21 results on '"Wilkins, Oscar G."'
Search Results
2. Identifying and rectifying aberrant RNA metabolism in amyotrophic lateral sclerosis
- Author
-
Wilkins, Oscar G.
- Abstract
Amyotrophic lateral sclerosis is a devastating and incurable disease. Despite decades of work, its cause is yet to be fully understood, and we lack effective treatments. There is therefore a great need for further research on the mechanisms which drive disease to help guide new drug development. In this thesis, I describe work spanning from the development of new techniques and software to aid the fundamental study of RNA biology, to the identification of a novel disease mechanism in ALS that should be straightforward to target therapeutically, and the development of a new precision medicine approach that could enable safer and more efficacious gene therapy for this disease. In the first chapter, I outline three short projects: 1. The development of software for the processing of fastq files with inline barcodes and UMIs; 2. A streamlined computational and experimental method for the removal of rRNA sequences from sequencing libraries, and 3. Several related protocols for the production of various RNA sequencing library types, all of which involve template-switching. In the second chapter, I describe how I helped characterise and validate a novel cryptic exon in UNC13A using a variety of wet- and dry-lab-based approaches. Furthermore, I describe how I designed and tested candidate therapeutic antisense oligonucleotides to rescue this splicing abnormality, and how I developed a protocol for detecting large numbers of cryptic exons in parallel. Finally, in the third chapter, I describe the development of software to design expression vectors which are activated by the depletion of TDP-43, potentially paving the way towards safer and more efficacious gene therapy for ALS and related diseases.
- Published
- 2023
3. TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A
- Author
-
Brown, Anna-Leigh, Wilkins, Oscar G, Keuss, Matthew J, Hill, Sarah E, Zanovello, Matteo, Lee, Weaverly Colleen, Bampton, Alexander, Lee, Flora CY, Masino, Laura, Qi, Yue A, Bryce-Smith, Sam, Gatt, Ariana, Hallegger, Martina, Fagegaltier, Delphine, Phatnani, Hemali, Newcombe, Jia, Gustavsson, Emil K, Seddighi, Sahba, Reyes, Joel F, Coon, Steven L, Ramos, Daniel, Schiavo, Giampietro, Fisher, Elizabeth MC, Raj, Towfique, Secrier, Maria, Lashley, Tammaryn, Ule, Jernej, Buratti, Emanuele, Humphrey, Jack, Ward, Michael E, and Fratta, Pietro
- Subjects
Rare Diseases ,Dementia ,Prevention ,ALS ,Brain Disorders ,Neurodegenerative ,Neurosciences ,Acquired Cognitive Impairment ,Genetics ,Clinical Research ,2.1 Biological and endogenous factors ,Aetiology ,Neurological ,Alternative Splicing ,Amyotrophic Lateral Sclerosis ,Codon ,Nonsense ,DNA-Binding Proteins ,Frontotemporal Dementia ,Humans ,Nerve Tissue Proteins ,Polymorphism ,Single Nucleotide ,TDP-43 Proteinopathies ,NYGC ALS Consortium ,General Science & Technology - Abstract
Variants of UNC13A, a critical gene for synapse function, increase the risk of amyotrophic lateral sclerosis and frontotemporal dementia1-3, two related neurodegenerative diseases defined by mislocalization of the RNA-binding protein TDP-434,5. Here we show that TDP-43 depletion induces robust inclusion of a cryptic exon in UNC13A, resulting in nonsense-mediated decay and loss of UNC13A protein. Two common intronic UNC13A polymorphisms strongly associated with amyotrophic lateral sclerosis and frontotemporal dementia risk overlap with TDP-43 binding sites. These polymorphisms potentiate cryptic exon inclusion, both in cultured cells and in brains and spinal cords from patients with these conditions. Our findings, which demonstrate a genetic link between loss of nuclear TDP-43 function and disease, reveal the mechanism by which UNC13A variants exacerbate the effects of decreased TDP-43 function. They further provide a promising therapeutic target for TDP-43 proteinopathies.
