Search Results - "Streaker, Emily D."

A folate receptor beta-specific human monoclonal antibody recognizes activated macrophage of rheumatoid patients and mediates antibody-dependent cell-mediated cytotoxicity by Feng, Yang, Shen, Jiayin, Streaker, Emily D, Lockwood, Michael, Zhu, Zhongyu, Low, Philip S, Dimitrov, Dimiter S

“…Folate receptor beta (FRβ) is only detectable in placenta and limited to some hematopoietic cells of myeloid lineage in healthy people. Studies have indicated…”
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Characterization of germline antibody libraries from human umbilical cord blood and selection of monoclonal antibodies to viral envelope glycoproteins: Implications for mechanisms of immune evasion and design of vaccine immunogens by Chen, Weizao, Streaker, Emily D., Russ, Daniel E., Feng, Yang, Prabakaran, Ponraj, Dimitrov, Dimiter S.

“…► We characterized human cord blood IgM antibody libraries by large-scale sequencing. ► Phage Fab library from human cord blood did not yield any binders for…”
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Characterization of human IgG repertoires in an acute HIV-1 infection by Chen, Weizao, Prabakaran, Ponraj, Zhu, Zhongyu, Feng, Yang, Streaker, Emily D., Dimitrov, Dimiter S.

“…All known broadly neutralizing antibodies (bnAbs) are highly somatically mutated and therefore significantly differ from their germline predecessors. Thus…”
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Coupling of Protein Assembly and DNA Binding: Biotin Repressor Dimerization Precedes Biotin Operator Binding by Streaker, Emily D., Beckett, Dorothy

“…The kinetics of coupling of protein dimerization and DNA binding have been investigated in the biotin repressor system. Two repressor monomers bind to the 40…”
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Nonenzymatic biotinylation of a biotin carboxyl carrier protein: Unusual reactivity of the physiological target lysine by Streaker, Emily D., Beckett, Dorothy

“…Enzyme‐catalyzed addition of biotin to proteins is highly specific. In any single organism one or a small number of proteins are biotinylated and only a single…”
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The Biotin Regulatory System:  Kinetic Control of a Transcriptional Switch by Streaker, Emily D, Beckett, Dorothy

“…An organism's response to environmental and metabolic cues requires communication between transcription regulatory processes and “other” cellular events. In a…”
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Allosteric Signaling in the Biotin Repressor Occurs via Local Folding Coupled to Global Dampening of Protein Dynamics by Laine, Olli, Streaker, Emily D., Nabavi, Maryam, Fenselau, Catherine C., Beckett, Dorothy

“…The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5′-AMP activates repressor…”
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The Biotin Repressor:  Thermodynamic Coupling of Corepressor Binding, Protein Assembly, and Sequence-Specific DNA Binding by Streaker, Emily D, Gupta, Aditi, Beckett, Dorothy

“…The Escherichia coli biotin repressor, an allosteric transcriptional regulator, is activated for binding to the biotin operator by the small molecule…”
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Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase by Kwon, Keehwan, Streaker, Emily D., Beckett, Dorothy

“…The binding of the Escherichia coli biotin holoenzyme synthetase to the two ligands, biotin and bio‐5′‐AMP, is coupled to disorder‐to‐order transitions in the…”
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Coupling of Site-Specific DNA Binding to Protein Dimerization in Assembly of the Biotin Repressor−Biotin Operator Complex by Streaker, Emily D, Beckett, Dorothy

“…The Escherichia coli repressor of biotin biosynthesis, BirA, binds site-specifically to the biotin operator, a 40 base pair imperfect inverted palindrome. Two…”
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A map of the biotin repressor-biotin operator interface: binding of a winged helix-turn-helix protein dimer to a forty base-pair site by Streaker, Emily D, Beckett, Dorothy

“…The Escherichia coli biotin repressor is a member of the “winged helix-turn-helix” class of site-specific DNA binding proteins. The protein binds as a dimer to…”
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Multiple Disordered Loops Function in Corepressor-induced Dimerization of the Biotin Repressor by Kwon, Keehwan, Streaker, Emily D., Ruparelia, Shreyesh, Beckett, Dorothy

“…Cooperative association of the Escherichia coli biotin repressor with the biotin operator is allosterically activated by binding of the corepressor,…”
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Ligand-linked Structural Changes in the Escherichia coli Biotin Repressor: The Significance of Surface Loops for Binding and Allostery by Streaker, Emily D., Beckett, Dorothy

“…The Escherichia coli repressor of biotin biosynthesis (BirA) is an allosteric site-specific DNA-binding protein. BirA catalyzes synthesis of biotinyl-5′-AMP…”
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