GO:0031234 extrinsic component of cytoplasmic side of plasma membrane: Components, Assembly and Research Methods, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0031234 describes proteins and protein complexes that are loosely bound to the cytoplasmic face of the plasma membrane without being integrated into the lipid bilayer.
• This extrinsic layer is experimentally defined by salt washing and sidedness assays that remove peripheral proteins while leaving integral membrane proteins embedded.
• The term is a cellular_component annotation that helps researchers distinguish peripheral membrane recruitment from transmembrane insertion.
• Proteins annotated to GO:0031234 often act as signaling scaffolds, cytoskeletal linkers, or redox-coupled peripheral factors.
• Loss of extrinsic membrane association can disrupt membrane-cytoskeleton coupling and downstream signaling, making this term relevant to disease modeling.
• CRISPR knockout, point-mutation, knock-in, and overexpression models are used to test whether candidate genes are causally required for extrinsic membrane localization.
Description
GO:0031234, extrinsic component of cytoplasmic side of plasma membrane, is a Gene Ontology cellular_component term that defines the subset of plasma membrane proteins and protein complexes that are loosely bound to the cytoplasmic surface but not integrated into the hydrophobic core of the bilayer. This annotation is important because it separates peripheral, reversibly associated factors from integral membrane proteins, a distinction that determines how a protein is regulated, how it can be experimentally released, and how it should be modeled in cells. The term is supported by classical biochemical evidence: sidedness measurements of isolated plasma membrane vesicles quantify exposure of peripheral proteins such as actin by DNase I inactivation, showing that extrinsic proteins can be selectively probed on the cytoplasmic face. Similarly, salt washing of photosynthetic membranes releases a 9-kDa extrinsic polypeptide without solubilizing integral components, establishing a general biochemical criterion for extrinsic membrane association. For researchers, GO:0031234 provides a controlled vocabulary for annotating proteins that dock onto the plasma membrane cytoplasmic leaflet, including signaling adaptors, cytoskeletal linkers, and peripheral redox or metabolic enzymes. Because these proteins are not transmembrane, their membrane association is often dynamic and sensitive to ionic strength, pH, and post-translational modification, making the term a useful anchor for experimental design in cell biology, neuroscience, and cancer research.
extrinsic component of cytoplasmic side of plasma membrane At A Glance
| GO ID | GO:0031234 |
|---|---|
| GO term | extrinsic component of cytoplasmic side of plasma membrane |
| Ontology | cellular_component |
| Synonym | extrinsic to cytoplasmic side of plasma membrane; extrinsic to internal leaflet of plasma membrane; extrinsic to internal side of plasma membrane |
| Definition | The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region. |
| Major function | Annotates peripheral proteins and complexes that associate reversibly with the cytoplasmic face of the plasma membrane to support signaling, cytoskeletal coupling, and membrane-associated biochemistry. |
| Experimental criterion | Extrinsic proteins are released by salt washing or chelation, whereas integral membrane proteins remain membrane-embedded. |
| Cellular context | Cytoplasmic leaflet of the plasma membrane in eukaryotic cells; relevant to membrane-cytoskeleton interfaces and signal transduction. |
| Related annotation use | Used to distinguish peripheral membrane recruitment from transmembrane domain-containing proteins in proteomics and imaging studies. |
What Is GO:0031234?
In plain terms, GO:0031234 describes the collection of gene products and protein complexes that sit on the cytoplasmic side of the plasma membrane but are not embedded in the membrane's hydrophobic interior. These are peripheral or extrinsic proteins that can be removed by treatments such as high salt or chelating agents, in contrast to integral membrane proteins that require detergents for extraction. The QuickGO definition specifies that the component consists of gene products and protein complexes loosely bound to the cytoplasmic surface, excluding proteins integrated into the hydrophobic region. This term is therefore a spatial and biochemical annotation: it tells you where a protein acts (cytoplasmic face of the plasma membrane) and how it is associated (extrinsic, not transmembrane).
Why Is extrinsic component of cytoplasmic side of plasma membrane Important in Cell Biology?
GO:0031234 matters because the cytoplasmic face of the plasma membrane is a major hub for signal transduction, cytoskeletal anchoring, and membrane trafficking, and many of the proteins that operate there are extrinsic rather than transmembrane. Correctly annotating these proteins as extrinsic components influences how researchers interpret biochemical fractionation, imaging, and proteomics data, and it guides the choice of CRISPR models for testing gene function. Because extrinsic association is often reversible, this term also captures a dynamic regulatory layer that can be disrupted in disease without mutations in transmembrane domains.
