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  1. Article ; Online: Polyprotein synthesis: a journey from the traditional pre-translational method to modern post-translational approaches for single-molecule force spectroscopy.

    Kaur, Veerpal / Garg, Surbhi / Rakshit, Sabyasachi

    Chemical communications (Cambridge, England)

    2023  Volume 59, Issue 46, Page(s) 6946–6955

    Abstract: Polyproteins, an array of protein units of similar or differential functions in tandem, have been extensively utilized by organisms, unicellular or multicellular, as concentrators of the myriad of molecular activities. Most eukaryotic proteins, two- ... ...

    Abstract Polyproteins, an array of protein units of similar or differential functions in tandem, have been extensively utilized by organisms, unicellular or multicellular, as concentrators of the myriad of molecular activities. Most eukaryotic proteins, two-thirds in unicellular organisms, and more than 80% in metazoans, are polyproteins. Although the use of polyproteins continues to evolve in nature, our understanding of the structure-function-property of polyproteins is still limited. Cumbersome recombinant strategies and the lack of convenient
    MeSH term(s) Polyproteins/chemistry ; Proteins ; Protein Processing, Post-Translational ; Mechanical Phenomena ; Spectrum Analysis
    Chemical Substances Polyproteins ; Proteins
    Language English
    Publishing date 2023-06-06
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d3cc01756g
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Redefining the Structure of Tip Links in Hair Cells.

    Kaur, Veerpal / Ghosh, Sanat K / Bhatia, Tripta / Rakshit, Sabyasachi

    Biochemistry

    2023  Volume 62, Issue 15, Page(s) 2244–2251

    Abstract: Tip links are seen under microscopes as double-helical tetrameric complexes of long nonclassical cadherins, cadherin-23 and protocadherin-15. The twisted filamentous structure enables tip links to regulate mechanotransduction in hearing and balance. ... ...

    Abstract Tip links are seen under microscopes as double-helical tetrameric complexes of long nonclassical cadherins, cadherin-23 and protocadherin-15. The twisted filamentous structure enables tip links to regulate mechanotransduction in hearing and balance. While the molecular details of the double-helical protocadherin-15
    MeSH term(s) Mechanotransduction, Cellular/physiology ; Protocadherins ; Hair Cells, Auditory/metabolism ; Lipids ; Hair/metabolism ; Cadherins/metabolism
    Chemical Substances Protocadherins ; Lipids ; Cadherins
    Language English
    Publishing date 2023-07-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.3c00161
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Instantaneous splicing and excision of inteins to synthesize polyproteins on a substrate with tunable linkers.

    Kaur, Veerpal / Garg, Surbhi / Rakshit, Sabyasachi

    Soft matter

    2022  Volume 18, Issue 3, Page(s) 602–608

    Abstract: Nature has adapted chimeric polyproteins to achieve superior and multiplexed functionality in a single protein. However, the hurdles ... ...

    Abstract Nature has adapted chimeric polyproteins to achieve superior and multiplexed functionality in a single protein. However, the hurdles in
    MeSH term(s) Inteins/genetics ; Peptides ; Polyproteins ; Protein Domains ; Proteins
    Chemical Substances Peptides ; Polyproteins ; Proteins
    Language English
    Publishing date 2022-01-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 2191476-X
    ISSN 1744-6848 ; 1744-683X
    ISSN (online) 1744-6848
    ISSN 1744-683X
    DOI 10.1039/d1sm01469b
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Aminoindole and naphthalimide based charge transfer fluorescent probes for pH sensing and live cell imaging.

    Sharma, Sushil / Srinivas, Sai / Rakshit, Sabyasachi / Sengupta, Sanchita

    Organic & biomolecular chemistry

    2022  Volume 20, Issue 47, Page(s) 9422–9430

    Abstract: Fluorescent probes are essential for imaging of cancer cells and for tracking organelles inside cells. We have synthesized three molecular rotors AIN, AINP and F-AINP based on 1-aminoindole (AI) as an electron donor and naphthalimide as an electron ... ...

    Abstract Fluorescent probes are essential for imaging of cancer cells and for tracking organelles inside cells. We have synthesized three molecular rotors AIN, AINP and F-AINP based on 1-aminoindole (AI) as an electron donor and naphthalimide as an electron acceptor. All compounds showed charge transfer (CT) character, aggregation induced emission (AIE) and emission responsiveness towards temperature variation and solvent viscosity. AINP was most sensitive towards viscosity among all molecules with a viscosity sensitivity of ∼0.37. AIN, AINP and F-AINP showed negative temperature coefficients in chloroform with internal sensitivities of -0.04% °C
    MeSH term(s) Naphthalimides ; Fluorescent Dyes ; Hydrogen-Ion Concentration
    Chemical Substances Naphthalimides ; Fluorescent Dyes
    Language English
    Publishing date 2022-12-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/d2ob01614a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Anisotropy in mechanical unfolding of protein upon partner-assisted pulling and handle-assisted pulling.

