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Article ; Online: Developing Lipase Inhibitor as a Novel Approach to Address the Rice Bran Rancidity Issue─A Critical Review.

Li, Qingyun / Liu, Kunlun / Cai, Gongli / Yang, Xi / Ngo, Jacky Chi Ki

Journal of agricultural and food chemistry

2024 Volume 72, Issue 7, Page(s) 3277–3290

Abstract: Rice bran is a valuable byproduct from the food processing industry, which contains abundant protein, essential unsaturated fatty acids, and numerous bioactive compounds. However, its susceptibility to rancidity greatly restricts its wide utilization. ... ...

Abstract	Rice bran is a valuable byproduct from the food processing industry, which contains abundant protein, essential unsaturated fatty acids, and numerous bioactive compounds. However, its susceptibility to rancidity greatly restricts its wide utilization. Many strategies have been proposed to delay the rancidity of rice bran, but most of them have their respective limitations. Here, we proposed that developing rice ban lipase peptide inhibitors represents an alternative and promising prescription for impeding the rancidity of rice bran, in contrast to the conventional stabilization approaches for rice bran. For this reason, the rancidity mechanisms of rice bran and the research progress of rice bran lipases were discussed. In addition, the feasibility of utilizing
MeSH term(s)	Oryza/chemistry ; Lipase/chemistry ; Proteins ; Peptides/pharmacology
Chemical Substances	Lipase (EC 3.1.1.3) ; Proteins ; Peptides
Language	English
Publishing date	2024-02-08
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021/acs.jafc.3c07492
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Article ; Online: Molecular insights into the interaction of CAG trinucleotide RNA repeats with nucleolin and its implication in polyglutamine diseases.

An, Ying / Chen, Zhefan S / Chan, Ho Yin Edwin / Ngo, Jacky Chi Ki

Nucleic acids research

2022 Volume 50, Issue 13, Page(s) 7655–7668

Abstract: Polyglutamine (polyQ) diseases are a type of inherited neurodegenerative disorders caused by cytosine-adenine-guanine (CAG) trinucleotide expansion within the coding region of the disease-associated genes. We previously demonstrated that a pathogenic ... ...

Abstract	Polyglutamine (polyQ) diseases are a type of inherited neurodegenerative disorders caused by cytosine-adenine-guanine (CAG) trinucleotide expansion within the coding region of the disease-associated genes. We previously demonstrated that a pathogenic interaction between expanded CAG RNA and the nucleolin (NCL) protein triggers the nucleolar stress and neuronal cell death in polyQ diseases. However, mechanisms behind the molecular interaction remain unknown. Here, we report a 1.45 Å crystal structure of the r(CAG)5 oligo that comprises a full A'-form helical turn with widened grooves. Based on this structure, we simulated a model of r(CAG)5 RNA complexed with the RNA recognition motif 2 (RRM2) of NCL and identified NCL residues that are critical for its binding to CAG RNA. Combined with in vitro and in vivo site-directed mutagenesis studies, our model reveals that CAG RNA binds to NCL sites that are not important for other cellular functions like gene expression and rRNA synthesis regulation, indicating that toxic CAG RNA interferes with NCL functions by sequestering it. Accordingly, an NCL mutant that is aberrant in CAG RNA-binding could rescue RNA-induced cytotoxicity effectively. Taken together, our study provides new molecular insights into the pathogenic mechanism of polyQ diseases mediated by NCL-CAG RNA interaction.
MeSH term(s)	Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/pathology ; Oligonucleotides/metabolism ; Peptides ; Phosphoproteins/genetics ; RNA/genetics ; RNA-Binding Proteins/genetics ; Trinucleotide Repeats ; Nucleolin
Chemical Substances	Oligonucleotides ; Peptides ; Phosphoproteins ; RNA-Binding Proteins ; polyglutamine (26700-71-0) ; RNA (63231-63-0)
Language	English
Publishing date	2022-07-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkac532
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Zs.A 1067: Show issues

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Article ; Online: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly via Docking Interaction.

