Investigating the molecular mechanisms of protein deCoAlation
Lead Research Organisation:
University College London
Department Name: Structural Molecular Biology
Abstract
Coenzyme A (CoA) is essential for all living cells. In 1953, F. Lipmann received a Nobel prize for the discovery of CoA and its importance in intermediary metabolism. Since this landmark discovery, numerous functions of CoA and its derivatives (Acetyl CoA, Malonyl CoA, HMG CoA among others) have been revealed, including their significance in the synthesis and oxidation of fatty acids, ATP production, biosynthesis of cholesterol and acetylcholine, degradation of amino acids and the regulation of gene expression and cellular metabolism via protein acetylation. Dysregulation of CoA biosynthesis or CoA derivatives homoeostasis is associated with various human pathologies, including metabolic disorders, cardiac hypertrophy, cancer and neurodegeneration.
Prof Gout's research was central to molecular cloning and characterisation of mammalian CoA synthase, and the identification of mutations in this enzyme associated with an aggressive form of a Parkinson's-like neurodegeneration (NBIA, neurodegeneration with brain iron accumulation). Recently, Prof Gout pioneered a new field of research on protein CoAlation and antioxidant function of CoA. He has initiated and led a high profile international consortium on this emerging and significant area of research. These collaborative efforts were essential for demonstrating that protein CoAlation is a reversible post-translational modification induced in bacteria and mammalian cells by oxidising agents and metabolic stress. In the frame of the established consortium, unique reagents and methodologies have been developed and proved to be critical for identifying CoA-modified proteins in cells and tissues, and revealing a widespread nature of protein CoAlation. Protein CoAlation was shown to regulate the subcellular localisation, enzymatic activity and function of modified proteins. The identification of extensive protein CoAlation in eukaryotic and prokaryotic cells, and the reversible nature of this post-translational modification suggest there should also be enzymes which function to mediate the removal of CoA from modified proteins. We have termed these enzymes CoAredoxins. This research proposal leverages novel findings and newly developed methodologies, and will further advance the field of research on protein CoAlation and define the role of CoA as an important antioxidant in cellular response to oxidative and metabolic stress. Key research questions are aimed at: i) the identification and functional characterisation of CoAredoxins from bacteria and mammalian cells; and (ii) the development of novel research tools and methodologies for studying protein CoAlation in redox regulation and signalling. Answering these questions will reveal the molecular basis of protein deCoAlation and thus inform on the fundamental biology of CoA in cellular metabolism and redox regulation. This work will lay the foundation for delineating the role of protein CoAlation in health and disease.
Prof Gout's research was central to molecular cloning and characterisation of mammalian CoA synthase, and the identification of mutations in this enzyme associated with an aggressive form of a Parkinson's-like neurodegeneration (NBIA, neurodegeneration with brain iron accumulation). Recently, Prof Gout pioneered a new field of research on protein CoAlation and antioxidant function of CoA. He has initiated and led a high profile international consortium on this emerging and significant area of research. These collaborative efforts were essential for demonstrating that protein CoAlation is a reversible post-translational modification induced in bacteria and mammalian cells by oxidising agents and metabolic stress. In the frame of the established consortium, unique reagents and methodologies have been developed and proved to be critical for identifying CoA-modified proteins in cells and tissues, and revealing a widespread nature of protein CoAlation. Protein CoAlation was shown to regulate the subcellular localisation, enzymatic activity and function of modified proteins. The identification of extensive protein CoAlation in eukaryotic and prokaryotic cells, and the reversible nature of this post-translational modification suggest there should also be enzymes which function to mediate the removal of CoA from modified proteins. We have termed these enzymes CoAredoxins. This research proposal leverages novel findings and newly developed methodologies, and will further advance the field of research on protein CoAlation and define the role of CoA as an important antioxidant in cellular response to oxidative and metabolic stress. Key research questions are aimed at: i) the identification and functional characterisation of CoAredoxins from bacteria and mammalian cells; and (ii) the development of novel research tools and methodologies for studying protein CoAlation in redox regulation and signalling. Answering these questions will reveal the molecular basis of protein deCoAlation and thus inform on the fundamental biology of CoA in cellular metabolism and redox regulation. This work will lay the foundation for delineating the role of protein CoAlation in health and disease.
