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Journal Abstract Search


170 related items for PubMed ID: 30864660

  • 21. Surface-exposed loops and an acidic patch in the Scl1 protein of group A Streptococcus enable Scl1 binding to wound-associated fibronectin.
    McNitt DH, Choi SJ, Keene DR, Van De Water L, Squeglia F, Berisio R, Lukomski S.
    J Biol Chem; 2018 May 18; 293(20):7796-7810. PubMed ID: 29615492
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  • 22. Crystal structure of the YajQ-family protein XC_3703 from Xanthomonas campestris pv. campestris.
    Zhao Z, Wu Z, Zhang J.
    Acta Crystallogr F Struct Biol Commun; 2016 Sep 18; 72(Pt 9):720-5. PubMed ID: 27599864
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  • 28. Capturing the Mechanism Underlying TOP mRNA Binding to LARP1.
    Cassidy KC, Lahr RM, Kaminsky JC, Mack S, Fonseca BD, Das SR, Berman AJ, Durrant JD.
    Structure; 2019 Dec 03; 27(12):1771-1781.e5. PubMed ID: 31676287
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  • 29. Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands.
    Linossi EM, Li K, Veggiani G, Tan C, Dehkhoda F, Hockings C, Calleja DJ, Keating N, Feltham R, Brooks AJ, Li SS, Sidhu SS, Babon JJ, Kershaw NJ, Nicholson SE.
    Nat Commun; 2021 Dec 02; 12(1):7032. PubMed ID: 34857742
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  • 31. Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment.
    Xiong S, Lorenzen K, Couzens AL, Templeton CM, Rajendran D, Mao DYL, Juang YC, Chiovitti D, Kurinov I, Guettler S, Gingras AC, Sicheri F.
    Structure; 2018 Aug 07; 26(8):1101-1115.e6. PubMed ID: 29983373
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  • 35. Synergy and allostery in ligand binding by HIV-1 Nef.
    Aldehaiman A, Momin AA, Restouin A, Wang L, Shi X, Aljedani S, Opi S, Lugari A, Shahul Hameed UF, Ponchon L, Morelli X, Huang M, Dumas C, Collette Y, Arold ST.
    Biochem J; 2021 Apr 30; 478(8):1525-1545. PubMed ID: 33787846
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  • 37. Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.
    Teramoto T, Kaitany KJ, Kakuta Y, Kimura M, Fierke CA, Hall TMT.
    Nucleic Acids Res; 2020 Dec 02; 48(21):11815-11826. PubMed ID: 32719843
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