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  1. Article ; Online: A Proteomic Survey of the Cystic Fibrosis Transmembrane Conductance Regulator Surfaceome.

    Iazzi, Melissa / Sadeghi, Sara / Gupta, Gagan D

    International journal of molecular sciences

    2023  Volume 24, Issue 14

    Abstract: The aim of this review article is to collate recent contributions of proteomic studies to cystic fibrosis transmembrane conductance regulator (CFTR) biology. We summarize advances from these studies and create an accessible resource for future CFTR ... ...

    Abstract The aim of this review article is to collate recent contributions of proteomic studies to cystic fibrosis transmembrane conductance regulator (CFTR) biology. We summarize advances from these studies and create an accessible resource for future CFTR proteomic efforts. We focus our attention on the CFTR interaction network at the cell surface, thus generating a CFTR 'surfaceome'. We review the main findings about CFTR interactions and highlight several functional categories amongst these that could lead to the discovery of potential biomarkers and drug targets for CF.
    MeSH term(s) Humans ; Cell Membrane/physiology ; Cystic Fibrosis/genetics ; Cystic Fibrosis/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; Ion Transport ; Mutation ; Proteomics ; Signal Transduction
    Chemical Substances CFTR protein, human ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6)
    Language English
    Publishing date 2023-07-14
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241411457
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structural characterization of transcription-coupled repair protein UVSSA and its interaction with TFIIH protein.

    Mistry, Hiral / Kumari, Shweta / Aswal, Vinod K / Gupta, Gagan D

    International journal of biological macromolecules

    2023  Volume 247, Page(s) 125792

    Abstract: UV-stimulated scaffold protein A (UVSSA) is a key protein in the Transcription-Coupled Nucleotide Excision Repair (TC-NER) pathway. UVSSA, an intrinsically disordered protein, interacts with multiple members of the pathway, tethering them into the ... ...

    Abstract UV-stimulated scaffold protein A (UVSSA) is a key protein in the Transcription-Coupled Nucleotide Excision Repair (TC-NER) pathway. UVSSA, an intrinsically disordered protein, interacts with multiple members of the pathway, tethering them into the complex. Several studies have reported that UVSSA recruits Transcription Factor IIH (TFIIH) via direct interaction, following which CSB is degraded and the lesion recognition TC-NER complex dissociates from the damage site to facilitate the DNA repair. Structural insights into these events remain largely unknown. Herein, we have investigated the interaction of human UVSSA with the Pleckstrin-Homology-domain of p62 subunit of TFIIH (p62-PHD) using biophysical techniques. We observed that UVSSA forms a stable complex with the p62-PHD in vitro. Small-angle scattering measurements using X-rays and neutrons revealed a significant change in pair-distance distribution function for UVSSA
    MeSH term(s) Humans ; DNA Repair ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Protein Domains ; Protein Interaction Mapping ; Circular Dichroism ; Scattering, Small Angle ; Neutrons ; Mutation
    Chemical Substances UVSSA protein, human ; GTF2H2 protein, human ; Transcription Factors ; Carrier Proteins
    Language English
    Publishing date 2023-07-11
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.125792
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  3. Article ; Online: Synthesis and Evaluation of Ivacaftor Derivatives with Reduced Lipophilicity

    Melissa Iazzi / Phillip Junor / Jitesh Doshi / Saujanya Acharya / Roxana Sühring / Russell D. Viirre / Gagan D. Gupta

    ACS Omega, Vol 8, Iss 48, Pp 45606-

    2023  Volume 45615

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2023-11-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Proximity Mapping of Ciliary Proteins by BioID.

    Iazzi, Melissa / St-Germain, Jonathan / Acharya, Saujanya / Raught, Brian / Gupta, Gagan D

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2725, Page(s) 181–198

    Abstract: The primary cilium is a highly conserved microtubule-based organelle present in most vertebrate cell types. Mutations in ciliary protein genes can lead to dysfunctional or absent cilia and are the cause of a large group of heterogeneous diseases known as ...

