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  1. Article ; Online: Interaction and simulation studies suggest the possible molecular targets of intrinsically disordered amyloidogenic antimicrobial peptides in

    Sarkar, Sayani / Kumari, Aruna / Tiwari, Monalisa / Tiwari, Vishvanath

    Journal of biomolecular structure & dynamics

    2023  Volume 42, Issue 6, Page(s) 2747–2764

    Abstract: Acinetobacter ... ...

    Abstract Acinetobacter baumannii
    MeSH term(s) Antimicrobial Peptides ; Acinetobacter baumannii ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Microbial Sensitivity Tests
    Chemical Substances Antimicrobial Peptides ; Anti-Bacterial Agents
    Language English
    Publishing date 2023-05-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2023.2208219
    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:
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  2. Article ; Online: Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases.

    Sarkar, Sayani / Behera, Adaitya Prasad / Borar, Prateeka / Banka, Prerana Agarwal / Datta, Ajit B

    The Biochemical journal

    2019  Volume 476, Issue 10, Page(s) 1465–1482

    Abstract: Ubiquitin RING E3 ligases (E3s) catalyze ubiquitin (Ub) transfer to their substrates by engaging E2∼Ub intermediates with the help of their RING domains. Different E3s have been found to contain a conserved tryptophan residue in their RING that plays an ... ...

    Abstract Ubiquitin RING E3 ligases (E3s) catalyze ubiquitin (Ub) transfer to their substrates by engaging E2∼Ub intermediates with the help of their RING domains. Different E3s have been found to contain a conserved tryptophan residue in their RING that plays an essential role in E2 binding and, hence, enzymatic activity. Many active E3s, however, lack this specific residue. We mined through the existing data to observe that the conservation of the tryptophan and quaternary organization of the RING domains are remarkably correlated. Monomeric RINGs possess the tryptophan while all well-characterized dimeric RINGs, except RNF8, contain other amino acid residues. Biochemical analyses on representative E3s and their mutants reveal that the tryptophan is essential for optimal enzymatic activity of monomeric RINGs whereas dimeric E3s with tryptophan display hyperactivity. Most critically, the introduction of the tryptophan restores the activity of inactive monomeric RNF4 mutants, an obligatory dimeric E3. Binding studies indicate that monomeric RINGs retained the tryptophan for their optimal functionality to compensate for weak Ub binding. On the other hand, tryptophan was omitted from dimeric RINGs during the course of evolution to prevent unwanted modifications and allow regulation of their activity through oligomerization.
    MeSH term(s) Humans ; Mutation ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Multimerization ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Tryptophan/chemistry ; Tryptophan/genetics ; Tryptophan/metabolism ; Ubiquitin/chemistry ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Nuclear Proteins ; RNF4 protein, human ; Transcription Factors ; Ubiquitin ; Tryptophan (8DUH1N11BX) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2019-05-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20180883
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Correction: Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases.

    Sarkar, Sayani / Behera, Adaitya Prasad / Borar, Prateeka / Banka, Prerana Agarwal / Datta, Ajit B

    The Biochemical journal

    2019  Volume 476, Issue 17, Page(s) 2517–2518

    Language English
    Publishing date 2019-09-13
    Publishing country England
    Document type Journal Article ; Published Erratum
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20180883_COR
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Sustained release gastroretentive tablet of metformin hydrochloride based on poly (acrylic acid)-grafted-gellan.

    Sarkar, Debjani / Nandi, Gouranga / Changder, Abhijit / Hudati, Prasenjit / Sarkar, Sayani / Ghosh, Lakshmi Kanta

    International journal of biological macromolecules

    2017  Volume 96, Page(s) 137–148

    Abstract: Development of a gastroretentive sustained release tablet of metformin based on poly (acrylic acid)-grafted-gellan (PAAc-g-GG) is the main purpose of this study. At first, PAAc-g-GG was synthesized by microwave-promoted free radical initiation method ... ...

    Abstract Development of a gastroretentive sustained release tablet of metformin based on poly (acrylic acid)-grafted-gellan (PAAc-g-GG) is the main purpose of this study. At first, PAAc-g-GG was synthesized by microwave-promoted free radical initiation method using cerric (IV) ammonium nitrate (CAN) as redox initiator and characterized by elemental analysis, FTIR, DSC-TGA,
    MeSH term(s) Acrylic Resins/chemistry ; Adhesiveness ; Animals ; Delayed-Action Preparations ; Drug Carriers/chemistry ; Drug Liberation ; Female ; Gastric Mucosa/chemistry ; Metformin/chemistry ; Metformin/metabolism ; Mice ; Microwaves ; Polysaccharides, Bacterial/chemistry ; Stomach/metabolism ; Tablets ; Viscosity
    Chemical Substances Acrylic Resins ; Delayed-Action Preparations ; Drug Carriers ; Polysaccharides, Bacterial ; Tablets ; carbopol 940 (4Q93RCW27E) ; gellan gum (7593U09I4D) ; Metformin (9100L32L2N)
    Language English
    Publishing date 2017-03
    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.2016.12.022
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 2374: Show issues Location:
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  5. Article ; Online: RING E3-Catalyzed E2 Self-Ubiquitination Attenuates the Activity of Ube2E Ubiquitin-Conjugating Enzymes.

    Banka, Prerana Agarwal / Behera, Adaitya Prasad / Sarkar, Sayani / Datta, Ajit B

    Journal of molecular biology

    2015  Volume 427, Issue 13, Page(s) 2290–2304

    Abstract: Ubiquitination of a target protein is accomplished through sequential actions of the E1, E2s, and the E3s. E2s dictate the modification topology while E3 ligases confer substrate specificity and recruit the cognate E2. Human genome codes for ~35 ... ...

    Abstract Ubiquitination of a target protein is accomplished through sequential actions of the E1, E2s, and the E3s. E2s dictate the modification topology while E3 ligases confer substrate specificity and recruit the cognate E2. Human genome codes for ~35 different E2 proteins; all of which contain the characteristic ubiquitin-conjugating UBC core domain sufficient for catalysis. Many of these E2 enzymes also have N- or C-terminal extensions; roles of which are not very well understood. We show that the N-terminal extension of Ube2E1 undergoes intramolecular auto-ubiquitination. This self-ubiquitination activity is enhanced in the presence of interacting RING E3 ligases and results in a progressive attenuation of the E2 activity toward substrate/E3 modification. We also find that the N-terminal ubiquitination sites are conserved in all the three Ube2Es and replacing them with arginine renders all three full-length Ube2Es equally active as their core UBC domains. Based on these results, we propose that E3-catalyzed self-ubiquitination acts as a key regulatory mechanism that controls the activity of Ube2E class of ubiquitin E2s.
    MeSH term(s) Amino Acid Sequence ; Amino Acid Substitution ; Catalysis ; Conserved Sequence ; Humans ; Lysine/genetics ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Ubiquitin-Conjugating Enzymes/chemistry ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitination
    Chemical Substances Nuclear Proteins ; RNF4 protein, human ; Transcription Factors ; UBE2D2 protein, human (EC 2.3.2.23) ; UBE2E1 protein, human (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2015-07-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2015.04.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 867: Show issues Location:
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