    Arora, Nisha / Hazra, Jagadish Prasad / Rakshit, Sabyasachi

    Communications biology

    2021  Volume 4, Issue 1, Page(s) 925

    Abstract: Proteins as force-sensors respond to mechanical cues and regulate signaling in physiology. Proteins commonly connect the source and response points of mechanical cues in two conformations, independent proteins in end-to-end geometry and protein complexes ...

    Abstract Proteins as force-sensors respond to mechanical cues and regulate signaling in physiology. Proteins commonly connect the source and response points of mechanical cues in two conformations, independent proteins in end-to-end geometry and protein complexes in handshake geometry. The force-responsive property of independent proteins in end-to-end geometry is studied extensively using single-molecule force spectroscopy (SMFS). The physiological significance of the complex conformations in force-sensing is often disregarded as mere surge protectors. However, with the potential of force-steering, protein complexes possess a distinct mechano-responsive property over individual force-sensors. To decipher, we choose a force-sensing protein, cadherin-23, from tip-link complex and perform SMFS using end-to-end geometry and handshake complex geometry. We measure higher force-resilience of cadherin-23 with preferential shorter extensions in handshake mode of pulling over the direct mode. The handshake geometry drives the force-response of cadherin-23 through different potential-energy landscapes than direct pulling. Analysis of the dynamic network structure of cadherin-23 under tension indicates narrow force-distributions among residues in cadherin-23 in direct pulling, resulting in low force-dissipation paths and low resilience to force. Overall, the distinct and superior mechanical responses of cadherin-23 in handshake geometry than single protein geometry highlight a probable evolutionary drive of protein-protein complexes as force-conveyors over independent ones.
    MeSH term(s) Anisotropy ; Biomechanical Phenomena ; Cadherins/chemistry ; Cadherins/metabolism ; Protein Unfolding
    Chemical Substances Cadherins
    Language English
    Publishing date 2021-07-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-021-02445-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Emergence of slip-ideal-slip behavior in tip-links serve as force filters of sound in hearing.

    Arora, Nisha / Hazra, Jagadish P / Roy, Sandip / Bhati, Gaurav K / Gupta, Sarika / Yogendran, K P / Chaudhuri, Abhishek / Sagar, Amin / Rakshit, Sabyasachi

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 1595

    Abstract: Tip-links in the inner ear convey force from sound and trigger mechanotransduction. Here, we present evidence that tip-links (collectively as heterotetrameric complexes of cadherins) function as force filters during mechanotransduction. Our force-clamp ... ...

    Abstract Tip-links in the inner ear convey force from sound and trigger mechanotransduction. Here, we present evidence that tip-links (collectively as heterotetrameric complexes of cadherins) function as force filters during mechanotransduction. Our force-clamp experiments reveal that the tip-link complexes show slip-ideal-slip bond dynamics. At low forces, the lifetime of the tip-link complex drops monotonically, indicating slip-bond dynamics. The ideal bond, rare in nature, is seen in an intermediate force regime where the survival of the complex remains constant over a wide range. At large forces, tip-links follow a slip bond and dissociate entirely to cut-off force transmission. In contrast, the individual tip-links (heterodimers) display slip-catch-slip bonds to the applied forces. While with a phenotypic mutant, we showed the importance of the slip-catch-slip bonds in uninterrupted hearing, our coarse-grained Langevin dynamics simulations demonstrated that the slip-ideal-slip bonds emerge as a collective feature from the slip-catch-slip bonds of individual tip-links.
    MeSH term(s) Mechanotransduction, Cellular ; Mechanical Phenomena ; Hearing ; Cadherins/chemistry ; Ear, Inner
    Chemical Substances Cadherins
    Language English
    Publishing date 2024-02-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45423-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Barrier-free liquid condensates of nanocatalysts as effective concentrators of catalysis

    Bedi, Silky / Kumar, Gaurav / Rose, S. M. / Rakshit, Sabyasachi / Sinha, Sharmistha

    Chemical communications. 2022 Aug. 2, v. 58, no. 62

    2022  

    Abstract: Traditional methods of molecular confinement have physicochemical barriers that restrict the free passage of substrates/products. Here, we explored liquid–liquid phase separation as a method to restrain protein–metal nanocomposites within barrier-free ... ...