- Published
- 2022
4. Riboseq-flow: A streamlined, reliable pipeline for ribosome profiling data analysis and quality control
- Author
-
Iosub, Ira A., primary, Wilkins, Oscar G., additional, and Ule, Jernej, additional
- Published
- 2024
- Full Text
- View/download PDF
5. Mis-spliced transcripts generate de novo proteins in TDP-43–related ALS/FTD
- Author
-
Seddighi, Sahba, primary, Qi, Yue A., additional, Brown, Anna-Leigh, additional, Wilkins, Oscar G., additional, Bereda, Colleen, additional, Belair, Cedric, additional, Zhang, Yong-Jie, additional, Prudencio, Mercedes, additional, Keuss, Matthew J., additional, Khandeshi, Aditya, additional, Pickles, Sarah, additional, Kargbo-Hill, Sarah E., additional, Hawrot, James, additional, Ramos, Daniel M., additional, Yuan, Hebao, additional, Roberts, Jessica, additional, Sacramento, Erika Kelmer, additional, Shah, Syed I., additional, Nalls, Mike A., additional, Colón-Mercado, Jennifer M., additional, Reyes, Joel F., additional, Ryan, Veronica H., additional, Nelson, Matthew P., additional, Cook, Casey N., additional, Li, Ziyi, additional, Screven, Laurel, additional, Kwan, Justin Y., additional, Mehta, Puja R., additional, Zanovello, Matteo, additional, Hallegger, Martina, additional, Shantaraman, Anantharaman, additional, Ping, Lingyan, additional, Koike, Yuka, additional, Oskarsson, Björn, additional, Staff, Nathan P., additional, Duong, Duc M., additional, Ahmed, Aisha, additional, Secrier, Maria, additional, Ule, Jernej, additional, Jacobson, Steven, additional, Reich, Daniel S., additional, Rohrer, Jonathan D., additional, Malaspina, Andrea, additional, Dickson, Dennis W., additional, Glass, Jonathan D., additional, Ori, Alessandro, additional, Seyfried, Nicholas T., additional, Maragkakis, Manolis, additional, Petrucelli, Leonard, additional, Fratta, Pietro, additional, and Ward, Michael E., additional
- Published
- 2024
- Full Text
- View/download PDF
6. MIR-NATs repress MAPT translation and aid proteostasis in neurodegeneration
- Author
-
Simone, Roberto, Javad, Faiza, Emmett, Warren, Wilkins, Oscar G., Almeida, Filipa Lourenço, Barahona-Torres, Natalia, Zareba-Paslawska, Justyna, Ehteramyan, Mazdak, Zuccotti, Paola, Modelska, Angelika, Siva, Kavitha, Virdi, Gurvir S., Mitchell, Jamie S., Harley, Jasmine, Kay, Victoria A., Hondhamuni, Geshanthi, Trabzuni, Daniah, Ryten, Mina, Wray, Selina, Preza, Elisavet, Kia, Demis A., Pittman, Alan, Ferrari, Raffaele, Manzoni, Claudia, Lees, Andrew, Hardy, John A., Denti, Michela A., Quattrone, Alessandro, Patani, Rickie, Svenningsson, Per, Warner, Thomas T., Plagnol, Vincent, Ule, Jernej, and de Silva, Rohan
- Published
- 2021
- Full Text
- View/download PDF
7. Creation of de novo cryptic splicing for ALS/FTD precision medicine
- Author
-
Wilkins, Oscar G, primary, Chien, Max Z.Y.J., additional, Wlaschin, Josette J., additional, Pisliakova, Maria, additional, Thompson, David, additional, Digby, Holly, additional, Simkin, Rebecca L, additional, Diaz, Juan Antinao, additional, Mehta, Puja R, additional, Keuss, Matthew J., additional, Zanovello, Matteo, additional, Brown, Anna-Leigh, additional, Harley, Peter, additional, Darbey, Annalucia, additional, Karda, Rajvinder, additional, Fisher, Elizabeth M.C., additional, Cunningham, Tom J., additional, Le Pichon, Claire E., additional, Ule, Jernej, additional, and Fratta, Pietro, additional
- Published
- 2023
- Full Text
- View/download PDF
8. Highly disordered histone H1−DNA model complexes and their condensates
- Author
-
Turner, Abigail L., Watson, Matthew, Wilkins, Oscar G., Cato, Laura, Travers, Andrew, Thomas, Jean O., and Stott, Katherine
- Published
- 2018
9. Flow: a web platform and open database to analyse, store, curate and share bioinformatics data at scale
- Author
-
