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  1. Article ; Online: New vision on the new era of genome study.

    Kaur, Parwinder / Zhang, Baohong

    Functional & integrative genomics

    2022  Volume 22, Issue 1, Page(s) 1–2

    MeSH term(s) Genomics/trends
    Language English
    Publishing date 2022-01-17
    Publishing country Germany
    Document type Editorial
    ZDB-ID 2014670-X
    ISSN 1438-7948 ; 1438-793X
    ISSN (online) 1438-7948
    ISSN 1438-793X
    DOI 10.1007/s10142-022-00826-y
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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: High-Temperature Dielectric Relaxation and Electric Conduction Mechanisms in a LaCoO

    Singh, Surinder / Kaur, Anumeet / Kaur, Parwinder / Singh, Lakhwant

    ACS omega

    2023  Volume 8, Issue 28, Page(s) 25623–25638

    Abstract: This research study examines the high-temperature dielectric relaxation and electric conduction mechanisms in ( ...

    Abstract This research study examines the high-temperature dielectric relaxation and electric conduction mechanisms in (
    Language English
    Publishing date 2023-07-07
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.3c04490
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  3. Article ; Online: Protein Modelling Highlighted Key Catalytic Sites Involved in Position-Specific Glycosylation of Isoflavonoids

    Moon Sajid / Parwinder Kaur

    International Journal of Molecular Sciences, Vol 24, Iss 12356, p

    2023  Volume 12356

    Abstract: Uridine diphosphate glycosyltransferases (UGTs) are known for promiscuity towards sugar acceptors, a valuable characteristic for host plants but not desirable for heterologous biosynthesis. UGTs characterized for the O-glycosylation of isoflavonoids have ...

    Abstract Uridine diphosphate glycosyltransferases (UGTs) are known for promiscuity towards sugar acceptors, a valuable characteristic for host plants but not desirable for heterologous biosynthesis. UGTs characterized for the O-glycosylation of isoflavonoids have shown a variable efficiency, substrate preference, and OH site specificity. Thus, 22 UGTs with reported isoflavonoid O-glycosylation activity were analyzed and ranked for OH site specificity and catalysis efficiency. Multiple-sequence alignment (MSA) showed a 33.2% pairwise identity and 4.5% identical sites among selected UGTs. MSA and phylogenetic analysis highlighted a comparatively higher amino acid substitution rate in the N-terminal domain that likely led to a higher specificity for isoflavonoids. Based on the docking score, OH site specificity, and physical and chemical features of active sites, selected UGTs were divided into three groups. A significantly high pairwise identity (67.4%) and identical sites (31.7%) were seen for group 1 UGTs. The structural and chemical composition of active sites highlighted key amino acids that likely define substrate preference, OH site specificity, and glycosylation efficiency towards selected (iso)flavonoids. In conclusion, physical and chemical parameters of active sites likely control the position-specific glycosylation of isoflavonoids. The present study will help the heterologous biosynthesis of glycosylated isoflavonoids and protein engineering efforts to improve the substrate and site specificity of UGTs.
    Keywords glycosylation ; UGTs ; substrate and OH site specificity ; isoflavonoids ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 540 ; 572
    Language English
    Publishing date 2023-08-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
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  4. Article ; Online: High-Temperature Dielectric Relaxation and Electric Conduction Mechanisms in a LaCoO3‑Modified Na0.5Bi0.5TiO3 System

    Surinder Singh / Anumeet Kaur / Parwinder Kaur / Lakhwant Singh

    ACS Omega, Vol 8, Iss 28, Pp 25623-

    2023  Volume 25638

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
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  5. Article ; Online: Protein Modelling Highlighted Key Catalytic Sites Involved in Position-Specific Glycosylation of Isoflavonoids.

    Sajid, Moon / Kaur, Parwinder

    International journal of molecular sciences

    2023  Volume 24, Issue 15

    Abstract: Uridine diphosphate glycosyltransferases (UGTs) are known for promiscuity towards sugar acceptors, a valuable characteristic for host plants but not desirable for heterologous biosynthesis. UGTs characterized for the O-glycosylation of isoflavonoids have ...