Yip, Ryan Pak Hong / Kwok, Doris Ching Ying / Lai, Louis Tung Faat / Ho, Siu-Ming / Wong, Ivan Chun Kit / Chan, Chi-Ping / Lau, Wilson Chun Yu / Ngo, Jacky Chi Ki

PLoS pathogens

2024 Volume 20, Issue 2, Page(s) e1011978

Abstract: Members of the serine-arginine protein kinase (SRPK) family, SRPK1 and SRPK2, phosphorylate the hepatitis B core protein (Cp) and are crucial for pregenomic RNA encapsidation during viral nucleocapsid assembly. Among them, SRPK2 exhibits higher kinase ... ...

Abstract	Members of the serine-arginine protein kinase (SRPK) family, SRPK1 and SRPK2, phosphorylate the hepatitis B core protein (Cp) and are crucial for pregenomic RNA encapsidation during viral nucleocapsid assembly. Among them, SRPK2 exhibits higher kinase activity toward Cp. In this study, we identified Cp sites that are phosphorylated by SRPK2 and demonstrated that the kinase utilizes an SRPK-specific docking groove to interact with and regulate the phosphorylation of the C-terminal arginine rich domain of Cp. We determined that direct interaction between the docking groove of SRPK2 and unphosphorylated Cp inhibited premature viral capsid assembly in vitro, whereas the phosphorylation of the viral protein reactivated the process. Pull-down assays together with the new cryo-electron microscopy structure of the HBV capsid in complex with SRPK2 revealed that the kinases decorate the surface of the viral capsid by interacting with the C-terminal domain of Cp, underscoring the importance of the docking interaction in regulating capsid assembly and pregenome packaging. Moreover, SRPK2-knockout in HepG2 cells suppressed Cp phosphorylation, indicating that SRPK2 is an important cellular kinase for HBV life cycle.
MeSH term(s)	Phosphorylation ; Capsid/metabolism ; Hepatitis B virus/metabolism ; Cryoelectron Microscopy ; Protein Serine-Threonine Kinases/metabolism ; Capsid Proteins/metabolism ; Virus Assembly/physiology ; Arginine/metabolism
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Capsid Proteins ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2024-02-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011978
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Article ; Online: A structure model explaining the binding between a ubiquitous unconventional G-protein (OsYchF1) and a plant-specific C2-domain protein (OsGAP1) from rice.

Cheung, Ming-Yan / Ngo, Jacky Chi-Ki / Chen, Zhongzhou / Jia, Qi / Li, Tianjie / Gou, Yitao / Wang, Yi / Lam, Hon-Ming

The Biochemical journal

2020 Volume 477, Issue 20, Page(s) 3935–3949

Abstract: The unconventional G-protein OsYchF1 plays regulatory roles in plant defense and abiotic stress responses. We have previously resolved the crystal structures of OsYchF1 and its plant-specific regulator, OsGAP1, and determined the residues on OsGAP1 that ... ...

Abstract	The unconventional G-protein OsYchF1 plays regulatory roles in plant defense and abiotic stress responses. We have previously resolved the crystal structures of OsYchF1 and its plant-specific regulator, OsGAP1, and determined the residues on OsGAP1 that are essential for its binding to OsYchF1. In this study, we employed site-directed mutagenesis to identify four critical residues on the TGS domain of OsYchF1 that are critical for its binding to OsGAP1. We also generated a docking model of the OsYchF1 : OsGAP1 complex to dissect the molecular basis of their interactions. Our finding not only reveals the roles of the key interacting residues controlling the binding between OsYchF1 and OsGAP1, but also provides a working model on the potential regulatory mechanism mediated by a TGS domain, particularly in the class of GTPase of the OBG family.
MeSH term(s)	Amino Acid Sequence ; Arabidopsis/metabolism ; C2 Domains/genetics ; GTP-Binding Proteins/chemistry ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; GTPase-Activating Proteins/chemistry ; GTPase-Activating Proteins/metabolism ; Gene Expression Regulation, Plant/genetics ; Models, Structural ; Molecular Docking Simulation ; Mutagenesis, Site-Directed ; Oryza/chemistry ; Oryza/genetics ; Oryza/metabolism ; Plant Proteins/chemistry ; Plant Proteins/metabolism ; Plants, Genetically Modified ; Protein Binding ; Protein Domains/genetics ; Real-Time Polymerase Chain Reaction ; Recombinant Proteins ; Stress, Physiological/genetics
Chemical Substances	GTPase-Activating Proteins ; Plant Proteins ; Recombinant Proteins ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2020-09-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20200380
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Article: Emerging roles of the neural adaptor FE65 in neurite outgrowth.