Capitanchik, Charlotte, primary, Ireland, Sam, additional, Harston, Alex, additional, Cheshire, Chris, additional, Jones, D. Marc, additional, Lee, Flora C.Y., additional, Ruiz de los Mozos, Igor, additional, Iosub, Ira A., additional, Kuret, Klara, additional, Faraway, Rupert, additional, Wilkins, Oscar G., additional, Arora, Rahul, additional, Hallegger, Martina, additional, Modic, Miha, additional, Chakrabarti, Anob M., additional, Luscombe, Nicholas M., additional, and Ule, Jernej, additional
- Published
- 2023
- Full Text
- View/download PDF
10. Mutual homeostasis of charged proteins
- Author
-
Faraway, Rupert, primary, Heaven, Neve Costello, additional, Digby, Holly, additional, Wilkins, Oscar G, additional, Chakrabarti, Anob M, additional, Iosub, Ira A, additional, Knez, Lea, additional, Ameres, Stefan L, additional, Plaschka, Clemens, additional, and Ule, Jernej, additional
- Published
- 2023
- Full Text
- View/download PDF
11. Mis-spliced transcripts generatede novoproteins in TDP-43-related ALS/FTD
- Author
-
Seddighi, Sahba, primary, Qi, Yue A., additional, Brown, Anna-Leigh, additional, Wilkins, Oscar G., additional, Bereda, Colleen, additional, Belair, Cedric, additional, Zhang, Yongjie, additional, Prudencio, Mercedes, additional, Keuss, Matthew J, additional, Khandeshi, Aditya, additional, Pickles, Sarah, additional, Hill, Sarah E., additional, Hawrot, James, additional, Ramos, Daniel M., additional, Yuan, Hebao, additional, Roberts, Jessica, additional, Sacramento, Erika Kelmer, additional, Shah, Syed I., additional, Nalls, Mike A., additional, Colon-Mercado, Jenn, additional, Reyes, Joel F., additional, Ryan, Veronica H., additional, Nelson, Matthew P., additional, Cook, Casey, additional, Li, Ziyi, additional, Screven, Laurel, additional, Kwan, Justin Y, additional, Shantaraman, Anantharaman, additional, Ping, Lingyan, additional, Koike, Yuka, additional, Oskarsson, Björn, additional, Staff, Nathan, additional, Duong, Duc M., additional, Ahmed, Aisha, additional, Secrier, Maria, additional, Ule, Jerneg, additional, Jacobson, Steven, additional, Rohrer, Jonathan, additional, Malaspina, Andrea, additional, Glass, Jonathan D., additional, Ori, Alessandro, additional, Seyfried, Nicholas T., additional, Maragkakis, Manolis, additional, Petrucelli, Leonard, additional, Fratta, Pietro, additional, and Ward, Michael E., additional
- Published
- 2023
- Full Text
- View/download PDF
12. Identifying ribosome heterogeneity using ribosome profiling
- Author
-
Alkan, Ferhat, primary, Wilkins, Oscar G, additional, Hernández-Pérez, Santiago, additional, Ramalho, Sofia, additional, Silva, Joana, additional, Ule, Jernej, additional, and Faller, William J, additional
- Published
- 2022
- Full Text
- View/download PDF
13. FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translation
- Author
-
Birsa, Nicol, primary, Ule, Agnieszka M., additional, Garone, Maria Giovanna, additional, Tsang, Brian, additional, Mattedi, Francesca, additional, Chong, P. Andrew, additional, Humphrey, Jack, additional, Jarvis, Seth, additional, Pisiren, Melis, additional, Wilkins, Oscar G., additional, Nosella, Micheal L., additional, Devoy, Anny, additional, Bodo, Cristian, additional, de la Fuente, Rafaela Fernandez, additional, Fisher, Elizabeth M. C., additional, Rosa, Alessandro, additional, Viero, Gabriella, additional, Forman-Kay, Julie D., additional, Schiavo, Giampietro, additional, and Fratta, Pietro, additional
- Published
- 2021
- Full Text
- View/download PDF
14. Ribocutter: Cas9-mediated rRNA depletion from multiplexed Ribo-seq libraries
- Author
-
Wilkins, Oscar G., primary and Ule, Jernej, additional
- Published
- 2021
- Full Text
- View/download PDF
15. Ultraplex: A rapid, flexible, all-in-one fastq demultiplexer
- Author
-
Wilkins, Oscar G, primary, Capitanchik, Charlotte, additional, Luscombe, Nicholas M., additional, and Ule, Jernej, additional
- Published
- 2021
- Full Text
- View/download PDF
16. MIR-NATs repress MAPTtranslation and aid proteostasis in neurodegeneration
- Author
-