GO:0031234 extrinsic component of cytoplasmic side of plasma membrane
• Defines a distinct biochemical fraction of the plasma membrane that is released by salt washing, enabling clean separation from integral membrane proteins.
• Supports accurate annotation of peripheral signaling proteins that dock on the cytoplasmic leaflet without transmembrane domains.
• Provides a framework for studying membrane-cytoskeleton coupling, because peripheral actin and actin-binding proteins can be probed by sidedness assays.
• Helps interpret proteomics and imaging data by distinguishing extrinsic membrane association from transmembrane insertion.
• Relevant to redox and metabolic membrane-associated reactions, as shown by extrinsic polypeptides in photosynthetic membranes.
• Guides CRISPR experimental design by clarifying whether a candidate gene product is expected to be peripheral or integral.
• Connects to mitochondrial and chloroplast membrane biology, where extrinsic factors control processing and stability of membrane-associated complexes.
• Useful for disease modeling when loss of peripheral membrane recruitment, rather than catalytic inactivation, drives pathology.
What Happens During extrinsic component of cytoplasmic side of plasma membrane?
(未命名小节)
In simple terms: Proteins in this component are recruited to the cytoplasmic face of the plasma membrane, perform their function there, and can be released without destroying the membrane.
The biological process associated with GO:0031234 is not a single pathway but a spatial and biochemical state: gene products and complexes bind loosely to the cytoplasmic surface of the plasma membrane and act there. Classical sidedness measurements on isolated plasma membrane vesicles show that peripheral proteins such as actin are exposed on the cytoplasmic face and can be quantified by DNase I inactivation, providing a direct readout of extrinsic association. Salt washing experiments on photosynthetic membranes demonstrate that a 9-kDa extrinsic polypeptide can be specifically released without solubilizing integral membrane components, establishing a general principle that extrinsic proteins are held by electrostatic and hydrophobic interactions that are weaker than transmembrane anchoring. In cells, this state supports dynamic recruitment and release of signaling and cytoskeletal factors at the membrane-cytoplasm interface.
Assembly and Recruitment of Extrinsic Components
In simple terms: Extrinsic proteins find their way to the membrane through charge-based interactions and protein-protein contacts, not by being threaded through the lipid bilayer.
Assembly of the extrinsic component of the cytoplasmic side of the plasma membrane involves electrostatic interactions between basic residues or lipid-binding motifs and the negatively charged inner leaflet, as well as protein-protein contacts with integral membrane or cortical proteins. Because these interactions are not transmembrane, the assembly is reversible and sensitive to ionic strength, which is the basis for salt-wash release assays. Sidedness measurements of plasma membrane vesicles further show that the orientation of extrinsic proteins can be determined experimentally, allowing researchers to confirm that a protein is on the cytoplasmic rather than the extracellular face. In photosynthetic systems, extrinsic polypeptides such as the 9-kDa protein are assembled on the lumenal or cytoplasmic side depending on the membrane system, illustrating that extrinsic association is a general membrane-binding strategy.
Structure and Composition of extrinsic component of cytoplasmic side of plasma membrane
In simple terms: This component is made of peripheral proteins and complexes that sit on the membrane surface, often together with cortical cytoskeleton and signaling molecules.
The structure of the extrinsic component is defined by peripheral proteins and protein complexes that are not integrated into the hydrophobic region of the plasma membrane. These can include cytoskeletal proteins such as actin, which is exposed on the cytoplasmic face of isolated plasma membrane vesicles and can be quantified by DNase I inactivation. The composition is dynamic and can include signaling scaffolds, adaptors, and enzymes that are recruited from the cytosol. In related membrane systems, extrinsic polypeptides such as the 9-kDa photosystem I subunit are released by salt washing, confirming that extrinsic components can be isolated as a distinct biochemical fraction. Redox-dependent assembly of extrinsic factors has also been observed in photosynthetic membranes, where photoligation of manganese to the apo-water-oxidizing complex depends on redox conditions.
Molecular Mechanism of extrinsic component of cytoplasmic side of plasma membrane
In simple terms: The molecular mechanism is binding to the membrane surface through electrostatic and protein-protein interactions, often regulated by redox or metabolic state.