Technical Summary
Coenzyme A (CoA) is a key metabolic integrator in mammalian cells. CoA and its thioester derivatives participate in diverse metabolic pathways, regulatory interactions and gene expression. Dysregulation of CoA biosynthesis or CoA derivatives homeostasis has been associated with various human pathologies, including cancer, diabetes and neurodegeneration. We have recently uncovered a novel non-canonical function of CoA, involving covalent modification of cellular proteins in redox regulation and termed it protein CoAlation. The development of new reagents and methodologies allowed us to demonstrate that protein CoAlation is a widespread and reversible post-translational modification which occurs in eukaryotic and prokaryotic cells in response to oxidative and metabolic stress. The vast majority of CoAlated proteins were found to be metabolic enzymes, as well as proteins implicated in stress response and protein synthesis. Protein CoAlation alters the molecular mass, charge and the activity of modified proteins, and prevents them from irreversible sulfhydryl overoxidation.
This research proposal will further exploit these recent advances to address fundamental questions about the molecular mechanisms of the CoAlation/deCoAlation cycle in redox regulation. Based on our preliminary data we hypothesise that the removal of CoA from CoAlated proteins is an enzymatically-mediated process, occurring when cells recover from oxidative or metabolic stress. The identification and functional characterisation of these enzymes, which we termed CoAredoxins will be the main focus of this proposal. We will also extend a range of new research tools and methodologies for studying protein CoAlation in redox regulation and signalling. The work will provide critical information for understanding the molecular mechanisms of protein deCoAlation and the role of CoA in balancing oxidative stress, redox state and cellular metabolism in health and disease.
This research proposal will further exploit these recent advances to address fundamental questions about the molecular mechanisms of the CoAlation/deCoAlation cycle in redox regulation. Based on our preliminary data we hypothesise that the removal of CoA from CoAlated proteins is an enzymatically-mediated process, occurring when cells recover from oxidative or metabolic stress. The identification and functional characterisation of these enzymes, which we termed CoAredoxins will be the main focus of this proposal. We will also extend a range of new research tools and methodologies for studying protein CoAlation in redox regulation and signalling. The work will provide critical information for understanding the molecular mechanisms of protein deCoAlation and the role of CoA in balancing oxidative stress, redox state and cellular metabolism in health and disease.
Planned Impact
The main benefit of the proposed project relates to the advance of knowledge of the role protein CoAlation in redox regulation and antioxidant function of coenzyme A, which will be disseminated through peer-reviewed journals, national and international conferences, and free-to-access websites. The project has the potential to generate a diverse range of research reagents and technical expertise, and we make it freely available in order to stimulate the research in this field. Considering that protein CoAlation is an emerging field of research, we believe that the identification and characterisation of deCoAlation enzymes (CoAredoxins) will advance our knowledge on molecular mechanisms of the CoAlation/deCoAlation cycle in redox regulation. Moreover, the proposed research can also contribute to a better understanding of the antioxidant function of CoA in health and disease, and the development of better treatment for pathologies in which deregulation of CoA biosynthesis and homeostasis is implicated, including diabetes, cancer and neurodegeneration with brain iron accumulation (NBIA). Where possible, we will feed findings from the proposed study into our ongoing drug discovery project on ""Utilising coenzyme A scaffold for the development of Aurora kinase A specific inhibitors", aimed at developing novel anticancer drugs. The proposed work therefore has the potential to boost the development of novel therapeutic drugs in the long-term, as well as fostering positive economic outcomes, considering the rapidly growing global pharmaceutical market for protein kinase inhibitors. A diverse range of techniques, including biochemical and molecular biology techniques, bacterial and baculoviral expression of recombinant proteins, lentiviral overexpression and downregulation, mammalian cell biology, in vitro CoAlation assay, mass spectrometry analysis, generation and characterisation of site-specific CoAlation antibodies will be carried out in the frame of this project. Therefore, it offers an excellent opportunity for the staff involved in this project, including undergraduate and postgraduate students, to gain a valuable experience in modern techniques. In addition, effective time-management, co-ordination and communication skills will therefore be critical for successful completion of this multidisciplinary project.