    Abstract The primary cilium is a highly conserved microtubule-based organelle present in most vertebrate cell types. Mutations in ciliary protein genes can lead to dysfunctional or absent cilia and are the cause of a large group of heterogeneous diseases known as ciliopathies. ARL13B is a member of the ARF family of regulatory GTPases and is highly enriched on the ciliary membrane. The absence of ARL13B disrupts cilia architecture and mutations have been linked to several diseases; yet there remain major gaps in our understanding of the role that ARL13B plays in primary cilia function. Here, we demonstrate how in cellulo proximity-dependent biotinylation (BioID) can be used to generate a comprehensive protein proximity map of ciliary proteins by performing BioID on N- and C-terminally BirA*-tagged ARL13B. This method can theoretically provide insight into any cilia protein, identifying key interactors that play a critical role in ciliary biology.
    MeSH term(s) Biotinylation ; Proteins/metabolism ; GTP Phosphohydrolases/metabolism ; Microtubules/metabolism ; Mutation ; Cilia/metabolism
    Chemical Substances Proteins ; GTP Phosphohydrolases (EC 3.6.1.-)
    Language English
    Publishing date 2023-10-19
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3507-0_11
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  5. Article: Crystal structure of

    Patel, Stuti N / Sonani, Ravi R / Chaubey, Mukesh G / Gupta, Gagan D / Singh, Niraj Kumar / Kumar, Vinay / Madamwar, Datta

    3 Biotech

    2023  Volume 13, Issue 7, Page(s) 247

    Abstract: Phycobiliproteins is a family of chromophore-containing proteins having light-harvesting and antioxidant capacity. The phycocyanin (PC) is a brilliant blue coloured phycobiliprotein, found in rod structure of phycobilisome and has been widely studied for ...

    Abstract Phycobiliproteins is a family of chromophore-containing proteins having light-harvesting and antioxidant capacity. The phycocyanin (PC) is a brilliant blue coloured phycobiliprotein, found in rod structure of phycobilisome and has been widely studied for their therapeutic and fluorescent properties. In the present study, the hexameric assembly structure of phycocyanin (Syn-PC) from
    Supplementary information: The online version contains supplementary material available at 10.1007/s13205-023-03665-1.
    Language English
    Publishing date 2023-06-24
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2600522-0
    ISSN 2190-5738 ; 2190-572X
    ISSN (online) 2190-5738
    ISSN 2190-572X
    DOI 10.1007/s13205-023-03665-1
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  6. Article ; Online: Crystal structure analysis of phycoerythrin from marine cyanobacterium

    Patel, Stuti N / Sonani, Ravi R / Gupta, Gagan D / Singh, Niraj Kumar / Kumar, Vinay / Madamwar, Datta

    Journal of biomolecular structure & dynamics

    2022  Volume 41, Issue 9, Page(s) 3752–3761

    Abstract: Phycoerythrin (PE) is green light-absorbing pigment-protein that assists in efficient light harvesting in cyanobacteria and red-algae. PE in cyanobacteria stays less studied so far as compared to that in red algae. In this study, PE from marine ... ...

    Abstract Phycoerythrin (PE) is green light-absorbing pigment-protein that assists in efficient light harvesting in cyanobacteria and red-algae. PE in cyanobacteria stays less studied so far as compared to that in red algae. In this study, PE from marine cyanobacteria
    MeSH term(s) Phycoerythrin/chemistry ; Phycoerythrin/metabolism ; Cyanobacteria/chemistry ; Cyanobacteria/metabolism ; Crystallography, X-Ray ; Peptides/metabolism
    Chemical Substances Phycoerythrin (11016-17-4) ; Peptides
    Language English
    Publishing date 2022-03-31
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2022.2055647
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  7. Article ; Online: Structural characterization of transcription-coupled repair protein UVSSA and its interaction with TFIIH protein

    Mistry, Hiral / Kumari, Shweta / Aswal, Vinod K. / Gupta, Gagan D.

    International Journal of Biological Macromolecules. 2023 July 11, p.125792-

    2023  , Page(s) 125792–

    Abstract: UV-stimulated scaffold protein A (UVSSA) is a key protein in the Transcription-Coupled Nucleotide Excision Repair (TC-NER) pathway. UVSSA, an intrinsically disordered protein, interacts with multiple members of the pathway, tethering them into the ... ...