Simone, Roberto, Javad, Faiza, Emmett, Warren, Wilkins, Oscar G., Almeida, Filipa Lourenço, Barahona-Torres, Natalia, Zareba-Paslawska, Justyna, Ehteramyan, Mazdak, Zuccotti, Paola, Modelska, Angelika, Siva, Kavitha, Virdi, Gurvir S., Mitchell, Jamie S., Harley, Jasmine, Kay, Victoria A., Hondhamuni, Geshanthi, Trabzuni, Daniah, Ryten, Mina, Wray, Selina, Preza, Elisavet, Kia, Demis A., Pittman, Alan, Ferrari, Raffaele, Manzoni, Claudia, Lees, Andrew, Hardy, John A., Denti, Michela A., Quattrone, Alessandro, Patani, Rickie, Svenningsson, Per, Warner, Thomas T., Plagnol, Vincent, Ule, Jernej, and de Silva, Rohan
- Abstract
The human genome expresses thousands of natural antisense transcripts (NAT) that can regulate epigenetic state, transcription, RNA stability or translation of their overlapping genes1,2. Here we describe MAPT-AS1, a brain-enriched NAT that is conserved in primates and contains an embedded mammalian-wide interspersed repeat (MIR), which represses tau translation by competing for ribosomal RNA pairing with the MAPTmRNA internal ribosome entry site3. MAPTencodes tau, a neuronal intrinsically disordered protein (IDP) that stabilizes axonal microtubules. Hyperphosphorylated, aggregation-prone tau forms the hallmark inclusions of tauopathies4. Mutations in MAPTcause familial frontotemporal dementia, and common variations forming the MAPTH1 haplotype are a significant risk factor in many tauopathies5and Parkinson’s disease. Notably, expression of MAPT-AS1 or minimal essential sequences from MAPT-AS1 (including MIR) reduces—whereas silencing MAPT-AS1 expression increases—neuronal tau levels, and correlate with tau pathology in human brain. Moreover, we identified many additional NATs with embedded MIRs (MIR-NATs), which are overrepresented at coding genes linked to neurodegeneration and/or encoding IDPs, and confirmed MIR-NAT-mediated translational control of one such gene, PLCG1. These results demonstrate a key role for MAPT-AS1 in tauopathies and reveal a potentially broad contribution of MIR-NATs to the tightly controlled translation of IDPs6, with particular relevance for proteostasis in neurodegeneration.
- Published
- 2021
- Full Text
- View/download PDF
17. Highly disordered histone H1--DNA model complexes and their condensates.
- Author
-
Turner, Abigail L., Watson, Matthew, Wilkins, Oscar G., Thomas, Jean O., Stott, Katherine, Cato, Laura, and Travers, Andrew
- Subjects
HISTONES ,CHROMATIN ,PHOSPHORYLATION ,PHASE separation ,POLYMERS - Abstract
Disordered proteins play an essential role in a wide variety of biological processes, and are often posttranslationally modified. One such protein is histone H1; its highly disordered C-terminal tail (CH1) condenses internucleosomal linker DNA in chromatin in a way that is still poorly understood. Moreover, CH1 is phosphorylated in a cell cycle-dependent manner that correlates with changes in the chromatin condensation level. Here we present a model system that recapitulates key aspects of the in vivo process, and also allows a detailed structural and biophysical analysis of the stages before and after condensation. CH1 remains disordered in the DNA-bound state, despite its nanomolar affinity. Phase-separated droplets (coacervates) form, containing higher-order assemblies of CH1/DNA complexes. Phosphorylation at three serine residues, spaced along the length of the tail, has little effect on the local properties of the condensate. However, it dramatically alters higher-order structure in the coacervate and reduces partitioning to the coacervate phase. These observations show that disordered proteins can bind tightly to DNA without a disorder-to-order transition. Importantly, they also provide mechanistic insights into how higher-order structures can be exquisitely sensitive to perturbation by posttranslational modifications, thus broadening the repertoire of mechanisms that might regulate chromatin and other macromolecular assemblies. [ABSTRACT FROM AUTHOR]