At the molecular level, extrinsic components bind to the cytoplasmic face of the plasma membrane through a combination of electrostatic interactions, hydrophobic patches, and specific protein-protein contacts, without crossing the bilayer. This mechanism is experimentally defined by the ability of salt washing to release extrinsic polypeptides while integral membrane proteins remain embedded. In photosynthetic membranes, the assembly of extrinsic manganese-stabilizing proteins is redox-dependent, showing that the binding of extrinsic factors can be controlled by the redox state of the membrane environment. Flash-induced fluorescence studies of photosystem II further demonstrate that events at the water-oxidizing complex, which involves extrinsic polypeptides, can be modulated by the redox state, linking extrinsic membrane association to catalytic activity. These principles are relevant to the plasma membrane cytoplasmic face, where redox and metabolic signals can regulate the recruitment of peripheral proteins.
Regulation and Dynamics of Extrinsic Membrane Association
In simple terms: Extrinsic proteins can come and go from the membrane, and their binding is controlled by signals such as ions, redox state, and protein modifications.
The association of extrinsic components with the cytoplasmic side of the plasma membrane is dynamic and regulated. Salt washing experiments show that extrinsic polypeptides can be released by changes in ionic strength, indicating that electrostatic interactions are a key regulatory node. Redox conditions control the photoligation of manganese to the apo-water-oxidizing complex in chloroplasts, demonstrating that extrinsic factor assembly can be redox-regulated. In yeast, overexpression of Rmd9p compensates for a partial deficiency of Oxa1p, a mitochondrial membrane protein, showing that extrinsic and membrane-associated factors can functionally interact and that their levels are genetically regulated. These examples illustrate that extrinsic membrane association is not a static annotation but a regulated state that can be probed by biochemical and genetic methods.
Key Genes Involved in GO:0031234 extrinsic component of cytoplasmic side of plasma membrane
The following genes and proteins are representative of the types of factors that can be annotated to or studied in the context of GO:0031234, based on the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ACTB | Actin is a peripheral cytoskeletal protein exposed on the cytoplasmic face of plasma membrane vesicles. | Used as a marker for sidedness assays and extrinsic membrane association. |
| PSI-9kDa | Extrinsic polypeptide of photosystem I released by salt washing. | Model for salt-dependent release of extrinsic membrane proteins. |
| OEC extrinsic proteins | Manganese-stabilizing extrinsic polypeptides of photosystem II. | Redox-dependent assembly and function of extrinsic membrane complexes. |
| RMD9 | Mitochondrial mRNA processing/stability factor; overexpression compensates for Oxa1p deficiency. | Genetic interaction between extrinsic and membrane-associated factors. |
| OXA1 | Mitochondrial inner membrane protein involved in insertion of membrane proteins. | Model for functional compensation by extrinsic factors. |
| HIF-1 signaling genes | Glycolysis/gluconeogenesis and HIF-1 pathways identified in proteomics/metabolomics. | Example of pathway-level analysis that can include membrane-associated proteins. |
| DNase I | Enzyme used to quantify actin exposure in plasma membrane vesicles. | Tool for measuring sidedness of extrinsic components. |
| Photosystem II core | Integral membrane complex whose extrinsic subunits are redox-regulated. | Model for studying extrinsic subunit assembly. |
| Photosystem I complex | Integral membrane complex with extrinsic 9-kDa subunit. | Model for salt-wash release of extrinsic polypeptides. |
| Water-oxidizing complex | Manganese cluster whose photoligation depends on redox state. | Model for redox-dependent extrinsic factor assembly. |
| Mitochondrial ribosome-associated factors | Factors controlling mitochondrial mRNA stability. | Link between extrinsic factors and organellar gene expression. |
| Cortical actin-binding proteins | Proteins that link actin to the plasma membrane cytoplasmic face. | Targets for studying membrane-cytoskeleton coupling. |
| Peripheral signaling adaptors | Proteins recruited to the cytoplasmic leaflet for signal transduction. | Candidate genes for CRISPR knockout and localization studies. |
| Redox-regulated peripheral proteins | Proteins whose membrane binding depends on redox state. | Models for point-mutation studies of redox-sensitive binding. |
| Salt-washable membrane proteins | Proteins released by high-salt treatment. | Biochemical fractionation markers for extrinsic components. |
| Fluorescence reporters of PSII | Readouts of events at the water-oxidizing complex. | Functional assays for extrinsic subunit activity. |
How Is extrinsic component of cytoplasmic side of plasma membrane Regulated?
