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「タンパク質進化の隠れた主役「融合」の再発見」の検索結果

131 件中 10 件を表示 (2896 ms) · ⭐ 保存した論文

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("protein evolution"[MeSH] OR "protein evolution") AND ("gene fusion"[MeSH] OR "protein fusion" OR "domain fusion" OR fusion)

💡 タンパク質進化における遺伝子融合・ドメイン融合の役割に焦点を当てたクエリ

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  • Cooperative hydrophobic core interactions in the β-trefoil architecture.

    Michael Blaber · Protein science : a publication of the Protein Society · 2021

    Symmetric protein architectures have a compelling aesthetic that suggests a plausible evolutionary process (i.e., gene duplication/fusion) yielding complex architecture from a simpler structural motif. Furthermore, symmetry inspires a practical approach to computational protein design that substantially reduces the combinatorial explosion problem, and may provide practical solutions for structure …

    📄 PubMed で読む (PMID: 33686691)
  • Detection and quantification of C-terminally tagged proteins by in-gel fluorescence.

    Adrian C D Fuchs · Scientific reports · 2024

    The analysis of recombinant proteins in complex solutions is often accomplished with tag-specific antibodies in western blots. Recently, I introduced an antibody-free alternative wherein tagged proteins are visualized directly within polyacrylamide gels. For this, I used the protein ligase Connectase to selectively attach fluorophores to target proteins possessing an N-terminal recognition sequenc…

    📄 PubMed で読む (PMID: 38977739)
  • Inducing conformational preference of the membrane protein transporter EmrE through conservative mutations.

    Maureen Leninger, Ampon Sae Her, Nathaniel J Traaseth 他 · eLife · 2019

    Transporters from bacteria to humans contain inverted repeat domains thought to arise evolutionarily from the fusion of smaller membrane protein genes. Association between these domains forms the functional unit that enables transporters to adopt distinct conformations necessary for function. The small multidrug resistance (SMR) family provides an ideal system to explore the role of mutations in a…

    📄 PubMed で読む (PMID: 31637997)
  • [Gene duplication and protein evolution. Case of aminoacyl-t-RNA synthetases].

    Y Boulanger · Comptes rendus des seances de la Societe de biologie et de ses filiales · 1977

    Aminoacyl-tRNA synthetases are a functionally homologous group of enzymes which catalyse the first step of protein synthesis. The accumulation of data on the oligomeric structures of these enzymes has revealed a wide diversity in the sizes and organization of the protomers. This is not consistent with the idea of a family with homologous primary and tertiary structures. Howewer recent studies have…

    📄 PubMed で読む (PMID: 142542)
  • A covalent chemical genotype-phenotype linkage for in vitro protein evolution.

    Viktor Stein, India Sielaff, Kai Johnsson 他 · Chembiochem : a European journal of chemical biology · 2007

    📄 PubMed で読む (PMID: 17948318)
  • HIV-1 proviral DNA excision using an evolved recombinase.

    Indrani Sarkar, Ilona Hauber, Joachim Hauber 他 · Science (New York, N.Y.) · 2007

    HIV-1 integrates into the host chromosome and persists as a provirus flanked by long terminal repeats (LTRs). To date, treatment regimens primarily target the virus enzymes or virus-cell fusion, but not the integrated provirus. We report here the substrate-linked protein evolution of a tailored recombinase that recognizes an asymmetric sequence within an HIV-1 LTR. This evolved recombinase efficie…

    📄 PubMed で読む (PMID: 17600219)
  • Emulating membrane protein evolution by rational design.

    Mikaela Rapp, Susanna Seppälä, Erik Granseth 他 · Science (New York, N.Y.) · 2007

    How do integral membrane proteins evolve in size and complexity? Using the small multidrug-resistance protein EmrE from Escherichia coli as a model, we experimentally demonstrated that the evolution of membrane proteins composed of two homologous but oppositely oriented domains can occur in a small number of steps: An original dual-topology protein evolves, through a gene-duplication event, to a h…

    📄 PubMed で読む (PMID: 17255477)
  • Gram-negative outer-membrane proteins with multiple β-barrel domains.

    Ron Solan, Joana Pereira, Andrei N Lupas 他 · Proceedings of the National Academy of Sciences of the United States of America · 2021

    Outer-membrane beta barrels (OMBBs) are found in the outer membrane of gram-negative bacteria and eukaryotic organelles. OMBBs fold as antiparallel β-sheets that close onto themselves, forming pores that traverse the membrane. Currently known structures include only one barrel, of 8 to 36 strands, per chain. The lack of multi-OMBB chains is surprising, as most OMBBs form oligomers, and some functi…

    📄 PubMed で読む (PMID: 34330833)
  • Protein evolution by "codon shuffling": a novel method for generating highly variant mutant libraries by assembly of hexamer DNA duplexes.

    Sidharth Chopra, Anand Ranganathan · Chemistry & biology · 2003

    📄 PubMed で読む (PMID: 14583258)
  • An Efficient Ligation Method in the Making of an in vitro Virus for in vitro Protein Evolution.

    Ichiro Tabuchi, Sayaka Soramoto, Miho Suzuki 他 · Biological procedures online · 2002

    The "in vitro virus" is a molecular construct to perform evolutionary protein engineering. The "virion (=viral particle)" (mRNA-peptide fusion), is made by bonding a nascent protein with its coding mRNA via puromycin in a test tube for in vitro translation. In this work, the puromycin-linker was attached to mRNA using the Y-ligation, which was a method of two single-strands ligation at the end of …

    📄 PubMed で読む (PMID: 12734569)