    Abstract UV-stimulated scaffold protein A (UVSSA) is a key protein in the Transcription-Coupled Nucleotide Excision Repair (TC-NER) pathway. UVSSA, an intrinsically disordered protein, interacts with multiple members of the pathway, tethering them into the complex. Several studies have reported that UVSSA recruits Transcription Factor IIH (TFIIH) via direct interaction, following which CSB is degraded and the lesion recognition TC-NER complex dissociates from the damage site to facilitate the DNA repair. Structural insights into these events remain largely unknown. Herein, we have investigated the interaction of human UVSSA with the Pleckstrin-Homology-domain of p62 subunit of TFIIH (p62-PHD) using biophysical techniques. We observed that UVSSA forms a stable complex with the p62-PHD in vitro. Small-angle scattering measurements using X-rays and neutrons revealed a significant change in pair-distance distribution function for UVSSA₆₆₂/p62-PHD complex compared to UVSSA alone. Additionally, a significant decrease was observed in the radius of gyration of the complex. Our findings suggest that TFIIH binding to UVSSA causes significant conformational changes in UVSSA. We hypothesize that these conformational changes play an important role in the dissociation of the lesion recognition TC-NER complex.
    Keywords DNA repair ; dissociation ; humans ; scaffolding proteins ; transcription factors ; UVSSA ; Transcription-coupled repair ; Transcription-factor IIH ; Intrinsically disordered protein ; Small-angle scattering ; UV-sensitive syndrome
    Language English
    Dates of publication 2023-0711
    Publishing place Elsevier B.V.
    Document type Article ; Online
    Note Pre-press version
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.125792
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  8. Article ; Online: Synthesis and Evaluation of Ivacaftor Derivatives with Reduced Lipophilicity.

    Iazzi, Melissa / Junor, Phillip / Doshi, Jitesh / Acharya, Saujanya / Sühring, Roxana / Viirre, Russell D / Gupta, Gagan D

    ACS omega

    2023  Volume 8, Issue 48, Page(s) 45606–45615

    Abstract: Mutations in the unique ATP-binding cassette anion channel, the cystic fibrosis conductance regulator (CFTR), lead to the inherited fatal disease known as cystic fibrosis (CF). Ivacaftor enhances channel gating of CFTR by stabilizing its open state and ... ...

    Abstract Mutations in the unique ATP-binding cassette anion channel, the cystic fibrosis conductance regulator (CFTR), lead to the inherited fatal disease known as cystic fibrosis (CF). Ivacaftor enhances channel gating of CFTR by stabilizing its open state and has been approved as monotherapy for CF patients with CFTR gating mutations (e.g., G551D) and as part of combination therapy with lumacaftor for CFTR folding mutations (e.g., ΔF508). However, in the latter context, ivacaftor may destabilize folding-rescued ΔF508-CFTR and membrane-associated proteins and attenuate lumacaftor pharmacotherapy. Here, we tested the hypothesis that the high lipophilicity of ivacaftor may contribute to this effect. We describe the synthesis of three glutamic acid ivacaftor derivatives with reduced lipophilicity that bear different charges at neutral pH (compounds
    Language English
    Publishing date 2023-11-25
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.3c05839
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Characterization of phi112, a Molecular Marker Tightly Linked to the

    Singh, Alla / Karjagi, Chikkappa / Kaur, Sehgeet / Jeet, Gagan / Bhamare, Deepak / Gupta, Sonu / Kumar, Sunil / Das, Abhijit / Gupta, Mamta / Chaudhary, D P / Bhushan, Bharat / Jat, B S / Kumar, Ramesh / Dagla, M C / Kumar, Manoj

    Genes

    2023  Volume 14, Issue 2

    Abstract: Quality Protein Maize (QPM) contains higher amounts of essential amino acids lysine and tryptophan. The QPM phenotype is based on regulating zein protein synthesis ... ...

    Abstract Quality Protein Maize (QPM) contains higher amounts of essential amino acids lysine and tryptophan. The QPM phenotype is based on regulating zein protein synthesis by
    MeSH term(s) Zea mays/genetics ; Plant Proteins/genetics ; Multiplex Polymerase Chain Reaction ; Transcription Factors/genetics ; Lysine/metabolism ; Biomarkers/metabolism
    Chemical Substances Plant Proteins ; Transcription Factors ; Lysine (K3Z4F929H6) ; Biomarkers
    Language English
    Publishing date 2023-02-20
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2527218-4
    ISSN 2073-4425 ; 2073-4425
    ISSN (online) 2073-4425
    ISSN 2073-4425
    DOI 10.3390/genes14020531
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  10. Article ; Online: Centrosome Biology: Polymer-Based Centrosome Maturation.

    Gupta, Gagan D / Pelletier, Laurence

    Current biology : CB

    2017  Volume 27, Issue 17, Page(s) R836–R839

    Abstract: The molecular mechanisms that control how the centrosome increases in size and microtubule nucleation capacity during mitosis have remained elusive. Recent work using in vitro assays provide exciting clues as to how this may occur. ...

    Abstract The molecular mechanisms that control how the centrosome increases in size and microtubule nucleation capacity during mitosis have remained elusive. Recent work using in vitro assays provide exciting clues as to how this may occur.
    MeSH term(s) Animals ; Centrosome ; Diptera ; Mitosis ; Polymers
    Chemical Substances Polymers
    Language English
    Publishing date 2017-09-12
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2017.07.036
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