Regulation of the extrinsic component of the cytoplasmic side of plasma membrane occurs at multiple levels. Ionic strength and electrostatic interactions control the reversible binding of peripheral proteins, as demonstrated by salt-wash release of extrinsic polypeptides. Redox state regulates the assembly of extrinsic manganese-stabilizing proteins in photosynthetic membranes, showing that post-translational and environmental signals can control extrinsic factor recruitment. Genetic regulation is illustrated by Rmd9p overexpression compensating for a partial deficiency of Oxa1p in yeast, indicating that levels of extrinsic or membrane-associated factors can be modulated to maintain function. In mammalian cells, signaling pathways such as HIF-1 and glycolysis/gluconeogenesis have been profiled in proteomics and metabolomics studies, providing a framework for understanding how metabolic state may influence membrane-associated protein composition.
extrinsic component of cytoplasmic side of plasma membrane and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ACTB | Membrane-cytoskeleton coupling; cell motility and shape | Knockout or tagged knock-in of ACTB to monitor extrinsic membrane localization |
| RMD9 | Mitochondrial mRNA processing and stability | Yeast overexpression and knockout to test compensation of Oxa1p deficiency |
| OXA1 | Mitochondrial membrane protein insertion | Point-mutation and knockout models to study functional interactions |
| HIF-1 pathway genes | Metabolic and hypoxic signaling | Proteomics and metabolomics profiling in animal models |
| Photosystem II extrinsic subunits | Redox-dependent assembly and oxidative stress | In vitro reconstitution and fluorescence assays |
Membrane-Cytoskeleton Disruption in Disease
Because GO:0031234 includes peripheral cytoskeletal proteins such as actin that are exposed on the cytoplasmic face of the plasma membrane, disruption of this extrinsic layer can affect cell shape, motility, and signaling. Sidedness assays that quantify actin exposure provide a biochemical readout that can be used to detect disease-associated changes in membrane-cytoskeleton coupling. While the verified literature does not directly link GO:0031234 to a specific human disease, the experimental framework is relevant to cancers and developmental disorders where membrane-cytoskeleton interactions are altered.
Redox-Dependent Extrinsic Factors and Oxidative Stress
Redox-dependent assembly of extrinsic factors, such as the manganese-stabilizing polypeptides of photosystem II, demonstrates that extrinsic membrane components can be sensitive to oxidative conditions. In human cells, similar redox-sensitive peripheral proteins may be affected by oxidative stress, although direct disease links for GO:0031234 require further study. The concept that extrinsic factor assembly is redox-regulated provides a mechanistic hypothesis for how oxidative stress could alter membrane-associated signaling.
Mitochondrial and Organellar Membrane Biology
The genetic interaction between Rmd9p and Oxa1p in yeast shows that extrinsic and membrane-associated factors cooperate in mitochondrial function, and their dysfunction can impair organellar gene expression. This provides a model for understanding how mutations in extrinsic or membrane-associated factors might contribute to mitochondrial disease, although the verified literature does not establish a direct human disease link for GO:0031234. Researchers can use this yeast model to dissect functional compensation and synthetic phenotypes.
Metabolic and Signaling Pathway Integration
Proteomics and metabolomics studies of glycolysis/gluconeogenesis and HIF-1 signaling in rats with dental fluorosis identified pathway-level changes that can include membrane-associated proteins. Although this study does not directly annotate GO:0031234, it illustrates how systemic metabolic perturbations can be analyzed for effects on membrane-associated protein networks. Such integrated approaches can be adapted to study extrinsic membrane components in other disease contexts.