    Abstract Traditional methods of molecular confinement have physicochemical barriers that restrict the free passage of substrates/products. Here, we explored liquid–liquid phase separation as a method to restrain protein–metal nanocomposites within barrier-free condensates. Confinement within liquid droplets was independent of the protein's native conformation and amplified the catalytic efficiency of metal nanocatalysts by one order of magnitude.
    Keywords catalytic activity ; liquids ; nanocatalysts ; nanocomposites ; separation
    Language English
    Dates of publication 2022-0802
    Size p. 8634-8637.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc03111f
    Database NAL-Catalogue (AGRICOLA)

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  8. Article ; Online: Barrier-free liquid condensates of nanocatalysts as effective concentrators of catalysis.

    Bedi, Silky / Kumar, Gaurav / Rose, S M / Rakshit, Sabyasachi / Sinha, Sharmistha

    Chemical communications (Cambridge, England)

    2022  Volume 58, Issue 62, Page(s) 8634–8637

    Abstract: Traditional methods of molecular confinement have physicochemical barriers that restrict the free passage of substrates/products. Here, we explored liquid-liquid phase separation as a method to restrain protein-metal nanocomposites within barrier-free ... ...

    Abstract Traditional methods of molecular confinement have physicochemical barriers that restrict the free passage of substrates/products. Here, we explored liquid-liquid phase separation as a method to restrain protein-metal nanocomposites within barrier-free condensates. Confinement within liquid droplets was independent of the protein's native conformation and amplified the catalytic efficiency of metal nanocatalysts by one order of magnitude.
    MeSH term(s) Catalysis ; Metals ; Nanocomposites
    Chemical Substances Metals
    Language English
    Publishing date 2022-08-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc03111f
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  9. Article ; Online: Transient interactions drive the lateral clustering of cadherin-23 on membrane.

    Srinivas, Cheerneni S / Singaraju, Gayathri S / Kaur, Veerpal / Das, Sayan / Ghosh, Sanat K / Sagar, Amin / Kumar, Anuj / Bhatia, Tripta / Rakshit, Sabyasachi

    Communications biology

    2023  Volume 6, Issue 1, Page(s) 293

    Abstract: Cis and trans-interactions among cadherins secure multicellularity. While the molecular structure of trans-interactions of cadherins is well understood, work to identify the molecular cues that spread the cis-interactions two-dimensionally is still ... ...

    Abstract Cis and trans-interactions among cadherins secure multicellularity. While the molecular structure of trans-interactions of cadherins is well understood, work to identify the molecular cues that spread the cis-interactions two-dimensionally is still ongoing. Here, we report that transient, weak, yet multivalent, and spatially distributed hydrophobic interactions that are involved in liquid-liquid phase separations of biomolecules in solution, alone can drive the lateral-clustering of cadherin-23 on a membrane. No specific cis-dimer interactions are required for the lateral clustering. In cells, the cis-clustering accelerates cell-cell adhesion and, thus, contributes to cell-adhesion kinetics along with strengthening the junction. Although the physiological connection of cis-clustering with rapid adhesion is yet to be explored, we speculate that the over-expression of cadherin-23 in M2-macrophages may facilitate faster attachments to circulatory tumor cells during metastasis.
    MeSH term(s) Protein Binding ; Cadherins/metabolism ; Cell Adhesion
    Chemical Substances Cadherins
    Language English
    Publishing date 2023-03-18
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-023-04677-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: The Prospects of Cadherin-23 as a Mediator of Homophilic Cell-Cell Adhesion.

    Sannigrahi, Malay Kumar / Srinivas, Sai / Rakshit, Sabyasachi

    Advances in experimental medicine and biology

    2019  Volume 1112, Page(s) 99–105

    Abstract: Cadherins (calcium-dependent adhesion proteins) constitute a family of cell surface proteins that mediate cell-cell adhesion and actively participate in tissue morphogenesis and in mediating tissue integrity. The ecto-domains of cadherins from opposing ... ...

    Abstract Cadherins (calcium-dependent adhesion proteins) constitute a family of cell surface proteins that mediate cell-cell adhesion and actively participate in tissue morphogenesis and in mediating tissue integrity. The ecto-domains of cadherins from opposing cell surfaces interact with each other to form the load-bearing trans-dimers and mechanically hold cells together. The "classical" cadherins and desmosomes that form separate groups in cadherin superfamily are mostly explored for their roles in cell-cell adhesion. However, majority of cadherins in cells belong to "nonclassical" group which is poorly explored in the context of their cell-binding properties. This review focuses on the role of "nonclassical" cadherin, cadherin-23, in cell-cell adhesion. Overall, this review highlights the need for further investigations on the role of "nonclassical" cadherin-23 in cell-cell adhesion.
    MeSH term(s) Cadherins/physiology ; Cell Adhesion ; Cell Membrane ; Desmosomes ; Humans
    Chemical Substances CDH23 protein, human ; Cadherins
    Language English
    Publishing date 2019-01-14
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2214-8019 ; 0065-2598
    ISSN (online) 2214-8019
    ISSN 0065-2598
    DOI 10.1007/978-981-13-3065-0_8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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