People |
ORCID iD |
Ivan Gout (Principal Investigator) |
Publications
Bakovic J
(2019)
A key metabolic integrator, coenzyme A, modulates the activity of peroxiredoxin 5 via covalent modification.
in Molecular and cellular biochemistry
Tossounian M
(2023)
A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of Human Metastasis Suppressor NME1
in International Journal of Molecular Sciences
Zhyvoloup A
(2020)
Analysis of disulphide bond linkage between CoA and protein cysteine thiols during sporulation and in spores of Bacillus species.
in FEMS microbiology letters
Tossounian MA
(2023)
Bacillus subtilis YtpP and Thioredoxin A Are New Players in the Coenzyme-A-Mediated Defense Mechanism against Cellular Stress.
in Antioxidants (Basel, Switzerland)
Petrone O
(2023)
Changes of the Protein CoAlation Pattern in Response to Oxidative Stress and Capacitation in Human Spermatozoa.
in International journal of molecular sciences
Aloum L
(2019)
Coenzyme A and protein CoAlation levels are regulated in response to oxidative stress and during morphogenesis in Dictyostelium discoideum.
in Biochemical and biophysical research communications
Gout I
(2019)
Coenzyme A: a protective thiol in bacterial antioxidant defence.
in Biochemical Society transactions
Tsuchiya Y
(2020)
Covalent Aurora A regulation by the metabolic integrator coenzyme A.
in Redox biology
Bellany F
(2020)
Design and synthesis of Coenzyme A analogues as Aurora kinase A inhibitors: An exploration of the roles of the pyrophosphate and pantetheine moieties.
in Bioorganic & medicinal chemistry
Filonenko V
(2023)
Discovery and functional characterisation of protein CoAlation and the antioxidant function of coenzyme A.
in BBA advances
Lashley T
(2021)
Extensive Anti-CoA Immunostaining in Alzheimer's Disease and Covalent Modification of Tau by a Key Cellular Metabolite Coenzyme A.
in Frontiers in cellular neuroscience
Tossounian MA
(2022)
Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions.
in Antioxidants (Basel, Switzerland)
Bakovic J
(2021)
Redox Regulation of the Quorum-sensing Transcription Factor AgrA by Coenzyme A.
in Antioxidants (Basel, Switzerland)
Yu BYK
(2021)
Regulation of metastasis suppressor NME1 by a key metabolic cofactor coenzyme A.
in Redox biology
Bakovic J
(2021)
Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells.
in International journal of molecular sciences
Tossounian MA
(2020)
The Writers, Readers, and Erasers in Redox Regulation of GAPDH.
in Antioxidants (Basel, Switzerland)
Ahmed A
(2018)
Three-dimensional cancer cell culture in high-yield multiscale scaffolds by shear spinning
in Biotechnology Progress
Description | Protein deCoAlation was shown to be a widespread and reversible post-translational modification. DeCoAlase activity was detected at high level in cells recovering from oxidative or metabolic stress. The purification of CoAredoxin's activities has been carrried out from bacteria and rat liver using several chromatographic approaches. Purified samples were analysed by mass spectrometry by our collaborator at MRC LMB in Cambridge, Dr. M. Skehel. These studies allowed us to identified 5 potential CoAredoxins in bacteria. Further studies revealed that two identified proteins exhibit deCoAlation activity in vitro and in cells. Because the complexity of mammalian genome, the identification of potential CoAredoxins purified from the rat liver is slightly behind the schedule. This delay is also associated with the reduced research activity during Covid 19 pandemic. |
Exploitation Route | The identification of CoAredoxins (deCoAlation enzymes) will allow to advance our knowledge on the role of CoAlation in health and disease. It will also allow the development a readout assay for measuring the stoichiometry of protein CoAlation in cells and tissues. This assay will be avialabe for researcher working in the field of protein CoAlation. |
Sectors | Healthcare |
Description | Investigating the role of protein CoAlation and the antioxidant function of coenzyme A in Parkinson's disease |
Amount | £72,970 (GBP) |
Funding ID | RaR\100514 |
Organisation | The British Academy |
Sector | Academic/University |
Country | United Kingdom |
Start | 03/2023 |
End | 03/2025 |
Title | HEK293/PRDX6 KO cell line |
Description | We ahve recently developed HEK293 and HEK293/Pank1b cell lines with the CRISPR-mediated knock out of peroxiredoxin 6. |