From extrinsic component of cytoplasmic side of plasma membrane-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate gene product a peripheral or integral membrane protein? | Biochemical fractionation with salt washing and sidedness assays |
| Does loss of a gene disrupt extrinsic membrane association? | CRISPR knockout followed by membrane fractionation and imaging |
| Does a specific residue control membrane binding? | CRISPR point mutation of candidate basic or hydrophobic residues |
| Can a tagged version of the protein report its membrane localization? | Knock-in of an epitope or fluorescent tag |
| Does overexpression of a factor compensate for a membrane protein deficiency? | Overexpression in yeast or mammalian cells |
| Is extrinsic factor assembly redox-regulated? | Redox perturbation and photoligation assays |
How to Study the extrinsic component of cytoplasmic side of plasma membrane Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Sidedness assay with DNase I | Exposure of actin on the cytoplasmic face of plasma membrane vesicles | Confirm extrinsic localization of peripheral proteins |
| Salt washing | Release of extrinsic polypeptides from membranes | Biochemical definition of extrinsic components |
| Proteomics | Protein composition of membrane fractions | Identify membrane-associated pathway changes |
| Metabolomics | Metabolic pathway activity | Integrate with proteomics to study membrane-associated metabolism |
| Flash-induced fluorescence | Events at the water-oxidizing complex | Assay extrinsic subunit function in photosynthesis |
| Redox photoligation assay | Manganese assembly in the water-oxidizing complex | Study redox-dependent extrinsic factor assembly |
| Genetic overexpression | Functional compensation between factors | Test interactions between extrinsic and membrane proteins |
| CRISPR knockout | Loss-of-function phenotype | Determine requirement for extrinsic membrane association |
Biochemical Fractionation and Sidedness Assays
The classical method to study GO:0031234 is isolation of plasma membrane vesicles followed by sidedness measurements, such as DNase I inactivation to quantify actin exposure on the cytoplasmic face. Salt washing is used to release extrinsic polypeptides while integral membrane proteins remain embedded, providing a biochemical criterion for extrinsic association. These methods are essential for validating whether a protein of interest belongs to the extrinsic component.
Proteomics and Metabolomics
Proteomics and metabolomics can profile membrane-associated protein fractions and identify pathways that co-vary with extrinsic component changes. In a rat model of dental fluorosis, integrated proteomics and metabolomics revealed changes in glycolysis/gluconeogenesis and HIF-1 signaling, demonstrating the power of multi-omics to detect membrane-associated pathway shifts. Similar workflows can be applied to cells with CRISPR edits in candidate genes.
Fluorescence and Redox Assays
Flash-induced photosystem II fluorescence can report events at the water-oxidizing complex, which involves extrinsic polypeptides, and can be modulated by redox conditions. Redox-dependent photoligation of manganese to the apo-water-oxidizing complex provides a direct assay for extrinsic factor assembly. These approaches are useful for studying redox-sensitive extrinsic membrane components in model systems.
Genetic Interaction and Compensation Studies
Overexpression of Rmd9p compensates for a partial deficiency of Oxa1p in Saccharomyces cerevisiae, illustrating how genetic interaction studies can reveal functional relationships between extrinsic and membrane-associated factors. Such experiments can be combined with CRISPR knockout or point mutation in mammalian cells to test conservation of mechanism.
How CRISPR Can Be Used to Study GO:0031234 extrinsic component of cytoplasmic side of plasma membrane
Knockout
CRISPR knockout of a candidate gene can test whether its product is required for the extrinsic component of the cytoplasmic side of the plasma membrane. After knockout, researchers can perform salt washing and sidedness assays to determine whether the extrinsic protein fraction is depleted. This approach is particularly useful for distinguishing essential peripheral factors from redundant ones.
Point Mutation
Point mutations can be introduced to test specific residues predicted to mediate electrostatic or hydrophobic interactions with the cytoplasmic leaflet. For example, mutating basic residues in a peripheral protein may reduce salt-wash resistance and alter membrane localization. Such experiments help define the molecular determinants of extrinsic membrane association.
Knock-in
Knock-in of fluorescent or epitope tags allows direct visualization and biochemical isolation of extrinsic components. Tagged proteins can be used in imaging and co-immunoprecipitation to confirm their presence on the cytoplasmic face of the plasma membrane. This approach is valuable for tracking dynamic recruitment and release.
Overexpression
Overexpression of a candidate gene can test whether increased levels of an extrinsic factor compensate for deficiency of a membrane-associated partner, as shown for Rmd9p and Oxa1p. Overexpression models are also useful for producing sufficient material for biochemical assays of extrinsic membrane association.
How EDITGENE Supports extrinsic component of cytoplasmic side of plasma membrane Research
Researchers studying extrinsic component of cytoplasmic side of plasma membrane-related genes often need to determine whether a candidate gene is causally involved in membrane association, signaling, or disease phenotypes. EDITGENE provides CRISPR-based cell models and screening services to test these hypotheses with rigor and reproducibility.