Li, Wen / Chan, Wai Wa Ray / Ngo, Jacky Chi Ki / Lau, Kwok-Fai

Neural regeneration research

2018 Volume 13, Issue 12, Page(s) 2085–2086

Language	English
Publishing date	2018-10-14
Publishing country	India
Document type	Journal Article
ZDB-ID	2388460-5
ISSN	1876-7958 ; 1673-5374
ISSN (online)	1876-7958
ISSN	1673-5374
DOI	10.4103/1673-5374.241449
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Article: A Peptidylic Inhibitor for Neutralizing

Zhang, Qian / An, Ying / Chen, Zhefan Stephen / Koon, Alex Chun / Lau, Kwok-Fai / Ngo, Jacky Chi Ki / Chan, Ho Yin Edwin

Molecular therapy. Nucleic acids

2019 Volume 16, Page(s) 172–185

Abstract: One drug, two diseases is a rare and economical therapeutic strategy that is highly desirable in the pharmaceutical industry. We previously reported a 21-amino acid peptide named beta-structured inhibitor for neurodegenerative diseases (BIND) that can ... ...

Abstract	One drug, two diseases is a rare and economical therapeutic strategy that is highly desirable in the pharmaceutical industry. We previously reported a 21-amino acid peptide named beta-structured inhibitor for neurodegenerative diseases (BIND) that can effectively inhibit expanded CAG trinucleotide toxicity in polyglutamine (polyQ) diseases. Here we report that BIND also effectively inhibits GGGGCC repeat-mediated neurodegeneration in vitro and in vivo. When fused with a cell-penetrating peptide derived from the transactivator of transcription (TAT) protein of the HIV, TAT-BIND reduces cell death, formation of GGGGCC RNA foci, and levels of poly-GR, poly-GA, and poly-GP dipeptide proteins in cell models of C9ORF72-associated amyotrophic lateral sclerosis and frontotemporal dementia (C9ALS-FTD). We showed that TAT-BIND disrupts the interaction between GGGGCC RNA and nucleolin protein, restores rRNA maturation, and inhibits mislocalization of nucleolin and B23, which eventually suppresses nucleolar stress in C9ALS-FTD. In a Drosophila model of C9ALS-FTD, TAT-BIND suppresses retinal degeneration, rescues climbing ability, and extends the lifespan of flies. In contrast, TAT-BIND has no effect on UAS-poly-glycine-arginine (poly-GR)
Language	English
Publishing date	2019-02-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	2662631-7
ISSN	2162-2531
ISSN	2162-2531
DOI	10.1016/j.omtn.2019.02.015
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Article ; Online: Protein-Protein Interaction Inhibitor of SRPKs Alters the Splicing Isoforms of VEGF and Inhibits Angiogenesis.

Li, Qingyun / Zeng, Chuyue / Liu, Haizhen / Yung, Kristen Wing Yu / Chen, Chun / Xie, Qiuling / Zhang, Yu / Wan, Stephanie Winn Chee / Mak, Bertha Sze Wing / Xia, Jiang / Xiong, Sheng / Ngo, Jacky Chi Ki

iScience

2021 Volume 24, Issue 5, Page(s) 102423

Abstract: Serine-arginine (SR) protein kinases (SRPKs) regulate the functions of the SR-rich splicing factors by phosphorylating multiple serines within their C-terminal arginine-serine-rich domains. Dysregulation of these phosphorylation events has been ... ...

Abstract	Serine-arginine (SR) protein kinases (SRPKs) regulate the functions of the SR-rich splicing factors by phosphorylating multiple serines within their C-terminal arginine-serine-rich domains. Dysregulation of these phosphorylation events has been implicated in many diseases, suggesting SRPKs are potential therapeutic targets. In particular, aberrant SRPK1 expression alters the balances of proangiogenic (VEGF
Language	English
Publishing date	2021-04-20
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2021.102423
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Article ; Online: Neuronal adaptor FE65 stimulates Rac1-mediated neurite outgrowth by recruiting and activating ELMO1.

