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Journal Abstract Search

365 related items for PubMed ID: 28805060

  • 1. Substrate-Induced Facilitated Dissociation of the Competitive Inhibitor from the Active Site of O-Acetyl Serine Sulfhydrylase Reveals a Competitive-Allostery Mechanism.
    Singh AK, Ekka MK, Kaushik A, Pandya V, Singh RP, Banerjee S, Mittal M, Singh V, Kumaran S.
    Biochemistry; 2017 Sep 19; 56(37):5011-5025. PubMed ID: 28805060
    [Abstract] [Full Text] [Related]

  • 2. Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus.
    Dharavath S, Raj I, Gourinath S.
    Biochem J; 2017 Mar 23; 474(7):1221-1239. PubMed ID: 28126739
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  • 3. Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
    Benoni R, Pertinhez TA, Spyrakis F, Davalli S, Pellegrino S, Paredi G, Pezzotti A, Bettati S, Campanini B, Mozzarelli A.
    FEBS Lett; 2016 Apr 23; 590(7):943-53. PubMed ID: 27072053
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  • 4. Two Distinct Assembly States of the Cysteine Regulatory Complex of Salmonella typhimurium Are Regulated by Enzyme-Substrate Cognate Pairs.
    Kaushik A, Ekka MK, Kumaran S.
    Biochemistry; 2017 May 09; 56(18):2385-2399. PubMed ID: 28414426
    [Abstract] [Full Text] [Related]

  • 5. Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase.
    Spyrakis F, Felici P, Bayden AS, Salsi E, Miggiano R, Kellogg GE, Cozzini P, Cook PF, Mozzarelli A, Campanini B.
    Biochim Biophys Acta; 2013 Jan 09; 1834(1):169-81. PubMed ID: 23000429
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  • 6. A two-step process controls the formation of the bienzyme cysteine synthase complex.
    Salsi E, Campanini B, Bettati S, Raboni S, Roderick SL, Cook PF, Mozzarelli A.
    J Biol Chem; 2010 Apr 23; 285(17):12813-22. PubMed ID: 20164178
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  • 7. Molecular mechanism of selective substrate engagement and inhibitor disengagement of cysteine synthase.
    Kaushik A, Rahisuddin R, Saini N, Singh RP, Kaur R, Koul S, Kumaran S.
    J Biol Chem; 2021 Apr 23; 296():100041. PubMed ID: 33162395
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  • 10. Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature.
    Salsi E, Bayden AS, Spyrakis F, Amadasi A, Campanini B, Bettati S, Dodatko T, Cozzini P, Kellogg GE, Cook PF, Roderick SL, Mozzarelli A.
    J Med Chem; 2010 Jan 14; 53(1):345-56. PubMed ID: 19928859
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  • 11. Serine acetyltransferase from Neisseria gonorrhoeae; structural and biochemical basis of inhibition.
    Oldham KEA, Prentice EJ, Summers EL, Hicks JL.
    Biochem J; 2022 Jan 14; 479(1):57-74. PubMed ID: 34890451
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  • 12. Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex.
    Francois JA, Kumaran S, Jez JM.
    Plant Cell; 2006 Dec 14; 18(12):3647-55. PubMed ID: 17194764
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  • 13. Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase.
    Chinthalapudi K, Kumar M, Kumar S, Jain S, Alam N, Gourinath S.
    Proteins; 2008 Sep 14; 72(4):1222-32. PubMed ID: 18350570
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  • 14. Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.
    Banerjee S, Ekka MK, Kumaran S.
    BMC Biochem; 2011 Jun 02; 12():31. PubMed ID: 21631959
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  • 15. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.
    Huang B, Vetting MW, Roderick SL.
    J Bacteriol; 2005 May 02; 187(9):3201-5. PubMed ID: 15838047
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  • 16. Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate.
    Tai CH, Yoon MY, Kim SK, Rege VD, Nalabolu SR, Kredich NM, Schnackerz KD, Cook PF.
    Biochemistry; 1998 Jul 28; 37(30):10597-604. PubMed ID: 9692949
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