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  1. Article ; Online: In silico

    Kaur, Apneet / Goyal, Bhupesh

    Journal of biomolecular structure & dynamics

    2023  , Page(s) 1–16

    Abstract: The aberrant misfolding and self-aggregation of human islet amyloid polypeptide (hIAPP or amylin) into cytotoxic aggregates are implicated in the pathogenesis of type 2 diabetes (T2D). Among various inhibitors, short peptides derived from the ... ...

    Abstract The aberrant misfolding and self-aggregation of human islet amyloid polypeptide (hIAPP or amylin) into cytotoxic aggregates are implicated in the pathogenesis of type 2 diabetes (T2D). Among various inhibitors, short peptides derived from the amyloidogenic regions of hIAPP have been employed as hIAPP aggregation inhibitors due to their low immunogenicity, biocompatibility, and high chemical diversity. Recently, hIAPP fragment HSSNN
    Language English
    Publishing date 2023-09-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2023.2254411
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2093: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  2. Article ; Online: Identification of new pentapeptides as potential inhibitors of amyloid-β

    Kaur, Apneet / Goyal, Bhupesh

    Journal of molecular graphics & modelling

    2023  Volume 124, Page(s) 108558

    Abstract: Alzheimer's disease (AD) is a multifactorial neurodegenerative disease mainly characterized by extracellular accumulation of amyloid-β (Aβ) peptide. Previous studies reported pentapeptide RIIGL as an effective inhibitor of Aβ aggregation and ... ...

    Abstract Alzheimer's disease (AD) is a multifactorial neurodegenerative disease mainly characterized by extracellular accumulation of amyloid-β (Aβ) peptide. Previous studies reported pentapeptide RIIGL as an effective inhibitor of Aβ aggregation and neurotoxicity induced by Aβ aggregates. In this work, a library of 912 pentapeptides based on RIIGL has been designed and assessed for their efficacy to inhibit Aβ
    MeSH term(s) Humans ; Molecular Dynamics Simulation ; Molecular Docking Simulation ; Neurodegenerative Diseases ; Amyloid beta-Peptides/chemistry ; Alzheimer Disease/metabolism ; Peptide Fragments/chemistry
    Chemical Substances Amyloid beta-Peptides ; Peptide Fragments
    Language English
    Publishing date 2023-06-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1396450-1
    ISSN 1873-4243 ; 1093-3263
    ISSN (online) 1873-4243
    ISSN 1093-3263
    DOI 10.1016/j.jmgm.2023.108558
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3491: Show issues Location:
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  3. Article ; Online: Mechanistic insights into the mitigation of Aβ aggregation and protofibril destabilization by a D-enantiomeric decapeptide rk10.

    Singh, Kamaljot / Kaur, Anupamjeet / Goyal, Deepti / Goyal, Bhupesh

    Physical chemistry chemical physics : PCCP

    2022  Volume 24, Issue 36, Page(s) 21975–21994

    Abstract: According to clinical studies, the development of Alzheimer's disease (AD) is linked to the abnormal aggregation of amyloid-β (Aβ) peptides into toxic soluble oligomers, protofibrils as well as mature fibrils. The most acceptable therapeutic strategy for ...

    Abstract According to clinical studies, the development of Alzheimer's disease (AD) is linked to the abnormal aggregation of amyloid-β (Aβ) peptides into toxic soluble oligomers, protofibrils as well as mature fibrils. The most acceptable therapeutic strategy for the treatment of AD is to block the Aβ aggregation. Sun and co-workers have reported a decapeptide, D-enantiomeric RTHLVFFARK-NH
    MeSH term(s) Alzheimer Disease/metabolism ; Amides ; Amyloid/chemistry ; Amyloid beta-Peptides/chemistry ; Humans ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Peptide Fragments/chemistry ; Protein Conformation, beta-Strand ; Protons
    Chemical Substances Amides ; Amyloid ; Amyloid beta-Peptides ; Peptide Fragments ; Protons
    Language English
    Publishing date 2022-09-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 1476244-4
    ISSN 1463-9084 ; 1463-9076
    ISSN (online) 1463-9084
    ISSN 1463-9076
    DOI 10.1039/d2cp02601e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Unravelling the destabilization potential of ellagic acid on α-synuclein fibrils using molecular dynamics simulations.

    Mankoo, Opinder Kaur / Kaur, Anupamjeet / Goyal, Deepti / Goyal, Bhupesh

    Physical chemistry chemical physics : PCCP

    2023  Volume 25, Issue 11, Page(s) 8128–8143

    Abstract: The aberrant deposition of α-synuclein (α-Syn) protein into the intracellular neuronal aggregates termed Lewy bodies and Lewy neurites characterizes the devastating neurodegenerative condition known as Parkinson's disease (PD). The disruption of pre- ... ...

