Search Results - "Kruziki, Max A"

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  1. 1

    Identification of Transport Proteins Involved in Free Fatty Acid Efflux in Escherichia coli by Lennen, Rebecca M, Politz, Mark G, Kruziki, Max A, Pfleger, Brian F

    Published in Journal of Bacteriology (01-01-2013)
    “…Escherichia coli has been used as a platform host for studying the production of free fatty acids (FFA) and other energy-dense compounds useful in biofuel…”
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    Journal Article
  2. 2

    Membrane Stresses Induced by Overproduction of Free Fatty Acids in Escherichia coli by LENNEN, Rebecca M, KRUZIKI, Max A, PFLEGER, Brian F, KUMAR, Kritika, ZINKEL, Robert A, BURNUM, Kristin E, LIPTON, Mary S, HOOVER, Spencer W, RANATUNGA, Don R, WITTKOPP, Tyler M, MARNER, Wesley D

    Published in Applied and Environmental Microbiology (01-11-2011)
    “…Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit…”
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    Journal Article
  3. 3

    Constrained Combinatorial Libraries of Gp2 Proteins Enhance Discovery of PD-L1 Binders by Kruziki, Max A, Sarma, Vidur, Hackel, Benjamin J

    Published in ACS combinatorial science (09-07-2018)
    “…Engineered protein ligands are used for molecular therapy, diagnostics, and industrial biotechnology. The Gp2 domain is a 45-amino acid scaffold that has been…”
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    Journal Article
  4. 4

    Engineered Charge Redistribution of Gp2 Proteins through Guided Diversity for Improved PET Imaging of Epidermal Growth Factor Receptor by Case, Brett A, Kruziki, Max A, Johnson, Sadie M, Hackel, Benjamin J

    Published in Bioconjugate chemistry (16-05-2018)
    “…The Gp2 domain is a protein scaffold for synthetic ligand engineering. However, the native protein function results in a heterogeneous distribution of charge…”
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    Journal Article
  5. 5

    Engineering an EGFR‐binding Gp2 domain for increased hydrophilicity by Du, Feifan, Kruziki, Max A., Zudock, Elizabeth J., Zhang, Yi, Lown, Patrick S., Hackel, Benjamin J.

    Published in Biotechnology and bioengineering (01-03-2019)
    “…The Gp2 domain is a 45 amino‐acid scaffold that has been evolved for specific, high‐affinity binding towards multiple targets and was proven useful in…”
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    Journal Article
  6. 6

    A 45-Amino-Acid Scaffold Mined from the PDB for High-Affinity Ligand Engineering by Kruziki, Max A., Bhatnagar, Sumit, Woldring, Daniel R., Duong, Vandon T., Hackel, Benjamin J.

    Published in Chemistry & biology (23-07-2015)
    “…Small protein ligands can provide superior physiological distribution compared with antibodies, and improved stability, production, and specific conjugation…”
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    Journal Article
  7. 7

    64Cu-Labeled Gp2 Domain for PET Imaging of Epidermal Growth Factor Receptor by Kruziki, Max A, Case, Brett A, Chan, Jie Y, Zudock, Elizabeth J, Woldring, Daniel R, Yee, Douglas, Hackel, Benjamin J

    Published in Molecular pharmaceutics (07-11-2016)
    “…This purpose of this study is to determine the efficacy of a 45-amino acid Gp2 domain, engineered to bind to epidermal growth factor receptor (EGFR), as a…”
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    Journal Article
  8. 8

    64 Cu-Labeled Gp2 Domain for PET Imaging of Epidermal Growth Factor Receptor by Kruziki, Max A, Case, Brett A, Chan, Jie Y, Zudock, Elizabeth J, Woldring, Daniel R, Yee, Douglas, Hackel, Benjamin J

    Published in Molecular pharmaceutics (07-11-2016)
    “…This purpose of this study is to determine the efficacy of a 45-amino acid Gp2 domain, engineered to bind to epidermal growth factor receptor (EGFR), as a…”
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    Journal Article
  9. 9

    A 45-amino acid scaffold mined from the Protein Data Bank for high affinity ligand engineering by Kruziki, Max A., Bhatnagar, Sumit, Woldring, Daniel R., Duong, Vandon T., Hackel, Benjamin J.

    Published in Chemistry & biology (09-07-2015)
    “…Small protein ligands can provide superior physiological distribution versus antibodies and improved stability, production, and specific conjugation…”
    Get full text
    Journal Article