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  • Ebooks (Sách điện tử)

  • Membrane Proteins: Structure, Function and Motion

    • Authors : - (2023)

  • Cuốn sách này là tập hợp các bài đánh giá và bài nghiên cứu gốc về sinh hóa vật lý của protein màng. Các khía cạnh khác nhau của cấu trúc phức tạp và động và hành vi chức năng của protein màng trong màng tế bào và tương tác của chúng với lipid, protein và các phân tử và ion khác đã được một số nhà khoa học hàng đầu trong lĩnh vực này nghiên cứu. Cuốn sách này hữu ích cho sinh...
  • Journal Article

  • Conformation and structural dynamics of the Xist lncRNA A-repeats

    • Authors : Jones, Alisha N. (2023)

  • Long noncoding RNAs (lncRNAs) are non‐protein‐encoding transcripts with lengths of 500 or more nucleotides (nt), with some spanning up to several thousands of nucleotides 1. LncRNAs have emerged as important regulators of gene expression and cellular functions, as transcriptional regulators at the level of chromatin, as scaffolding platforms, and as guides for RNP localization 2–9. Recent advancements in chemical probing experiments and their couplin...
  • Journal Article

  • Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain

    • Authors : Jojoa-Cruz, Sebastian (2023)

  • Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we use...
  • Journal Article

  • Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo

    • Authors : Mendoza, Johnny (2023)

  • Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine and folate one-carbon metabolism. MS is a large multi-domain protein capable of binding and activating three substrates: homocysteine, folate, S-adenosylmethionine for methylation. Achieving three chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access to the cobalamin cofactor at the right time. The distinct conformations required for each r...
  • Ebooks (Sách điện tử)

  • Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases

    • Authors : Yadav, Lumbini R. (2023)

  • Class I ribonucleotide reductases consisting of R1 and R2 subunits convert ribonucleoside diphosphates to deoxyribonucleoside diphosphates involving an intricate free radical mechanism. The generation of free radicals in the Class Ib ribonucleotide reductases is mediated by reaction involving di-manganese ions in the R2 subunits and is externally assisted by flavodoxin-like NrdI subunit. This is unlike Class Ia ribonucleotide reductases, where the free radical generation&#x...
  • Journal Article

  • MicroED structure of the human vasopressin 1B receptor

    • Authors : Shiriaeva, Anna (2023)

  • Mucin 1 (MUC1) is a transmembrane mucin expressed at the apical surface of epithelial cells at different mucosal surfaces including breast and intestine. In the gastrointestinal tract, MUC1 has a barrier function against bacterial invasion, but can also serve as an entry receptor for pathogenic Salmonella bacteria. Moreover, MUC1 is well known for its aberrant expression and glycosylation in adenocarcinomas The MUC1 extracellular do...
  • Journal article

  • Structural analysis of SALL4 zinc-finger domain reveals a link between AT-rich DNA binding and Okihiro syndrome

    • Authors : Watson, James A. (2023)

  • Spalt-like 4 (SALL4) maintains vertebrate embryonic stem cell identity and is required for the development of multiple organs, including limbs. Mutations in SALL4 are associated with Okihiro syndrome and SALL4 is also a known target of thalidomide. SALL4 protein has a distinct preference for AT-rich sequences, recognised by a pair of zinc fingers at the C-terminus. However, unlike many characterised zinc finger proteins, SALL4 shows flexibl...