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  1. Article ; Online: Safeguarding Non-COVID-19 Research: Looking Up from Ground Zero.

    Chan, Christine Hui-Shan / Tan, Eng-King

    Archives of medical research

    2020  Volume 51, Issue 7, Page(s) 731–732

    Abstract: The COVID-19 pandemic has kicked off a global race to launch clinical trials of experimental vaccines and treatments for the coronavirus. Worldwide, as resources are directed toward accelerating the research into unravelling the mechanism of COVID-19 ... ...

    Abstract The COVID-19 pandemic has kicked off a global race to launch clinical trials of experimental vaccines and treatments for the coronavirus. Worldwide, as resources are directed toward accelerating the research into unravelling the mechanism of COVID-19 pathophysiology, concerns have been raised regarding the future of clinical research in United Kingdom and elsewhere during the current pandemic. However, the real immediate impact of these restrictions due to lock-down is most acutely felt by scientists working on non-COVID-19 biomedical research bench and clinical researchers whose drug trials have to be delayed, suspended or ceased. Here, we highlight our views from "ground zero" as we represent those whose work are deeply affected by the restrictions. We draw attention to some of the practical realities and emotions experienced in the laboratory. In addition, we also highlight the difficulties for policy makers to maintain equanimity in prioritizing their decisions cross the different fields of science.
    MeSH term(s) Biomedical Research/organization & administration ; Biomedical Research/standards ; COVID-19 ; Humans ; SARS-CoV-2
    Keywords covid19
    Language English
    Publishing date 2020-05-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1156844-6
    ISSN 1873-5487 ; 0188-4409 ; 0188-0128
    ISSN (online) 1873-5487
    ISSN 0188-4409 ; 0188-0128
    DOI 10.1016/j.arcmed.2020.05.023
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  2. Article ; Online: Safeguarding Non-COVID-19 Research

    Chan, Christine Hui-Shan / Tan, Eng-King

    Archives of Medical Research

    Looking Up from Ground Zero

    2020  Volume 51, Issue 7, Page(s) 731–732

    Keywords General Medicine ; covid19
    Language English
    Publisher Elsevier BV
    Publishing country us
    Document type Article ; Online
    ZDB-ID 1156844-6
    ISSN 0188-4409 ; 0188-0128
    ISSN 0188-4409 ; 0188-0128
    DOI 10.1016/j.arcmed.2020.05.023
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Safeguarding Non-COVID-19 Research: Looking Up from Ground Zero

    Chan, Christine Hui-Shan / Tan, Eng-King

    Arch Med Res

    Abstract: The COVID-19 pandemic has kicked off a global race to launch clinical trials of experimental vaccines and treatments for the coronavirus. Worldwide, as resources are directed toward accelerating the research into unravelling the mechanism of COVID-19 ... ...

    Abstract The COVID-19 pandemic has kicked off a global race to launch clinical trials of experimental vaccines and treatments for the coronavirus. Worldwide, as resources are directed toward accelerating the research into unravelling the mechanism of COVID-19 pathophysiology, concerns have been raised regarding the future of clinical research in United Kingdom and elsewhere during the current pandemic. However, the real immediate impact of these restrictions due to lock-down is most acutely felt by scientists working on non-COVID-19 biomedical research bench and clinical researchers whose drug trials have to be delayed, suspended or ceased. Here, we highlight our views from "ground zero" as we represent those whose work are deeply affected by the restrictions. We draw attention to some of the practical realities and emotions experienced in the laboratory. In addition, we also highlight the difficulties for policy makers to maintain equanimity in prioritizing their decisions cross the different fields of science.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #436814
    Database COVID19

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  4. Article: A Proteome-Wide Effect of PHF8 Knockdown on Cortical Neurons Shows Downregulation of Parkinson's Disease-Associated Protein Alpha-Synuclein and Its Interactors.

