Header Logo
Last Name

Augen A Pioszak

InstitutionUniversity of Oklahoma Health Sciences Center
DepartmentBiochemistry/Molecular Biology
vCardDownload vCard

    Collapse Biography 
    Collapse education and training
    University of Michigan, Ann Arbor, MIPhD2003Biological Chemistry
    RIKEN Yokohama Institute, Yokohama, JAPANPostdoc2005Protein X-ray Crystallography
    Van Andel Research Institute, Grand Rapids, MIPostdoc2010Structural Biology of G Protein-coupled Receptors

    Collapse Research 
    Collapse research activities and funding
    R01GM104251     (PIOSZAK, AUGEN A)Sep 26, 2012 - Aug 31, 2021
    RAMP-altered class B GPCR hormone recognition
    Role: Principal Investigator

    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
    List All   |   Timeline
    1. Roehrkasse AM, Booe JM, Lee SM, Warner ML, Pioszak AA. Structure-function analyses reveal a triple ß-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design. J Biol Chem. 2018 Oct 12; 293(41):15840-15854. PMID: 30139742.
      View in: PubMed
    2. Booe JM, Warner ML, Roehrkasse AM, Hay DL, Pioszak AA. Probing the Mechanism of Receptor Activity-Modifying Protein Modulation of GPCR Ligand Selectivity through Rational Design of Potent Adrenomedullin and Calcitonin Gene-Related Peptide Antagonists. Mol Pharmacol. 2018 04; 93(4):355-367. PMID: 29363552.
      View in: PubMed
    3. Lee SM, Booe JM, Gingell JJ, Sjoelund V, Hay DL, Pioszak AA. N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity. Biochemistry. 2017 07 05; 56(26):3380-3393. PMID: 28614667.
      View in: PubMed
    4. Lee SM, Hay DL, Pioszak AA. Calcitonin and amylin receptor peptide interaction mechanisms. INSIGHTS INTO PEPTIDE-BINDING MODES AND ALLOSTERIC MODULATION OF THE CALCITONIN RECEPTOR BY RECEPTOR ACTIVITY-MODIFYING PROTEINS. J Biol Chem. 2016 07 29; 291(31):16416. PMID: 27474777.
      View in: PubMed
    5. Gingell JJ, Simms J, Barwell J, Poyner DR, Watkins HA, Pioszak AA, Sexton PM, Hay DL. Erratum: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology. Cell Discov. 2016; 2:16020. PMID: 27463403; PMCID: PMC4915271.
    6. J Gingell J, Simms J, Barwell J, Poyner DR, Watkins HA, Pioszak AA, Sexton PM, Hay DL. An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology. Cell Discov. 2016; 2:16012. PMID: 27462459; PMCID: PMC4869360.
    7. Watkins HA, Chakravarthy M, Abhayawardana RS, Gingell JJ, Garelja M, Pardamwar M, McElhinney JM, Lathbridge A, Constantine A, Harris PW, Yuen TY, Brimble MA, Barwell J, Poyner DR, Woolley MJ, Conner AC, Pioszak AA, Reynolds CA, Hay DL. Receptor Activity-modifying Proteins 2 and 3 Generate Adrenomedullin Receptor Subtypes with Distinct Molecular Properties. J Biol Chem. 2016 May 27; 291(22):11657-75. PMID: 27013657.
      View in: PubMed
    8. Lee SM, Hay DL, Pioszak AA. Calcitonin and Amylin Receptor Peptide Interaction Mechanisms: INSIGHTS INTO PEPTIDE-BINDING MODES AND ALLOSTERIC MODULATION OF THE CALCITONIN RECEPTOR BY RECEPTOR ACTIVITY-MODIFYING PROTEINS. J Biol Chem. 2016 Apr 15; 291(16):8686-700. PMID: 26895962; PMCID: PMC4861438 [Available on 04/15/17].
    9. Hay DL, Pioszak AA. Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles. Annu Rev Pharmacol Toxicol. 2016; 56:469-87. PMID: 26514202.
      View in: PubMed
    10. Lee SM, Booe JM, Pioszak AA. Structural insights into ligand recognition and selectivity for classes A, B, and C GPCRs. Eur J Pharmacol. 2015 Sep 15; 763(Pt B):196-205. PMID: 25981303; PMCID: PMC4584177.
    11. Booe JM, Walker CS, Barwell J, Kuteyi G, Simms J, Jamaluddin MA, Warner ML, Bill RM, Harris PW, Brimble MA, Poyner DR, Hay DL, Pioszak AA. Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor. Mol Cell. 2015 Jun 18; 58(6):1040-52. PMID: 25982113.
      View in: PubMed
    12. Warner ML, Bell T, Pioszak AA. Engineering high-potency R-spondin adult stem cell growth factors. Mol Pharmacol. 2015; 87(3):410-20. PMID: 25504990; PMCID: PMC4352588.
