Search Results - "Fierer, Jacob"

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  1. 1

    SpyLigase peptide–peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture by Fierer, Jacob O, Veggiani, Gianluca, Howarth, Mark

    “…Individual proteins can now often be modified with atomic precision, but there are still major obstacles to connecting proteins into larger assemblies. To…”
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    Journal Article
  2. 2

    Structural Analysis and Optimization of the Covalent Association between SpyCatcher and a Peptide Tag by Li, Long, Fierer, Jacob O., Rapoport, Tom A., Howarth, Mark

    Published in Journal of molecular biology (23-01-2014)
    “…Peptide tagging is a key strategy for observing and isolating proteins. However, the interactions of proteins with peptides are nearly all rapidly reversible…”
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  3. 3

    Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin by Zakeri, Bijan, Fierer, Jacob O, Celik, Emrah, Chittock, Emily C, Schwarz-Linek, Ulrich, Moy, Vincent T, Howarth, Mark

    “…Protein interactions with peptides generally have low thermodynamic and mechanical stability. Streptococcus pyogenes fibronectin-binding protein FbaB contains…”
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    Journal Article
  4. 4

    SpyTag/SpyCatcher Cyclization Confers Resilience to Boiling on a Mesophilic Enzyme by Schoene, Christopher, Fierer, Jacob O., Bennett, S. Paul, Howarth, Mark

    Published in Angewandte Chemie International Edition (10-06-2014)
    “…SpyTag is a peptide that spontaneously forms an amide bond with its protein partner SpyCatcher. SpyTag was fused at the N terminus of β‐lactamase and…”
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    Journal Article
  5. 5

    SpyTag/SpyCatcher Cyclization Confers Resilience to Boiling on a Mesophilic Enzyme by Schoene, Christopher, Fierer, Jacob O., Bennett, S. Paul, Howarth, Mark

    Published in Angewandte Chemie (10-06-2014)
    “…SpyTag is a peptide that spontaneously forms an amide bond with its protein partner SpyCatcher. SpyTag was fused at the N terminus of β‐lactamase and…”
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    Journal Article
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  7. 7

    Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences by Shanmugam, Raghuvaran, Fierer, Jacob, Kaiser, Steffen, Helm, Mark, Jurkowski, Tomasz P, Jeltsch, Albert

    Published in Cell discovery (09-06-2015)
    “…The Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp, but the molecular role of this methylation is unknown…”
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    Journal Article
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