    Abstract The aberrant deposition of α-synuclein (α-Syn) protein into the intracellular neuronal aggregates termed Lewy bodies and Lewy neurites characterizes the devastating neurodegenerative condition known as Parkinson's disease (PD). The disruption of pre-existing disease-relevant α-Syn fibrils is recognized as a viable therapeutic approach for PD. Ellagic acid (EA), a natural polyphenolic compound, is experimentally proven as a potential candidate that prevents or reverses the α-Syn fibrillization process. However, the detailed inhibitory mechanism of EA against the destabilization of α-Syn fibril remains largely unclear. In this work, the influence of EA on α-Syn fibril and its putative binding mechanism were explored using molecular dynamics (MD) simulations. EA interacted primarily with the non-amyloid-β component (NAC) of α-Syn fibril, disrupting its β-sheet content and thereby increasing the coil content. The E46-K80 salt bridge, critical for the stability of Greek-key-like α-Syn fibril, was disrupted in the presence of EA. The binding free energy analysis using the MM-PBSA method demonstrates the favourable binding of EA to α-Syn fibril (Δ
    MeSH term(s) Humans ; alpha-Synuclein/chemistry ; Molecular Dynamics Simulation ; Ellagic Acid/pharmacology ; Parkinson Disease ; Neurodegenerative Diseases
    Chemical Substances alpha-Synuclein ; Ellagic Acid (19YRN3ZS9P)
    Language English
    Publishing date 2023-03-15
    Publishing country England
    Document type Journal Article
    ZDB-ID 1476244-4
    ISSN 1463-9084 ; 1463-9076
    ISSN (online) 1463-9084
    ISSN 1463-9076
    DOI 10.1039/d2cp06006j
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Unveiling How Hydroxytyrosol Destabilizes α-Syn Oligomers Using Molecular Simulations.

    Kaur, Gagandeep / Mankoo, Opinder Kaur / Goyal, Deepti / Goyal, Bhupesh

    The journal of physical chemistry. B

    2023  Volume 127, Issue 25, Page(s) 5620–5632

    Abstract: The etiology of Parkinson's disease (PD) is mainly linked to the α-synuclein (α-Syn) fibrillogenesis. Hydroxytyrosol (HT), also known as 3,4-dihydroxyphenylethanol, is a naturally occurring polyphenol, found in extra virgin olive oil, and has been shown ... ...

    Abstract The etiology of Parkinson's disease (PD) is mainly linked to the α-synuclein (α-Syn) fibrillogenesis. Hydroxytyrosol (HT), also known as 3,4-dihydroxyphenylethanol, is a naturally occurring polyphenol, found in extra virgin olive oil, and has been shown to have cardioprotective, anticancer, antiobesity, and antidiabetic properties. HT has neuroprotective benefits in neurodegenerative diseases and lessens the severity of PD by reducing the aggregation of α-Syn and destabilizing the preformed toxic α-Syn oligomers. However, the molecular mechanism by which HT destabilizes α-Syn oligomers and alleviates the accompanying cytotoxicity remains unexplored. The impact of HT on the α-Syn oligomer structure and its potential binding mechanism was examined in this work by employing molecular dynamics (MD) simulations. The secondary structure analysis depicted that HT significantly reduces the β-sheet and concomitantly increases the coil content of α-Syn trimer. Visualization of representative conformations from the clustering analysis depicted the hydrogen bond interactions of the hydroxyl groups in HT with the N-terminal and nonamyloid-β component (NAC) region residues of α-Syn trimer, which, in turn, leads to the weakening of interchain interactions in α-Syn trimer and resulted in the disruption of the α-Syn oligomer. The binding free energy calculations depict that HT binds favorably to α-Syn trimer (Δ
    MeSH term(s) Humans ; alpha-Synuclein/chemistry ; Parkinson Disease/metabolism ; Phenylethyl Alcohol/pharmacology ; Neurodegenerative Diseases/metabolism
    Chemical Substances alpha-Synuclein ; 3,4-dihydroxyphenylethanol (10597-60-1) ; Phenylethyl Alcohol (ML9LGA7468)
    Language English
    Publishing date 2023-06-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.3c02434
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Structural and molecular insights into tacrine-benzofuran hybrid induced inhibition of amyloid-β peptide aggregation and BACE1 activity.

    Kaur, Rajdeep / Narang, Simranjeet Singh / Singh, Pritpal / Goyal, Bhupesh

    Journal of biomolecular structure & dynamics

    2023  Volume 41, Issue 22, Page(s) 13211–13227

    Abstract: Amyloid-β (Aβ) aggregation and β-amyloid precursor protein cleaving enzyme 1 (BACE1) are the potential therapeutic drug targets for Alzheimer's disease (AD). A recent study highlighted that tacrine-benzofuran hybrid C1 displayed anti-aggregation activity ...

    Abstract Amyloid-β (Aβ) aggregation and β-amyloid precursor protein cleaving enzyme 1 (BACE1) are the potential therapeutic drug targets for Alzheimer's disease (AD). A recent study highlighted that tacrine-benzofuran hybrid C1 displayed anti-aggregation activity against Aβ
    MeSH term(s) Humans ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Protein Precursor ; Tacrine/pharmacology ; Amyloid Precursor Protein Secretases ; Ligands ; Aspartic Acid Endopeptidases ; Alzheimer Disease/drug therapy ; Molecular Dynamics Simulation ; Benzofurans/pharmacology ; Peptide Fragments/chemistry
    Chemical Substances Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Tacrine (4VX7YNB537) ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Ligands ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; Benzofurans ; Peptide Fragments ; BACE1 protein, human (EC 3.4.23.46)
    Language English
    Publishing date 2023-04-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2023.2191722
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2093: 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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  7. Article ; Online: Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy.