    Oey, Nicodemus E / Zhou, Lei / Chan, Christine Hui Shan / VanDongen, Antonius M J / Tan, Eng King

    Biomedicines

    2023  Volume 11, Issue 2

    Abstract: Synaptic dysfunction may underlie the pathophysiology of Parkinson's disease (PD), a presently incurable condition characterized by motor and cognitive symptoms. Here, we used quantitative proteomics to study the role of PHD Finger Protein 8 (PHF8), a ... ...

    Abstract Synaptic dysfunction may underlie the pathophysiology of Parkinson's disease (PD), a presently incurable condition characterized by motor and cognitive symptoms. Here, we used quantitative proteomics to study the role of PHD Finger Protein 8 (PHF8), a histone demethylating enzyme found to be mutated in X-linked intellectual disability and identified as a genetic marker of PD, in regulating the expression of PD-related synaptic plasticity proteins. Amongst the list of proteins found to be affected by PHF8 knockdown were Parkinson's-disease-associated SNCA (alpha synuclein) and PD-linked genes DNAJC6 (auxilin), SYNJ1 (synaptojanin 1), and the PD risk gene SH3GL2 (endophilin A1). Findings in this study show that depletion of PHF8 in cortical neurons affects the activity-induced expression of proteins involved in synaptic plasticity, synaptic structure, vesicular release and membrane trafficking, spanning the spectrum of pre-synaptic and post-synaptic transmission. Given that the depletion of even a single chromatin-modifying enzyme can affect synaptic protein expression in such a concerted manner, more in-depth studies will be needed to show whether such a mechanism can be exploited as a potential disease-modifying therapeutic drug target in PD.
    Language English
    Publishing date 2023-02-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines11020486
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  5. Article ; Online: Genetic and pharmacologic p32-inhibition rescue CHCHD2-linked Parkinson's disease phenotypes in vivo and in cell models.

    Tio, Murni / Wen, Rujing / Choo, Cai Ning / Tan, Jian Bin / Chua, Aaron / Xiao, Bin / Sundaram, Jeyapriya Rajameenakshi / Chan, Christine Hui Shan / Tan, Eng-King

    Journal of biomedical science

    2024  Volume 31, Issue 1, Page(s) 24

    Abstract: Background: Mutations in CHCHD2 have been linked to Parkinson's disease, however, their exact pathophysiologic roles are unclear. The p32 protein has been suggested to interact with CHCHD2, however, the physiological functions of such interaction in the ...

    Abstract Background: Mutations in CHCHD2 have been linked to Parkinson's disease, however, their exact pathophysiologic roles are unclear. The p32 protein has been suggested to interact with CHCHD2, however, the physiological functions of such interaction in the context of PD have not been clarified.
    Methods: Interaction between CHCHD2 and p32 was confirmed by co-immunoprecipitation experiments. We studied the effect of p32-knockdown in the transgenic Drosophila and Hela cells expressing the wild type and the pathogenic variants of hCHCHD2. We further investigated the rescue ability of a custom generated p32-inhibitor in these models as well as in the human fibroblast derived neural precursor cells and the dopaminergic neurons harboring hCHCHD2-Arg145Gln.
    Results: Our results showed that wildtype and mutant hCHCHD2 could bind to p32 in vitro, supported by in vivo interaction between human CHCHD2 and Drosophila p32. Knockdown of p32 reduced mutant hCHCHD2 levels in Drosophila and in vitro. In Drosophila hCHCHD2 models, inhibition of p32 through genetic knockdown and pharmacological treatment using a customized p32-inhibitor restored dopaminergic neuron numbers and improved mitochondrial morphology. These were correlated with improved locomotor function, reduced oxidative stress and decreased mortality. Consistently, Hela cells expressing mutant hCHCHD2 showed improved mitochondrial morphology and function after treatment with the p32-inhibitor. As compared to the isogenic control cells, large percentage of the mutant neural precursor cells and dopaminergic neurons harboring hCHCHD2-Arg145Gln contained fragmented mitochondria which was accompanied by lower ATP production and cell viability. The NPCs harboring hCHCHD2-Arg145Gln also had a marked increase in α-synuclein expression. The p32-inhibitor was able to ameliorate the mitochondrial fragmentation, restored ATP levels, increased cell viability and reduced α-synuclein level in these cells.
    Conclusions: Our study identified p32 as a modulator of CHCHD2, possibly exerting its effects by reducing the toxic mutant hCHCHD2 expression and/or mitigating the downstream effects. Inhibition of the p32 pathway can be a potential therapeutic intervention for CHCHD2-linked PD and diseases involving mitochondrial dysfunction.
    MeSH term(s) Animals ; Humans ; Adenosine Triphosphate/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Dopaminergic Neurons/metabolism ; Drosophila/genetics ; Drosophila/metabolism ; HeLa Cells ; Neural Stem Cells/metabolism ; Parkinson Disease/drug therapy ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Phenotype ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances Adenosine Triphosphate (8L70Q75FXE) ; alpha-Synuclein ; CHCHD2 protein, human ; DNA-Binding Proteins ; Transcription Factors ; C1QBP protein, human
    Language English
    Publishing date 2024-02-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 1193378-1
    ISSN 1423-0127 ; 1021-7770
    ISSN (online) 1423-0127
    ISSN 1021-7770
    DOI 10.1186/s12929-024-01010-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4037: Show issues Location:
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  6. Article ; Online: Neurological research & training after the easing of lockdown in countries impacted by COVID-19.