    Abstract Uridine diphosphate glycosyltransferases (UGTs) are known for promiscuity towards sugar acceptors, a valuable characteristic for host plants but not desirable for heterologous biosynthesis. UGTs characterized for the O-glycosylation of isoflavonoids have shown a variable efficiency, substrate preference, and OH site specificity. Thus, 22 UGTs with reported isoflavonoid O-glycosylation activity were analyzed and ranked for OH site specificity and catalysis efficiency. Multiple-sequence alignment (MSA) showed a 33.2% pairwise identity and 4.5% identical sites among selected UGTs. MSA and phylogenetic analysis highlighted a comparatively higher amino acid substitution rate in the N-terminal domain that likely led to a higher specificity for isoflavonoids. Based on the docking score, OH site specificity, and physical and chemical features of active sites, selected UGTs were divided into three groups. A significantly high pairwise identity (67.4%) and identical sites (31.7%) were seen for group 1 UGTs. The structural and chemical composition of active sites highlighted key amino acids that likely define substrate preference, OH site specificity, and glycosylation efficiency towards selected (iso)flavonoids. In conclusion, physical and chemical parameters of active sites likely control the position-specific glycosylation of isoflavonoids. The present study will help the heterologous biosynthesis of glycosylated isoflavonoids and protein engineering efforts to improve the substrate and site specificity of UGTs.
    MeSH term(s) Glycosylation ; Catalytic Domain ; Phylogeny ; Glycosyltransferases/metabolism ; Uridine Diphosphate/metabolism ; Flavones ; Substrate Specificity
    Chemical Substances Glycosyltransferases (EC 2.4.-) ; Uridine Diphosphate (58-98-0) ; Flavones
    Language English
    Publishing date 2023-08-02
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241512356
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  6. Article: Bioprospecting microbes and enzymes for the production of pterocarpans and coumestans.

    Perez Rojo, Fernando / Pillow, J Jane / Kaur, Parwinder

    Frontiers in bioengineering and biotechnology

    2023  Volume 11, Page(s) 1154779

    Abstract: The isoflavonoid derivatives, pterocarpans and coumestans, are explored for multiple clinical applications as osteo-regenerative, neuroprotective and anti-cancer agents. The use of plant-based systems to produce isoflavonoid derivatives is limited due to ...

    Abstract The isoflavonoid derivatives, pterocarpans and coumestans, are explored for multiple clinical applications as osteo-regenerative, neuroprotective and anti-cancer agents. The use of plant-based systems to produce isoflavonoid derivatives is limited due to cost, scalability, and sustainability constraints. Microbial cell factories overcome these limitations in which model organisms such as
    Language English
    Publishing date 2023-04-28
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2719493-0
    ISSN 2296-4185
    ISSN 2296-4185
    DOI 10.3389/fbioe.2023.1154779
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  7. Article ; Online: Analysing potent biomarkers along phytochemicals for breast cancer therapy: an in silico approach.

    Shekar, Nivruthi / Vuong, Paton / Kaur, Parwinder

    Breast cancer research and treatment

    2023  Volume 203, Issue 1, Page(s) 29–47

    Abstract: Purpose: This research focused on the identification of herbal compounds as potential anti-cancer drugs, especially for breast cancer, that involved the recognition of Notch downstream targets NOTCH proteins (1-4) specifically expressed in breast ... ...

