B
Bijan Zakeri
Researcher at Massachusetts Institute of Technology
Publications - 22
Citations - 1994
Bijan Zakeri is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Isopeptide bond & Synthetic biology. The author has an hindex of 11, co-authored 19 publications receiving 1548 citations. Previous affiliations of Bijan Zakeri include Merck Serono & University of Oxford.
Papers
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Journal ArticleDOI
Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin
Bijan Zakeri,Jacob O. Fierer,Emrah Celik,Emily Chittock,Ulrich Schwarz-Linek,Vincent T. Moy,Mark Howarth +6 more
TL;DR: The robust reaction conditions and irreversible linkage of SpyTag shed light on spontaneous isopeptide bond formation and should provide a targetable lock in cells and a stable module for new protein architectures.
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Synthesis and patterning of tunable multiscale materials with engineered cells
Allen Y. Chen,Zhengtao Deng,Amanda N. Billings,Urartu Ozgur Safak Seker,Michelle Y. Lu,Robert J. Citorik,Bijan Zakeri,Timothy K. Lu +7 more
TL;DR: In this paper, inducible genetic circuits and cellular communication circuits are used to regulate Escherichia coli curli amyloid production, and E. coli cells can organize self-assembling amylid fibrils across multiple length scales.
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Spontaneous intermolecular amide bond formation between side chains for irreversible peptide targeting.
Bijan Zakeri,Mark Howarth +1 more
TL;DR: A 16 amino acid peptide is designed that spontaneously forms an amide bond to a protein partner, via reaction between lysine and asparagine side chains, which depended upon splitting a pilin subunit from a human pathogen.
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Chemical biology of tetracycline antibioticsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Systems and Chemical Biology, and has undergone the Journal's usual peer review process.
Bijan Zakeri,Gerard D. Wright +1 more
TL;DR: Recent findings that have clarified the mode of action and the biosynthetic pathway of tetracyclines and that have shed light on the chemical biology of t Petracycline antibiotics are discussed.
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Superglue from bacteria: unbreakable bridges for protein nanotechnology
TL;DR: In this paper, the authors suggest that an ideal interaction between proteins would be covalent, specific, require addition of only a peptide tag to the protein of interest, and form under a wide range of conditions.