- Published
- 2018
- Full Text
- View/download PDF
18. Loss of TDP-43 induces synaptic dysfunction that is rescued by UNC13A splice-switching ASOs.
- Author
-
Keuss MJ, Harley P, Ryadnov E, Jackson RE, Zanovello M, Wilkins OG, Barattucci S, Mehta PR, Oliveira MG, Parkes JE, Sinha A, Correa-Sánchez AF, Oliver PL, Fisher EMC, Schiavo G, Shah M, Burrone J, and Fratta P
- Abstract
TDP-43 loss of function induces multiple splicing changes, including a cryptic exon in the amyotrophic lateral sclerosis and fronto-temporal lobar degeneration risk gene UNC13A , leading to nonsense-mediated decay of UNC13A transcripts and loss of protein. UNC13A is an active zone protein with an integral role in coordinating pre-synaptic function. Here, we show TDP-43 depletion induces a severe reduction in synaptic transmission, leading to an asynchronous pattern of network activity. We demonstrate that these deficits are largely driven by a single cryptic exon in UNC13A . Antisense oligonucleotides targeting the UNC13A cryptic exon robustly rescue UNC13A protein levels and restore normal synaptic function, providing a potential new therapeutic approach for ALS and other TDP-43-related disorders., Competing Interests: Competing interests: PF, MJK and OGW have filed a patent application relating to the use of antisense oligonucleotides for the correction of cryptic splicing in UNC13A. PF is founder, advisor, and holds shares in Trace Neuroscience Inc. MJK performs consulting for and holds shares in Trace Neuroscience Inc. PH performs consulting for Trace Neuroscience Inc.
- Published
- 2024
- Full Text
- View/download PDF
19. TDP-43 loss induces extensive cryptic polyadenylation in ALS/FTD.
- Author
-
Bryce-Smith S, Brown AL, Mehta PR, Mattedi F, Mikheenko A, Barattucci S, Zanovello M, Dattilo D, Yome M, Hill SE, Qi YA, Wilkins OG, Sun K, Ryadnov E, Wan Y, Vargas JNS, Birsa N, Raj T, Humphrey J, Keuss M, Ward M, Secrier M, and Fratta P
- Abstract
Nuclear depletion and cytoplasmic aggregation of the RNA-binding protein TDP-43 is the hallmark of ALS, occurring in over 97% of cases. A key consequence of TDP-43 nuclear loss is the de-repression of cryptic exons. Whilst TDP-43 regulated cryptic splicing is increasingly well catalogued, cryptic alternative polyadenylation (APA) events, which define the 3' end of last exons, have been largely overlooked, especially when not associated with novel upstream splice junctions. We developed a novel bioinformatic approach to reliably identify distinct APA event types: alternative last exons (ALE), 3'UTR extensions (3'Ext) and intronic polyadenylation (IPA) events. We identified novel neuronal cryptic APA sites induced by TDP-43 loss of function by systematically applying our pipeline to a compendium of publicly available and in house datasets. We find that TDP-43 binding sites and target motifs are enriched at these cryptic events and that TDP-43 can have both repressive and enhancing action on APA. Importantly, all categories of cryptic APA can also be identified in ALS and FTD post mortem brain regions with TDP-43 proteinopathy underlining their potential disease relevance. RNA-seq and Ribo-seq analyses indicate that distinct cryptic APA categories have different downstream effects on transcript and translation. Intriguingly, cryptic 3'Exts occur in multiple transcription factors, such as ELK1 , SIX3, and TLX1, and lead to an increase in wild-type protein levels and function. Finally, we show that an increase in RNA stability leading to a higher cytoplasmic localisation underlies these observations. In summary, we demonstrate that TDP-43 nuclear depletion induces a novel category of cryptic RNA processing events and we expand the palette of TDP-43 loss consequences by showing this can also lead to an increase in normal protein translation.