Li, Wen / Tam, Ka Ming Vincent / Chan, Wai Wa Ray / Koon, Alex Chun / Ngo, Jacky Chi Ki / Chan, Ho Yin Edwin / Lau, Kwok-Fai

The Journal of biological chemistry

2018 Volume 293, Issue 20, Page(s) 7674–7688

Abstract: Neurite outgrowth is a crucial process in developing neurons for neural network formation. Understanding the regulatory mechanisms of neurite outgrowth is essential for developing strategies to stimulate neurite regeneration after nerve injury and in ... ...

Abstract	Neurite outgrowth is a crucial process in developing neurons for neural network formation. Understanding the regulatory mechanisms of neurite outgrowth is essential for developing strategies to stimulate neurite regeneration after nerve injury and in neurodegenerative disorders. FE65 is a brain-enriched adaptor that stimulates Rac1-mediated neurite elongation. However, the precise mechanism by which FE65 promotes the process remains elusive. Here, we show that ELMO1, a subunit of ELMO1-DOCK180 bipartite Rac1 guanine nucleotide exchange factor (GEF), interacts with the FE65 N-terminal region. Overexpression of FE65 and/or ELMO1 enhances, whereas knockdown of FE65 or ELMO1 inhibits, neurite outgrowth and Rac1 activation. The effect of FE65 alone or together with ELMO1 is attenuated by an FE65 double mutation that disrupts FE65-ELMO1 interaction. Notably, FE65 is found to activate ELMO1 by diminishing ELMO1 intramolecular autoinhibitory interaction and to promote the targeting of ELMO1 to the plasma membrane, where Rac1 is activated. We also show that FE65, ELMO1, and DOCK180 form a tripartite complex. Knockdown of DOCK180 reduces the stimulatory effect of FE65-ELMO1 on Rac1 activation and neurite outgrowth. Thus, we identify a novel mechanism by which FE65 stimulates Rac1-mediated neurite outgrowth by recruiting and activating ELMO1.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Movement ; Cells, Cultured ; Humans ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurogenesis ; Neuronal Outgrowth/physiology ; Neurons/cytology ; Neurons/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Rats ; rac1 GTP-Binding Protein/genetics ; rac1 GTP-Binding Protein/metabolism
Chemical Substances	APBB1 protein, human ; Adaptor Proteins, Signal Transducing ; ELMO1 protein, human ; Nerve Tissue Proteins ; Nuclear Proteins ; RAC1 protein, human ; rac1 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2018-04-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA117.000505
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Uc I Zs.108: Show issues

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Article ; Online: Attenuation of amyloid-β generation by atypical protein kinase C-mediated phosphorylation of engulfment adaptor PTB domain containing 1 threonine 35.

Chau, Dennis Dik-Long / Yung, Kristen Wing-Yu / Chan, William Wai-Lun / An, Ying / Hao, Yan / Chan, Ho-Yin Edwin / Ngo, Jacky Chi-Ki / Lau, Kwok-Fai

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2019 Volume 33, Issue 11, Page(s) 12019–12035

Abstract: Amyloid-β (Aβ) is derived from the proteolytic processing of amyloid precursor protein (APP), and the deposition of extracellular Aβ to form amyloid plaques is a pathologic hallmark of Alzheimer's disease (AD). Although reducing Aβ generation and ... ...