    13. Moad HE, Pioszak AA. Selective CGRP and adrenomedullin peptide binding by tethered RAMP-calcitonin receptor-like receptor extracellular domain fusion proteins. Protein Sci. 2013 Dec; 22(12):1775-85. PMID: 24115156; PMCID: PMC3843631.
    14. Moad HE, Pioszak AA. Reconstitution of R-spondin:LGR4:ZNRF3 adult stem cell growth factor signaling complexes with recombinant proteins produced in Escherichia coli. Biochemistry. 2013 Oct 15; 52(41):7295-304. PMID: 24050775; PMCID: PMC3836688.
    15. Hill HE, Pioszak AA. Bacterial expression and purification of a heterodimeric adrenomedullin receptor extracellular domain complex using DsbC-assisted disulfide shuffling. Protein Expr Purif. 2013 Mar; 88(1):107-13. PMID: 23247088; PMCID: PMC3568255.
    16. Kumar S, Pioszak A, Zhang C, Swaminathan K, Xu HE. Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors. PLoS One. 2011; 6(5):e19682. PMID: 21625560.
      View in: PubMed
    17. Pal K, Swaminathan K, Xu HE, Pioszak AA. Structural basis for hormone recognition by the Human CRFR2{alpha} G protein-coupled receptor. J Biol Chem. 2010 Dec 17; 285(51):40351-61. PMID: 20966082.
      View in: PubMed
    18. Pioszak AA, Harikumar KG, Parker NR, Miller LJ, Xu HE. Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation. J Biol Chem. 2010 Apr 16; 285(16):12435-44. PMID: 20172855.
      View in: PubMed
    19. Pioszak AA, Parker NR, Gardella TJ, Xu HE. Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides. J Biol Chem. 2009 Oct 09; 284(41):28382-91. PMID: 19674967.
      View in: PubMed
    20. Pioszak AA, Parker NR, Suino-Powell K, Xu HE. Molecular recognition of corticotropin-releasing factor by its G-protein-coupled receptor CRFR1. J Biol Chem. 2008 Nov 21; 283(47):32900-12. PMID: 18801728.
      View in: PubMed
    21. Pioszak AA, Xu HE. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc Natl Acad Sci U S A. 2008 Apr 01; 105(13):5034-9. PMID: 18375760; PMCID: PMC2278174.
    22. Jiang P, Pioszak AA, Ninfa AJ. Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC of Escherichia coli. Biochemistry. 2007 Apr 03; 46(13):4117-32. PMID: 17355124.
      View in: PubMed
    23. Pioszak AA, Murayama K, Nakagawa N, Ebihara A, Kuramitsu S, Shirouzu M, Yokoyama S. Structures of a putative RNA 5-methyluridine methyltransferase, Thermus thermophilus TTHA1280, and its complex with S-adenosyl-L-homocysteine. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 01; 61(Pt 10):867-74. PMID: 16511182; PMCID: PMC1991318.
    24. Pioszak AA, Ninfa AJ. Mutations altering the N-terminal receiver domain of NRI (NtrC) That prevent dephosphorylation by the NRII-PII complex in Escherichia coli. J Bacteriol. 2004 Sep; 186(17):5730-40. PMID: 15317778; PMCID: PMC516846.
    25. Song Y, Peisach D, Pioszak AA, Xu Z, Ninfa AJ. Crystal structure of the C-terminal domain of the two-component system transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli. Biochemistry. 2004 Jun 01; 43(21):6670-8. PMID: 15157101.
      View in: PubMed
    26. Pioszak AA, Ninfa AJ. Mechanism of the PII-activated phosphatase activity of Escherichia coli NRII (NtrB): how the different domains of NRII collaborate to act as a phosphatase. Biochemistry. 2003 Jul 29; 42(29):8885-99. PMID: 12873150.
      View in: PubMed
    27. Pioszak AA, Ninfa AJ. Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein. J Bacteriol. 2003 Feb; 185(4):1299-315. PMID: 12562801; PMCID: PMC142841.
    28. Pioszak AA, Jiang P, Ninfa AJ. The Escherichia coli PII signal transduction protein regulates the activities of the two-component system transmitter protein NRII by direct interaction with the kinase domain of the transmitter module. Biochemistry. 2000 Nov 07; 39(44):13450-61. PMID: 11063581.
      View in: PubMed
    Pioszak's Networks
    Click the "See All" links for more information and interactive visualizations!
    Concepts Expand Description
    Co-Authors Expand Description
    Similar People Expand Description
    Same Department Expand Description