- Published
- 2024
- Full Text
- View/download PDF
20. Creation of de novo cryptic splicing for ALS/FTD precision medicine.
- Author
-
Wilkins OG, Chien MZYJ, Wlaschin JJ, Pisliakova M, Thompson D, Digby H, Simkin RL, Diaz JA, Mehta PR, Keuss MJ, Zanovello M, Brown AL, Harley P, Darbey A, Karda R, Fisher EMC, Cunningham TJ, Le Pichon CE, Ule J, and Fratta P
- Abstract
A system enabling the expression of therapeutic proteins specifically in diseased cells would be transformative, providing greatly increased safety and the possibility of pre-emptive treatment. Here we describe "TDP-REG", a precision medicine approach primarily for amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), which exploits the cryptic splicing events that occur in cells with TDP-43 loss-of-function (TDP-LOF) in order to drive expression specifically in diseased cells. In addition to modifying existing cryptic exons for this purpose, we develop a deep-learning-powered algorithm for generating customisable cryptic splicing events, which can be embedded within virtually any coding sequence. By placing part of a coding sequence within a novel cryptic exon, we tightly couple protein expression to TDP-LOF. Protein expression is activated by TDP-LOF in vitro and in vivo , including TDP-LOF induced by cytoplasmic TDP-43 aggregation. In addition to generating a variety of fluorescent and luminescent reporters, we use this system to perform TDP-LOF-dependent genomic prime editing to ablate the UNC13A cryptic donor splice site. Furthermore, we design a panel of tightly gated, autoregulating vectors encoding a TDP-43/Raver1 fusion protein, which rescue key pathological cryptic splicing events. In summary, we combine deep-learning and rational design to create sophisticated splicing sensors, resulting in a platform that provides far safer therapeutics for neurodegeneration, potentially even enabling preemptive treatment of at-risk individuals., Competing Interests: Competing interests: PF and OGW have filed a patent application relating to TDP-REG technology. PF, ALB, MJK and OGW have filed a patent application relating to the use of ASO therapies for correcting cryptic splicing in UNC13A.
- Published
- 2023
- Full Text
- View/download PDF
21. Mis-spliced transcripts generate de novo proteins in TDP-43-related ALS/FTD.
- Author
-
Seddighi S, Qi YA, Brown AL, Wilkins OG, Bereda C, Belair C, Zhang Y, Prudencio M, Keuss MJ, Khandeshi A, Pickles S, Hill SE, Hawrot J, Ramos DM, Yuan H, Roberts J, Kelmer Sacramento E, Shah SI, Nalls MA, Colon-Mercado J, Reyes JF, Ryan VH, Nelson MP, Cook C, Li Z, Screven L, Kwan JY, Shantaraman A, Ping L, Koike Y, Oskarsson B, Staff N, Duong DM, Ahmed A, Secrier M, Ule J, Jacobson S, Rohrer J, Malaspina A, Glass JD, Ori A, Seyfried NT, Maragkakis M, Petrucelli L, Fratta P, and Ward ME
- Abstract
Functional loss of TDP-43, an RNA-binding protein genetically and pathologically linked to ALS and FTD, leads to inclusion of cryptic exons in hundreds of transcripts during disease. Cryptic exons can promote degradation of affected transcripts, deleteriously altering cellular function through loss-of-function mechanisms. However, the possibility of de novo protein synthesis from cryptic exon transcripts has not been explored. Here, we show that mRNA transcripts harboring cryptic exons generate de novo proteins both in TDP-43 deficient cellular models and in disease. Using coordinated transcriptomic and proteomic studies of TDP-43 depleted iPSC-derived neurons, we identified numerous peptides that mapped to cryptic exons. Cryptic exons identified in iPSC models were highly predictive of cryptic exons expressed in brains of patients with TDP-43 proteinopathy, including cryptic transcripts that generated de novo proteins. We discovered that inclusion of cryptic peptide sequences in proteins altered their interactions with other proteins, thereby likely altering their function. Finally, we showed that these de novo peptides were present in CSF from patients with ALS. The demonstration of cryptic exon translation suggests new mechanisms for ALS pathophysiology downstream of TDP-43 dysfunction and may provide a strategy for novel biomarker development., Competing Interests: Competing interests: MAN, ZL, and SIS’s participation in this project was part of a competitive contract awarded to Data Tecnica International LLC by the National Institutes of Health to support open science research. MAN also currently serves as an advisor for Character Biosciences and Neuron23 Inc.
- Published
- 2023
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.