    Abstract Purpose: This research focused on the identification of herbal compounds as potential anti-cancer drugs, especially for breast cancer, that involved the recognition of Notch downstream targets NOTCH proteins (1-4) specifically expressed in breast tumours as biomarkers for prognosis, along with P53 tumour antigens, that were used as comparisons to check the sensitivity of the herbal bio-compounds.
    Methods: After investigating phytochemical candidates, we employed an approach for computer-aided drug design and analysis to find strong breast cancer inhibitors. The present study utilized in silico analyses and protein docking techniques to characterize and rank selected bio-compounds for their efficiency in oncogenic inhibition for use in precise carcinomic cell growth control.
    Results: Several of the identified phytocompounds found in herbs followed Lipinski's Rule of Five and could be further investigated as potential medicinal molecules. Based on the Vina score obtained after the docking process, the active compound Epigallocatechin gallate in green tea with NOTCH (1-4) and P53 proteins showed promising results for future drug repurposing. The stiffness and binding stability of green tea pharmacological complexes were further elucidated by the molecular dynamic simulations carried out for the highest scoring phytochemical ligand complex.
    Conclusion: The target-ligand complex of green tea active compound Epigallocatechin gallate with NOTCH (1-4) had the potential to become potent anti-breast cancer therapeutic candidates following further research involving wet-lab experiments.
    MeSH term(s) Humans ; Female ; Breast Neoplasms/drug therapy ; Breast Neoplasms/genetics ; Molecular Docking Simulation ; Ligands ; Tumor Suppressor Protein p53/genetics ; Tea/chemistry ; Biomarkers ; Phytochemicals/pharmacology ; Phytochemicals/therapeutic use
    Chemical Substances Ligands ; Tumor Suppressor Protein p53 ; Tea ; Biomarkers ; Phytochemicals
    Language English
    Publishing date 2023-09-20
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 604563-7
    ISSN 1573-7217 ; 0167-6806
    ISSN (online) 1573-7217
    ISSN 0167-6806
    DOI 10.1007/s10549-023-07107-7
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1655: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  8. Article ; Online: Ten simple rules for investigating (meta)genomic data from environmental ecosystems.

    Vuong, Paton / Wise, Michael J / Whiteley, Andrew S / Kaur, Parwinder

    PLoS computational biology

    2022  Volume 18, Issue 12, Page(s) e1010675

    MeSH term(s) Ecosystem ; Genomics
    Language English
    Publishing date 2022-12-08
    Publishing country United States
    Document type Editorial
    ZDB-ID 2193340-6
    ISSN 1553-7358 ; 1553-734X
    ISSN (online) 1553-7358
    ISSN 1553-734X
    DOI 10.1371/journal.pcbi.1010675
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  9. Article ; Online: Ten simple rules for investigating (meta)genomic data from environmental ecosystems

    Paton Vuong / Michael J. Wise / Andrew S. Whiteley / Parwinder Kaur

    PLoS Computational Biology, Vol 18, Iss

    2022  Volume 12

    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-12-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
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  10. Article: Phylogenetic Analysis and Protein Modelling of Isoflavonoid Synthase Highlights Key Catalytic Sites towards Realising New Bioengineering Endeavours.

    Sajid, Moon / Stone, Shane R / Kaur, Parwinder

    Bioengineering (Basel, Switzerland)

    2022  Volume 9, Issue 11

    Abstract: Isoflavonoid synthase (IFS) is a critical enzyme for the biosynthesis of over 2400 isoflavonoids. Isoflavonoids are an important class of plant secondary metabolites that have a range of pharmaceutical and nutraceutical properties. With growing interest ... ...

    Abstract Isoflavonoid synthase (IFS) is a critical enzyme for the biosynthesis of over 2400 isoflavonoids. Isoflavonoids are an important class of plant secondary metabolites that have a range of pharmaceutical and nutraceutical properties. With growing interest in isoflavonoids from both research and industrial perspectives, efforts are being forwarded to enhance isoflavonoid production in-planta and ex-planta; therefore, in-silico analysis and characterisation of available IFS protein sequences are needed. The present study is the first-ever attempt toward phylogenetic analysis and protein modelling of available IFS protein sequences. Phylogenetic analysis has shown that IFS amino acid sequences have 86.4% pairwise identity and 26.5% identical sites, and the sequences were grouped into six different clades. The presence of a β-hairpin and extra loop at catalytic sites of
    Language English
    Publishing date 2022-10-24
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2746191-9
    ISSN 2306-5354
    ISSN 2306-5354
    DOI 10.3390/bioengineering9110609
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