic Reticulum
Effect Of The Detergent C12e8 On The Binding Of Monoclonal Antibodies To The (Ca2+-Mg2+)-Atpase Of Rabbit Skeletal Sarcoplasmic Reticulum
The Effect Of A Monoclonal Antibody On Specific Steps Of The Reaction Sequence Of The (Ca2+-Mg2+)-Atpase From Sarcoplasmic Reticulum
Effect Of The Detergent C12e8 On The Binding Of Monoclonal Antibodies To The (Ca2+-Mg2+)-Atpase Of Rabbit Skeletal Sarcoplasmic Reticulum
Distribution Of Two Distinct Ca2+ -Atpase-Like Proteins And Their Relationships To The Agonist-Sensitive Calcium Store In Adrenal Chromaffin Cells
Effect Of The Detergent C12e8 On The Binding Of Monoclonal Antibodies To The (Ca2+-Mg2+)-Atpase Of Rabbit Skeletal Sarcoplasmic Reticulum
Distribution Of Two Distinct Ca2+ -Atpase-Like Proteins And Their Relationships To The Agonist-Sensitive Calcium Store In Adrenal Chromaffin Cells
Effects Of Atpase Activity Of Monoclonal Antibodies Raised Against (Ca2+ + Mg2+)-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum And Their Correlation With Epitope Location
Distribution Of Two Distinct Ca2+ -Atpase-Like Proteins And Their Relationships To The Agonist-Sensitive Calcium Store In Adrenal Chromaffin Cells
Effects Of Atpase Activity Of Monoclonal Antibodies Raised Against (Ca2+ + Mg2+)-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum And Their Correlation With Epitope Location
Probing The Nucleotide-Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase With Anti-Fluorescein Antibodies
Effects Of Atpase Activity Of Monoclonal Antibodies Raised Against (Ca2+ + Mg2+)-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum And Their Correlation With Epitope Location
Probing The Nucleotide-Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase With Anti-Fluorescein Antibodies
Evidence For The Cytoplasmic Location Of The N- And C-Terminal Segments Of Sarcoplasmic Reticulum (Ca2+mg2+)-Atpase
Probing The Nucleotide-Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase With Anti-Fluorescein Antibodies
Evidence For The Cytoplasmic Location Of The N- And C-Terminal Segments Of Sarcoplasmic Reticulum (Ca2+mg2+)-Atpase
Probing The Nucleotide Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2)-Atpase With Anti-Fluorescein Antibodies
Evidence For The Cytoplasmic Location Of The N- And C-Terminal Segments Of Sarcoplasmic Reticulum (Ca2+mg2+)-Atpase
Probing The Nucleotide Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2)-Atpase With Anti-Fluorescein Antibodies
Use Of Antibodies To Detect Chemically Cross-Linked Products From Sarcoplasmic Reticulum
Probing The Nucleotide Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2)-Atpase With Anti-Fluorescein Antibodies
Use Of Antibodies To Detect Chemically Cross-Linked Products From Sarcoplasmic Reticulum
Effect Of Monoclonal Antibodies Raised Against Ca2+,mg2+-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum On Atpase Activity And Its Correlation With Epitope Location
Use Of Antibodies To Detect Chemically Cross-Linked Products From Sarcoplasmic Reticulum
Effect Of Monoclonal Antibodies Raised Against Ca2+,mg2+-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum On Atpase Activity And Its Correlation With Epitope Location
The Position Of The Atp Binding Site On The (Ca2+ + Mg2+)-Atpase
Effect Of Monoclonal Antibodies Raised Against Ca2+,mg2+-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum On Atpase Activity And Its Correlation With Epitope Location
The Position Of The Atp Binding Site On The (Ca2+ + Mg2+)-Atpase
Dependence Of The Fluorescence Of Fluorescein Labelled (Ca2+, Mg2+)-Atpase Upon The Lipid To Protein Ratio In Sarcoplasmic Reticulum Reconstituted Systems
The Position Of The Atp Binding Site On The (Ca2+ + Mg2+)-Atpase
Dependence Of The Fluorescence Of Fluorescein Labelled (Ca2+, Mg2+)-Atpase Upon The Lipid To Protein Ratio In Sarcoplasmic Reticulum Reconstituted Systems
Redox Interconversion Of Escherichia Coli Glutathione Reductase. A Study With Permeabilized And Intact Cells
Dependence Of The Fluorescence Of Fluorescein Labelled (Ca2+, Mg2+)-Atpase Upon The Lipid To Protein Ratio In Sarcoplasmic Reticulum Reconstituted Systems
Redox Interconversion Of Escherichia Coli Glutathione Reductase. A Study With Permeabilized And Intact Cells
Redox Interconversion Of Glutathione Reductase From Escherichia Coli. A Study With Pure Enzyme And Cell-Free Extracts
Redox Interconversion Of Escherichia Coli Glutathione Reductase. A Study With Permeabilized And Intact Cells
Redox Interconversion Of Glutathione Reductase From Escherichia Coli. A Study With Pure Enzyme And Cell-Free Extracts
The Redox Interconversion Mechanism Of Saccahromyces Cerevisiae Glutathione Reductase
Redox Interconversion Of Glutathione Reductase From Escherichia Coli. A Study With Pure Enzyme And Cell-Free Extracts
The Redox Interconversion Mechanism Of Saccahromyces Cerevisiae Glutathione Reductase
Purification By Affinity Chromatography Of Glutathione Reductase (Ec 1.6.4.2) From Escherichia Coli And Characterization Of Such Enzyme
The Redox Interconversion Mechanism Of Saccahromyces Cerevisiae Glutathione Reductase
Purification By Affinity Chromatography Of Glutathione Reductase (Ec 1.6.4.2) From Escherichia Coli And Characterization Of Such Enzyme
Reversible Inactivation Of Saccharomyces Cerevisiae Glutathione Reductase Under Reducing Conditions
Purification By Affinity Chromatography Of Glutathione Reductase (Ec 1.6.4.2) From Escherichia Coli And Characterization Of Such Enzyme
Reversible Inactivation Of Saccharomyces Cerevisiae Glutathione Reductase Under Reducing Conditions
Neurotoxic Amyloid Β‐peptide And Tau Produce Cytokine‐like Effects On Pmca In Glioblastoma Cell Lines, Enhancing Its Activity And Isoforms Expression
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