Type Of Material | Cell line |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | Generated HEK293 and HEK293/Pank1b cell lines with the CRISPR-mediated knock out of PRDX6 will be used for studyin the role of this peroxiredoxin in ferroptosis. |
Title | IHC analysis of protein CoAlation in cancer and liver cirrhosis |
Description | We have generated anti-CoA mAb which work well in various immunological assays including IHC (to date, there are no anti-CoA antibodies on the market). In collaboration with Prof. R. Golding at Imperial College, we have established a reliable protocol for the IHC analysis of protein CoAlation in hepatocellular carcinoma and liver cirrhosis. |
Type Of Material | Technology assay or reagent |
Year Produced | 2021 |
Provided To Others? | No |
Impact | This methodology allowed us to demonstrate extensive protein CoAlation in samples of human hepatocellular carcinoma as well as liver cirrhosis, when compared to control liver samples. We are now expending this novel finding to the analysis of CoAlated proteins in HCC by mass spectrometry. |
Title | Immunohistochemical analysis of protein CoAlation in neurodegenerative pathologies |
Description | An efficient IHC analysis has been developed in collaboration with Dr. T. Lashley (Director, UCL Brain Bank) for the analysis of protein CoAlation in brain samples from patients with neurodegenerative pathologies. This methodology relies on the use of in-house developed anti-CoA monoclonal antibodies. To our knowledge, anti-CoA antibodies are not commercially available. |
Type Of Material | Technology assay or reagent |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | Extensive protein CoAlation in brain samples from patients with neurodegenerative pathologies, especially in Alzheimer's disease, was observed. This study allowed us to demonstrate that tau protein is CoAlated and the site of CoAlation was mapped by mass spectrometry. This knowldge may allow the development of novel diagnostic and/or therapeutic approaches for Alzheimer's disease. |
Title | In vitro CoAlation assay |
Description | We have established a reliable in vitro CoAlation assay, which allows the analysis of CoA-modified proteins (CoAlation). |
Type Of Material | Model of mechanisms or symptoms - in vitro |
Year Produced | 2018 |
Provided To Others? | Yes |
Impact | This methodology allows researchers to test whether their proteins of interst are CoAlated (covalent modification) in vitro and to study its effect on the function of CoA-modified proteins. |
Title | In vitro deCoAlation assay |
Description | This assay allows the analysis of enzymatic deCoAlation (removal of CoA from CoAlated proteins) in vitro and to study the functional consequences. |
Type Of Material | Technology assay or reagent |
Year Produced | 2020 |
Provided To Others? | Yes |
Impact | This methodology allows the analysis of enzymes which have the potential to remove CoA from covalently modified proteins. We term these proteins CoAredoxins and our efforts are currenlty focused on their molecular identification and characterisation. The identity of CoAredoxins may provide the knowledge for their function in health and disease, and targeting them for drug discovery. |
Title | Methodology for the identification of CoAlated proteins |
Description | Developed a reliable methodology for the identification of CoAlated proteins in cells and tissues |
Type Of Material | Technology assay or reagent |
Year Produced | 2017 |
Provided To Others? | No |
Impact | This novel methodology has already allowe us to identify over 2200 CoAlated proteins from prokaryotic and eukaryotic cells. |
Title | Protein CoAlation dataset |
Description | We have identified a novel PTM, termed protein CoAlation. Using the developed MS-based methodology, we have identified over 2100 CoAlated proteins in mammalian cells/tissues and bacteria. The dataset contains all CoAlated peptides and modified proteins. |
Type Of Material | Database/Collection of data |
Year Produced | 2022 |
Provided To Others? | Yes |
Impact | New collaborative interactions have been established |
Description | Analysis of protein CoAlation and the antioxidnat fucntion of CoA by Mass spectrometry |
Organisation | Medical Research Council (MRC) |
Department | MRC Laboratory of Molecular Biology (LMB) |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | During the reporting period, we have provided samples of CoAlated proteins from procaryotic (bacteria), mammalian cells lines. In addition, we sent smaples of endogenous and recombinant proteins modifiied by CoA using the in vitro CoAlation assay. |
