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  1. Artikel ; Online: Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens.

    Harsolia, Ram Swaroop / Kanwar, Ambika / Gour, Shalini / Kumar, Vijay / Kumar, Vikas / Bansal, Rati / Kumar, Suman / Singh, Manish / Yadav, Jay Kant

    International journal of biological macromolecules

    2020  Band 163, Seite(n) 702–710

    Abstract: The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for ... ...

    Abstract The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for conformational change required for the self-assembly. To examine the presence of APRs, we systematically analyzed the primary structures of β-crystallins. Out of seven subtypes, the βB1-crystallin found to possess the highest aggregation score with 9 APRs in its primary structure. To confirm the amyloidogenic nature of these newly identified APRs, we further studied the aggregation behavior of one of the APRs spanning from 174 to 180 residues (
    Mesh-Begriff(e) Adsorption ; Amyloidogenic Proteins/chemistry ; Amyloidogenic Proteins/isolation & purification ; Amyloidogenic Proteins/metabolism ; Amyloidogenic Proteins/ultrastructure ; Amyloidosis ; Cataract/metabolism ; Chemical Phenomena ; Congo Red/chemistry ; Lens, Crystalline/chemistry ; Lens, Crystalline/metabolism ; Molecular Dynamics Simulation ; Protein Aggregates ; Protein Conformation ; Solubility ; Structure-Activity Relationship ; beta-Crystallin B Chain/chemistry ; beta-Crystallin B Chain/metabolism
    Chemische Substanzen Amyloidogenic Proteins ; Protein Aggregates ; beta-Crystallin B Chain ; Congo Red (3U05FHG59S)
    Sprache Englisch
    Erscheinungsdatum 2020-07-08
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2020.07.028
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens

    Harsolia, Ram Swaroop / Kanwar, Ambika / Gour, Shalini / Kumar, Vijay / Kumar, Vikas / Bansal, Rati / Kumar, Suman / Singh, Manish / Yadav, Jay Kant

    International journal of biological macromolecules. 2020 Nov. 15, v. 163

    2020  

    Abstract: The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for ... ...

    Abstract The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for conformational change required for the self-assembly. To examine the presence of APRs, we systematically analyzed the primary structures of β-crystallins. Out of seven subtypes, the βB1-crystallin found to possess the highest aggregation score with 9 APRs in its primary structure. To confirm the amyloidogenic nature of these newly identified APRs, we further studied the aggregation behavior of one of the APRs spanning from 174 to 180 residues (¹⁷⁴LWVYGFS¹⁸⁰) of βB1-crystallin, which is referred as βB1₍₁₇₄₋₁₈₀₎. Under in vitro conditions, the synthetic analogue of βB1₍₁₇₄₋₁₈₀₎ peptide formed visible aggregates and displayed high Congo red (CR) bathochromic shift, Thioflavin T (ThT) binding and fibrilar morphology under transmission electron microscopy, which are the typical characteristics of amyloids. Further, the aggregated βB1₍₁₇₄₋₁₈₀₎ was found to induce aggregation of the soluble fraction of proteins isolated from the human cataractous lens. This observation suggests that the presence of APRs in βB1-crystallin might be serving as one of the intrinsic supplementary factors responsible for constitutive aggregation behavior of βB1-crystallin and development of cataract.
    Schlagwörter aggregation behavior ; amyloid ; cataract ; eye lens ; humans ; peptides ; transmission electron microscopy
    Sprache Englisch
    Erscheinungsverlauf 2020-1115
    Umfang p. 702-710.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    Anmerkung NAL-AP-2-clean
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2020.07.028
    Datenquelle NAL Katalog (AGRICOLA)

    Volltext online

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    Verfügbar in ZB MED Köln/Königswinter

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    ab Jg. 2022: Lesesaal (EG)

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    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

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