Abstract	Amyloid-β (Aβ) is derived from the proteolytic processing of amyloid precursor protein (APP), and the deposition of extracellular Aβ to form amyloid plaques is a pathologic hallmark of Alzheimer's disease (AD). Although reducing Aβ generation and accumulation has been proposed as a means of treating the disease, adverse side effects and unsatisfactory efficacy have been reported in several clinical trials that sought to lower Aβ levels. Engulfment adaptor phosphotyrosine-binding (PTB) domain containing 1 (GULP1) is a molecular adaptor that has been shown to interact with APP to alter Aβ production. Therefore, the modulation of the GULP1-APP interaction may be an alternative approach to reducing Aβ. However, the mechanisms that regulate GULP1-APP binding remain elusive. As GULP1 is a phosphoprotein, and because phosphorylation is a common mechanism that regulates protein interaction, we anticipated that GULP1 phosphorylation would influence GULP1-APP interaction and thereby Aβ production. We show here that the phosphorylation of GULP1 threonine 35 (T35) reduces GULP1-APP interaction and suppresses the stimulatory effect of GULP1 on APP processing. The residue is phosphorylated by an isoform of atypical PKC (PKCζ). Overexpression of PKCζ reduces both GULP1-APP interaction and GULP1-mediated Aβ generation. Moreover, the activation of PKCζ
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; CHO Cells ; Cell Line, Tumor ; Cricetulus ; HEK293 Cells ; Humans ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Protein Processing, Post-Translational ; Threonine/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; GULP1 protein, human ; Threonine (2ZD004190S) ; PKC-3 protein (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2019-08-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.201802825RR
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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Assessing a peptidylic inhibitor-based therapeutic approach that simultaneously suppresses polyglutamine RNA- and protein-mediated toxicities in patient cells and Drosophila.

Zhang, Qian / Tsoi, Ho / Peng, Shaohong / Li, Pan P / Lau, Kwok-Fai / Rudnicki, Dobrila D / Ngo, Jacky Chi-Ki / Chan, Ho Yin Edwin

Disease models & mechanisms

2016 Volume 9, Issue 3, Page(s) 321–334

Abstract: Polyglutamine (polyQ) diseases represent a group of progressive neurodegenerative disorders that are caused by abnormal expansion of CAG triplet nucleotides in disease genes. Recent evidence indicates that not only mutant polyQ proteins, but also their ... ...

Abstract	Polyglutamine (polyQ) diseases represent a group of progressive neurodegenerative disorders that are caused by abnormal expansion of CAG triplet nucleotides in disease genes. Recent evidence indicates that not only mutant polyQ proteins, but also their corresponding mutant RNAs, contribute to the pathogenesis of polyQ diseases. Here, we describe the identification of a 13-amino-acid peptide, P3, which binds directly and preferentially to long-CAG RNA within the pathogenic range. When administered to cell and Drosophila disease models, as well as to patient-derived fibroblasts, P3 inhibited expanded-CAG-RNA-induced nucleolar stress and suppressed neurotoxicity. We further examined the combined therapeutic effect of P3 and polyQ-binding peptide 1 (QBP1), a well-characterized polyQ protein toxicity inhibitor, on neurodegeneration. When P3 and QBP1 were co-administered to disease models, both RNA and protein toxicities were effectively mitigated, resulting in a notable improvement of neurotoxicity suppression compared with the P3 and QBP1 single-treatment controls. Our findings indicate that targeting toxic RNAs and/or simultaneous targeting of toxic RNAs and their corresponding proteins could open up a new therapeutic strategy for treating polyQ degeneration.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Death/drug effects ; Drosophila melanogaster/drug effects ; Drosophila melanogaster/metabolism ; HEK293 Cells ; Humans ; Models, Biological ; Nerve Degeneration/pathology ; Peptides/administration & dosage ; Peptides/chemistry ; Peptides/pharmacology ; Peptides/toxicity ; Phosphoproteins/metabolism ; RNA/toxicity ; RNA, Ribosomal/genetics ; RNA-Binding Proteins/metabolism ; Stress, Physiological ; Structure-Activity Relationship ; Transcription, Genetic/drug effects ; Transfection ; Trinucleotide Repeat Expansion/genetics ; Nucleolin
Chemical Substances	Peptides ; Phosphoproteins ; RNA, Ribosomal ; RNA-Binding Proteins ; polyglutamine (26700-71-0) ; RNA (63231-63-0)
Language	English
Publishing date	2016-02-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2451104-3
ISSN	1754-8411 ; 1754-8403
ISSN (online)	1754-8411
ISSN	1754-8403
DOI	10.1242/dmm.022350
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