    Tan, Eng-King / Albanese, Alberto / Chaudhuri, K Ray / Opal, Puneet / Wu, Yun-Cheng / Chan, Christine Hui-Shan / Jeon, Beomseok / Truong, Daniel / Poewe, Werner / Tan, Louis / Pal, Pramod / Colosimo, Carlo / Lim, Shen-Yang / Jinnah, H A / Cardoso, Francisco

    Journal of the neurological sciences

    2020  Volume 418, Page(s) 117105

    MeSH term(s) Biomedical Research/education ; COVID-19/epidemiology ; COVID-19/prevention & control ; Humans ; Neurology/education ; Neurosciences/education ; Pandemics
    Keywords covid19
    Language English
    Publishing date 2020-08-24
    Publishing country Netherlands
    Document type Editorial
    ZDB-ID 80160-4
    ISSN 1878-5883 ; 0022-510X ; 0374-8642
    ISSN (online) 1878-5883
    ISSN 0022-510X ; 0374-8642
    DOI 10.1016/j.jns.2020.117105
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  7. Article: Neurological research & training after the easing of lockdown in countries impacted by COVID-19

    Tan, Eng-King / Albanese, Alberto / Chaudhuri, K Ray / Opal, Puneet / Wu, Yun-Cheng / Chan, Christine Hui-Shan / Jeon, Beomseok / Truong, Daniel / Poewe, Werner / Tan, Louis / Pal, Pramod / Colosimo, Carlo / Lim, Shen-Yang / Jinnah, H A / Cardoso, Francisco

    J Neurol Sci

    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #726649
    Database COVID19

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  8. Article ; Online: Neurological research & training after the easing of lockdown in countries impacted by COVID-19

    Tan, Eng-King / Albanese, Alberto / Chaudhuri, K. Ray / Opal, Puneet / Wu, Yun-Cheng / Chan, Christine Hui-Shan / Jeon, Beomseok / Truong, Daniel / Poewe, Werner / Tan, Louis / Pal, Pramod / Colosimo, Carlo / Lim, Shen-Yang / Jinnah, H.A. / Cardoso, Francisco

    Journal of the Neurological Sciences

    2020  Volume 418, Page(s) 117105

    Keywords Neurology ; Clinical Neurology ; covid19
    Language English
    Publisher Elsevier BV
    Publishing country us
    Document type Article ; Online
    ZDB-ID 80160-4
    ISSN 1878-5883 ; 0022-510X ; 0374-8642
    ISSN (online) 1878-5883
    ISSN 0022-510X ; 0374-8642
    DOI 10.1016/j.jns.2020.117105
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  9. Article ; Online: Ring finger protein 146/Iduna is a poly(ADP-ribose) polymer binding and PARsylation dependent E3 ubiquitin ligase.