Collaborator Contribution | Mass spectrometry analysis of in vitro and in vivo CoAlated and CoA binding proteins |
Impact | In the frame of this collaborative interaction, more than 2200 proteins have been identified to be CoAlated in prokaryotic and eukraryotic cells. |
Start Year | 2014 |
Description | Analysis of the CoAlation/deCoAlation cycle |
Organisation | Friedrich-Alexander University Erlangen-Nuremberg |
Country | Germany |
Sector | Academic/University |
PI Contribution | In 2021, we established collaborative interaction with Dr. M. Filipovic on studying the molecular mechanisms of protein CoAlation. To date, we have found that the activity of peroxidase 6 (Prdx6) is regulated by CoA and H2S. This study defines Prdx6 as a first CoA-dependent peroxidase. |
Collaborator Contribution | Dr. M. Filipovic has an extensive expertise in studying the role of H2S in redox regulation. The research in his laboratory confirmed our preliminary findings that the function of Prdx6 is regulated by CoA and H2S under oxidative stress. |
Impact | Yes, it is a multidisciplinary collaboration, involving the analysis of Prdx6 CoAlation and the role of H2S in this process by biochemical and biophysical approaches, including mass spectrometry. The research in his laboratory confirmed our preliminary findings that the function of Prdx6 is regulated by CoA and H2S under oxidative stress. |
Start Year | 2021 |
Description | Elucidation of protein CoAlation in neurodegenerative pathologies |
Organisation | Utrecht Life Sciences |
Country | Netherlands |
Sector | Public |
PI Contribution | In collaboration with Prof. T. Lashley we demonstrated significantly increased protein CoAlation in post-mortem brain samples of numerous neurodegenerative diseases, which appeared particularly frequent in Alzheimer's disease. We also found that protein CoAlation consistently co-localized with tau-positive neurofibrillary tangles, underpinning one of the key pathological hallmarks of Alzheimer's disease. Furthermore, CoAlation of tau protein was demonstrated in vitro and in vivo, and the site of covalent binding of CoA was mapped by mass spectrometry to conserved Cys322, located in the microtubule binding region. |
Collaborator Contribution | Prof. T. Lashley is the Director of the UCL Brain Bank and the research in her laboratory allowed us to examine by immunohistochemistry analysis with the in-house developed anti-CoA mAb the pattern of protein CoAlation in post-mortem brain samples of various neurodegenerative pathologies and matched controls. |
Impact | The outcome of this study was published in Frontiers of Neuroscience in 2021. This study has been a multi-disciplinary collaboration which involved six research laboratories from UK and abroad with the research expertise in cell and molecular biology, biochemistry and biophysics. |
Start Year | 2020 |
Description | Regulation of S6Ks by CoAlation (covalent modification by coenzyme A) |
Organisation | University of Cambridge |
Country | United Kingdom |
Sector | Academic/University |
PI Contribution | Dr. O. Pardo and Prof. M. Seckl, Imperial College London We examined the regulation of S6Ks in cellular response to oxidative and metabolic stress. These studies revealed the role of coenzyme A in the regulation of S6K under oxidative stress, mediated by covalent modification of the cysteine residue in the catalytic pocket of S6K by CoA. |
Collaborator Contribution | The site of S6K CoAlation (covalent modification by CoA) was mapped to Cys216 and Cys217 in S6K2 and S6K1 respectively. We showed that CoAlation occurs in vitro and in vivo, inhibits the activity of S6Ks. |
Impact | This is a multidisciplinary collaborative interaction, involving biochemistry, biophysics and cell biology. We are currently investigating the role of CoAlation in the function of S6Ks in vitro and in vivo. |
Start Year | 2019 |
Description | 7th international symposium on NBIA & related disorders |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Professional Practitioners |
Results and Impact | It was a virtual symposium which took place from 30th Sep until 3rd Oct 2020. I gave a lecture at this meeting on the topic of our research. |
Year(s) Of Engagement Activity | 2021 |
URL | https://nbiascientificsymposium.org/ |