Contact EDITGENE today to design your custom CRISPR model for extrinsic component of cytoplasmic side of plasma membrane research.
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Frequently Asked Questions About extrinsic component of cytoplasmic side of plasma membrane
What is GO:0031234?
GO:0031234 is a Gene Ontology cellular_component term for the extrinsic component of the cytoplasmic side of the plasma membrane, comprising proteins and complexes loosely bound to the cytoplasmic surface but not integrated into the hydrophobic region.
What does extrinsic component of cytoplasmic side of plasma membrane mean?
It means the set of proteins that associate reversibly with the cytoplasmic face of the plasma membrane without being transmembrane, and can be released by salt washing.
What genes are involved in extrinsic component of cytoplasmic side of plasma membrane?
Genes encoding peripheral cytoskeletal proteins such as actin, signaling adaptors, and redox-regulated factors can be annotated to this term, as illustrated by actin sidedness assays and salt-washable polypeptides.
How is GO:0031234 studied experimentally?
Common methods include plasma membrane vesicle isolation, DNase I inactivation for actin exposure, salt washing to release extrinsic proteins, and fluorescence assays for redox-dependent assembly.
What is the difference between extrinsic and integral membrane proteins?
Extrinsic proteins are loosely bound to the membrane surface and can be released by salt washing, whereas integral membrane proteins are embedded in the hydrophobic region and require detergents for extraction.
Why is the cytoplasmic side of the plasma membrane important?
The cytoplasmic face is a hub for signal transduction and cytoskeletal coupling, and many peripheral signaling proteins act there without being transmembrane.
Can CRISPR be used to study extrinsic membrane components?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression can test whether specific genes and residues are required for extrinsic membrane association.
What diseases are linked to extrinsic component of cytoplasmic side of plasma membrane?
Direct disease links are not established in the verified literature, but disruption of membrane-cytoskeleton coupling and redox-dependent extrinsic factors is relevant to cancer, oxidative stress, and mitochondrial biology.
What is an example of a salt-washable extrinsic membrane protein?
A 9-kDa extrinsic polypeptide of photosystem I can be specifically released from spinach chloroplasts by salt washing.
How does redox state affect extrinsic membrane components?
Redox conditions control the photoligation of manganese to the apo-water-oxidizing complex, demonstrating redox-dependent assembly of extrinsic factors.
Conclusion
GO:0031234 provides a precise annotation for proteins and complexes that associate extrinsically with the cytoplasmic face of the plasma membrane. This term is grounded in classical biochemical criteria such as salt washing and sidedness assays, and it remains essential for interpreting membrane proteomics, imaging, and functional studies. By combining CRISPR models with biochemical and multi-omics readouts, researchers can determine how extrinsic membrane components contribute to signaling, cytoskeletal coupling, and disease-relevant phenotypes.
References
- 1. Grinstein S et al.. 1983. Measurement of sidedness of isolated plasma-membrane vesicles: quantitation of actin exposure by DNase I inactivation.. Anal Biochem 130(1):151-7 PMID: 6223539
- 2. He WZ et al.. 1992. Specific release of a 9-kDa extrinsic polypeptide of photosystem I from spinach chloroplasts by salt washing.. FEBS Lett 308(3):298-300 PMID: 1505669
- 3. Ba Y et al.. 2022. Role of Glycolysis/Gluconeogenesis and HIF-1 Signaling Pathways in Rats with Dental Fluorosis Integrated Proteomics and Metabolomics Analysis.. Int J Mol Sci 23(15) PMID: 35897842
- 4. Tamura N et al.. 1997. Redox dependence for photoligation of manganese to the apo-water-oxidizing complex in chloroplasts and photosystem II membranes.. Biochemistry 36(20):6171-7 PMID: 9166789
- 5. Nouet C et al.. 2007. Rmd9p controls the processing/stability of mitochondrial mRNAs and its overexpression compensates for a partial deficiency of oxa1p in Saccharomyces cerevisiae.. Genetics 175(3):1105-15 PMID: 17194787
- 6. Putrenko II et al.. 1999. Modulation of flash-induced photosystem II fluorescence by events occurring at the water oxidizing complex.. Biochemistry 38(33):10632-41 PMID: 10451357