    Goyal, Bhupesh / Goyal, Deepti

    ACS combinatorial science

    2020  Volume 22, Issue 6, Page(s) 297–305

    Abstract: A new coronavirus (CoV) caused a pandemic named COVID-19, which has become a global health care emergency in the present time. The virus is referred to as SARS-CoV-2 (severe acute respiratory syndrome-coronavirus-2) and has a genome similar (∼82%) to ... ...

    Abstract A new coronavirus (CoV) caused a pandemic named COVID-19, which has become a global health care emergency in the present time. The virus is referred to as SARS-CoV-2 (severe acute respiratory syndrome-coronavirus-2) and has a genome similar (∼82%) to that of the previously known SARS-CoV (SARS coronavirus). An attractive therapeutic target for CoVs is the main protease (M
    MeSH term(s) Antiviral Agents/pharmacology ; Betacoronavirus/chemistry ; Betacoronavirus/drug effects ; Betacoronavirus/enzymology ; Betacoronavirus/genetics ; COVID-19 ; Coronavirus 3C Proteases ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Cysteine Endopeptidases/chemistry ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Drug Discovery ; Humans ; Models, Molecular ; Molecular Targeted Therapy ; Mutation/drug effects ; Pandemics ; Peptides/pharmacology ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/virology ; Protease Inhibitors/pharmacology ; Protein Conformation/drug effects ; Protein Multimerization/drug effects ; SARS-CoV-2 ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism
    Chemical Substances Antiviral Agents ; Peptides ; Protease Inhibitors ; Viral Nonstructural Proteins ; Cysteine Endopeptidases (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
    Keywords covid19
    Language English
    Publishing date 2020-05-27
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2156-8944
    ISSN (online) 2156-8944
    DOI 10.1021/acscombsci.0c00058
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Reply.

    Goyal, Bhupesh K

    Medical journal, Armed Forces India

    2015  Volume 71, Issue 3, Page(s) 303

    Language English
    Publishing date 2015-08-18
    Publishing country India
    Document type Journal Article
    ZDB-ID 196342-9
    ISSN 0377-1237
    ISSN 0377-1237
    DOI 10.1016/j.mjafi.2015.06.002
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    Zs.A 6511: Show issues Location:
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  9. Article ; Online: Triazole-Peptide Conjugate as a Modulator of Aβ-Aggregation, Metal-Mediated Aβ-Aggregation, and Cytotoxicity.

    Mann, Sukhmani / Kaur, Anupamjeet / Kaur, Amandeep / Priyadarshi, Nitesh / Goyal, Bhupesh / Singhal, Nitin Kumar / Goyal, Deepti

    ACS chemical neuroscience

    2023  Volume 14, Issue 9, Page(s) 1631–1645

    Abstract: Amyloid-β (Aβ) aggregation plays a key role in the pathogenesis of Alzheimer's disease (AD). Along with this, the presence of redox-active metals like ... ...

    Abstract Amyloid-β (Aβ) aggregation plays a key role in the pathogenesis of Alzheimer's disease (AD). Along with this, the presence of redox-active metals like Cu
    MeSH term(s) Humans ; Triazoles/pharmacology ; Triazoles/chemistry ; Neuroblastoma ; Amyloid beta-Peptides/metabolism ; Alzheimer Disease/metabolism ; Molecular Dynamics Simulation ; Metals ; Peptide Fragments/metabolism
    Chemical Substances Triazoles ; Amyloid beta-Peptides ; Metals ; Peptide Fragments
    Language English
    Publishing date 2023-04-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1948-7193
    ISSN (online) 1948-7193
    DOI 10.1021/acschemneuro.3c00041
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  10. Article ; Online: How Does the Mono-Triazole Derivative Modulate Aβ

    Kaur, Amandeep / Kaur, Anupamjeet / Goyal, Deepti / Goyal, Bhupesh

    ACS omega

    2020  Volume 5, Issue 25, Page(s) 15606–15619

    Abstract: Clinical studies have identified that abnormal self-assembly of amyloid-β (Aβ) peptide into toxic fibrillar aggregates is associated with the pathology of Alzheimer's disease (AD). The most acceptable therapeutic approach to stop the progression of AD is ...

    Abstract Clinical studies have identified that abnormal self-assembly of amyloid-β (Aβ) peptide into toxic fibrillar aggregates is associated with the pathology of Alzheimer's disease (AD). The most acceptable therapeutic approach to stop the progression of AD is to inhibit the formation of β-sheet-rich structures. Recently, we designed and evaluated a series of novel mono-triazole derivatives
    Language English
    Publishing date 2020-06-22
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.0c01825
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