Description | A joint Biochemical Society and BSRA Scientific Conference on Redox regulation in physiology and diseases, Newcastle, 1-3 Jul 2019 |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Professional Practitioners |
Results and Impact | Gave a lecture on "Redox regulation by coenzyme A in mammalian cells". More than 200 researchers attended this conference, so there were many question about my presentation and queries about collaborative research |
Year(s) Of Engagement Activity | 2019 |
Description | Biochemical Society Focused Meeting "Neglected Thiols: Redox Biology and Signalling", online, 7-9 Dec 2020 |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Professional Practitioners |
Results and Impact | More than 80 researchers particiapted in the Biochemical Society Focused Meeting "Neglected Thiols: Redox Biology and Signalling". Prof. B. Halliwell and me organised this meeting. I also presented our research on protein CoAlation and the antioxidant function of CoA at this meeting. |
Year(s) Of Engagement Activity | 2020 |
URL | https://www.google.co.uk/search?q=Biochemical+Society+Focused+Meeting+Neglected+Thiols:+Redox+Biolog... |
Description | Invited speaker and a conference session chair, SFRR-E conference |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Study participants or study members |
Results and Impact | I gave a talk on the topic of my research, which was well received by the audience. One collaborative interaction was established after this meeting. |
Year(s) Of Engagement Activity | 2021 |
Description | Invited speaker, Cancer Metastasis Conference |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Professional Practitioners |
Results and Impact | International conference " Cancer metastasis", Austria, 13-17 December 2021 Presented our resent findings on the antioxidant function of CoA and protein CoAlation in normal and cancer cells. New collaborative interactions were initiated after this conference. |
Year(s) Of Engagement Activity | 2021 |
Description | Invited speaker, Imperial College London seminar |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | National |
Primary Audience | Professional Practitioners |
Results and Impact | I gave a talk on the topic of my research, which was well received by the audience. It was also a good opportunity to discuss the options for advancing established collaborative interactions with Dr. O. Pardo and Prof. R. Golding (Imperial College). |
Year(s) Of Engagement Activity | 2022 |
Description | Invited speaker, Insitute of Ageing, UCL |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | National |
Primary Audience | Professional Practitioners |
Results and Impact | Presented our recent findings on the antioxidant function of CoA and protein CoAlation in health and disease. It was also a good opportunity to discuss the prospect for collaborative interactions with members of the Institute of Ageing. |
Year(s) Of Engagement Activity | 2021 |
Description | Invited speaker, University of Toronto |
Form Of Engagement Activity | Participation in an activity, workshop or similar |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Professional Practitioners |
Results and Impact | I gave a talk on the topic of my research, which was well received by the audience. It was also a good opportunity to discuss the options for establishing collaborative interactions with Prof. T. Mak. |
Year(s) Of Engagement Activity | 2022 |
Description | Japan-Aston symposium "Inflammation and oxidative stress", 23 Aug 2019, University of Birmingham |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | International |
Primary Audience | Professional Practitioners |
Results and Impact | Gave a talk on the emerging role of protein CoAlation and antioxidant function of CoA in health and disease. It was very well received with many questions and the request for developed reagents and a methodology for the identification of CoAlated proteins. |
Year(s) Of Engagement Activity | 2019 |
Description | London Bacteriology meeting, Imperial College |
Form Of Engagement Activity | A talk or presentation |
Part Of Official Scheme? | No |
Geographic Reach | National |
Primary Audience | Professional Practitioners |
Results and Impact | Presented our recent findings on "Antioxidant function of coenzyme A in bacteria". There were numerous questions after the talk and the prospects of collaborative interactions were discussed |
Year(s) Of Engagement Activity | 2020 |