    Zhou, Zhi-dong / Chan, Christine Hui-shan / Xiao, Zhi-cheng / Tan, Eng-king

    Cell adhesion & migration

    2012  Volume 5, Issue 6, Page(s) 463–471

    Abstract: Recent findings suggest that Ring finger protein 146 (RNF146), also called iduna, have neuroprotective property due to its inhibition of Parthanatos via binding with Poly(ADP-ribose) (PAR). The Parthanatos is a PAR dependent cell death that has been ... ...

    Abstract Recent findings suggest that Ring finger protein 146 (RNF146), also called iduna, have neuroprotective property due to its inhibition of Parthanatos via binding with Poly(ADP-ribose) (PAR). The Parthanatos is a PAR dependent cell death that has been implicated in many human diseases. RNF146/Iduna acts as a PARsylation-directed E3 ubquitin ligase to mediate tankyrase-dependent degradation of axin, thereby positively regulates Wnt signaling. RNF146/Iduna can also facilitate DNA repair and protect against cell death induced by DNA damaging agents or γ-irradiation. It can translocate to the nucleus after cellular injury and promote the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. The PARsylation-directed ubquitination mediated by RNF146/Iduna is analogous to the phosphorylation-directed ubquitination catalyzed by Skp1-Cul1-F-box (SCF) E3 ubiquitin complex. RNF146/Iduna has been found to be implicated in neurodegenerative disease and cancer development. Therefore modulation of the PAR-binding and PARsylation dependent E3 ligase activity of RNF146/Iduna could have therapeutic significance for diseases, in which PAR and PAR-binding proteins play key pathophysiologic roles.
    MeSH term(s) Amino Acid Sequence ; Cell Death ; Cell Transformation, Neoplastic ; Cytoprotection ; DNA Repair ; Humans ; Molecular Sequence Data ; Neurodegenerative Diseases/metabolism ; Poly Adenosine Diphosphate Ribose/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Proteins/metabolism ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitin-Protein Ligases/physiology ; Wnt Signaling Pathway
    Chemical Substances Proteins ; poly(ADP)-ribosylated proteins ; Poly Adenosine Diphosphate Ribose (26656-46-2) ; RNF146 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2012-01-25
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2268518-2
    ISSN 1933-6926 ; 1933-6918
    ISSN (online) 1933-6926
    ISSN 1933-6918
    DOI 10.4161/cam.5.6.18356
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  10. Article ; Online: Adapting to post-COVID19 research in Parkinson's disease: Lessons from a multinational experience.

    Tan, Eng-King / Albanese, Alberto / Chaudhuri, KRay / Lim, Shen-Yang / Oey, Nicodemus Edrick / Shan Chan, Christine Hui / Wu, Yun-Cheng / Jeon, Beomseok / Truong, Daniel / Poewe, Werner / Pal, Pramod Kumar / Tan, Louis / Opal, Puneet / Colosimo, Carlo / Jinnah, H A / Cardoso, Francisco

    Parkinsonism & related disorders

    2020  Volume 82, Page(s) 146–149

    MeSH term(s) Biomedical Research/methods ; Biomedical Research/trends ; COVID-19/epidemiology ; COVID-19/therapy ; Humans ; Internationality ; Parkinson Disease/epidemiology ; Parkinson Disease/therapy
    Keywords covid19
    Language English
    Publishing date 2020-10-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1311489-x
    ISSN 1873-5126 ; 1353-8020
    ISSN (online) 1873-5126
    ISSN 1353-8020
    DOI 10.1016/j.parkreldis.2020.10.009
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