Wolfgang Peti

Summary

Affiliation: Brown University
Country: USA

Publications

  1. pmc Structural basis for protein phosphatase 1 regulation and specificity
    Wolfgang Peti
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    FEBS J 280:596-611. 2013
  2. pmc Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
    Michael J Ragusa
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, USA
    Nat Struct Mol Biol 17:459-64. 2010
  3. pmc Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex
    Barbara Dancheck
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02912, United States
    Biochemistry 50:1238-46. 2011
  4. pmc Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity
    Anderson S Pinheiro
    Department of Molecular Pharmacology, Brown University, Providence, Rhode Island 02912, USA
    J Biol Chem 285:27402-10. 2010
  5. pmc Flexibility in the PP1:spinophilin holoenzyme
    Michael J Ragusa
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA
    FEBS Lett 585:36-40. 2011
  6. pmc Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa
    Dorothy Koveal
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA
    J Mol Biol 425:2219-31. 2013
  7. pmc The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme
    Nichole O'Connell
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    Structure 20:1746-56. 2012
  8. pmc Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
    Matthew S Kelker
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02903, USA
    J Mol Biol 385:11-21. 2009
  9. pmc Structural basis of substrate recognition by hematopoietic tyrosine phosphatase
    David A Critton
    Department of Molecular Biology, Brown University, Providence, Rhode Island 02912, USA
    Biochemistry 47:13336-45. 2008
  10. pmc The NLRP12 pyrin domain: structure, dynamics, and functional insights
    Anderson S Pinheiro
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02903, USA
    J Mol Biol 413:790-803. 2011

Collaborators

  • Robert Schwarzenbacher
  • Gerhard Hummer
  • Marc Allaire
  • Mathieu Bollen
  • Monique Beullens
  • Deborah K Morrison
  • Joseph A Marsh
  • Rebecca Page
  • Dorothy Koveal
  • Anderson S Pinheiro
  • Breann L Brown
  • Michael J Ragusa
  • Barbara Dancheck
  • Angus C Nairn
  • Matthew S Kelker
  • Simina Grigoriu
  • Thomas K Wood
  • Tingting Ju
  • Dana M Francis
  • Antoni Tortajada
  • David A Critton
  • Dana May Francis
  • Meng S Choy
  • Nichole O'Connell
  • Bartosz Różycki
  • Clarissa Eibl
  • Martina Proell
  • Anderson de Sa Pinheiro
  • Jebecka Hudak
  • Dana M Lord
  • Jennifer A Chen
  • Michael W Clarkson
  • Ganesan Senthil Kumar
  • Nina Ly
  • Thusitha B Jayasundera
  • Pilar Cossio
  • Rachel Bond
  • Martha S Cyert
  • Ewald Heroes
  • Daniel Ritt
  • Scott R Nichols
  • Natasha Schuh-Nuhfer
  • Julie D Forman-Kay
  • Zeynep Ekman-Vural
  • Jennifer M Arruda
  • Younghoon Kim
  • Andrew Davenport
  • Nina Ebner
  • Angela Ehart
  • Geoffrey Stetson
  • Rene P Kessler

Detail Information

Publications29

  1. pmc Structural basis for protein phosphatase 1 regulation and specificity
    Wolfgang Peti
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    FEBS J 280:596-611. 2013
    ..Here, we discuss recent advances in structural studies of PP1 holoenzyme complexes and summarize the new insights these studies have provided into the molecular basis of PP1 regulation and specificity...
  2. pmc Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
    Michael J Ragusa
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, USA
    Nat Struct Mol Biol 17:459-64. 2010
    ..Thus, our work provides the molecular basis for the ability of spinophilin to dictate PP1 substrate specificity...
  3. pmc Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex
    Barbara Dancheck
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02912, United States
    Biochemistry 50:1238-46. 2011
    ..Collectively, these data reveal the molecular events that enable PP1 heterotrimeric complexes to exploit both the targeting and inhibitory features of the PP1-regulatory proteins to form multifunctional PP1 holoenzymes...
  4. pmc Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity
    Anderson S Pinheiro
    Department of Molecular Pharmacology, Brown University, Providence, Rhode Island 02912, USA
    J Biol Chem 285:27402-10. 2010
    ..Thus, these results provide new insights into NLRP signaling and provide a first molecular understanding of inflammasome formation...
  5. pmc Flexibility in the PP1:spinophilin holoenzyme
    Michael J Ragusa
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA
    FEBS Lett 585:36-40. 2011
    ..Collectively, our data shows that the PP1:spinophilin holoenzyme is dynamic in solution, which allows for an increased capture radius of spinophilin and is likely important for its biological role...
  6. pmc Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa
    Dorothy Koveal
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA
    J Mol Biol 425:2219-31. 2013
    ..Taken together, these data structurally distinguish TpbA and possibly other bacterial DUSPs from eukaryotic DUSPs and provide a rich picture of active-site dynamics in the ligand-free state that are lost upon ligand binding...
  7. pmc The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme
    Nichole O'Connell
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    Structure 20:1746-56. 2012
    ..Together, our results provide the molecular basis by which NIPP1 directs PP1 substrate specificity in the nucleus...
  8. pmc Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
    Matthew S Kelker
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02903, USA
    J Mol Biol 385:11-21. 2009
    ..Furthermore, since tautomycin is a linear non-peptide-based toxin, our reported structure will aid the design of lead compounds for novel PP1-specific pharmaceuticals...
  9. pmc Structural basis of substrate recognition by hematopoietic tyrosine phosphatase
    David A Critton
    Department of Molecular Biology, Brown University, Providence, Rhode Island 02912, USA
    Biochemistry 47:13336-45. 2008
    ..g., Erk2, p38). Finally, we describe how this interaction of the KIM is sufficient for overcoming the otherwise weak interaction at the active site of KIM-PTPs...
  10. pmc The NLRP12 pyrin domain: structure, dynamics, and functional insights
    Anderson S Pinheiro
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02903, USA
    J Mol Biol 413:790-803. 2011
    ..Finally, we experimentally highlight a significant role for tryptophan 45 in the interaction between NLRP12 PYD and the FAF-1 UBA domain...
  11. ncbi request reprint Structural characterization of the neurabin sterile alpha motif domain
    Tingting Ju
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02912, USA
    Proteins 69:192-8. 2007
  12. pmc Structural basis of p38α regulation by hematopoietic tyrosine phosphatase
    Dana M Francis
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, USA
    Nat Chem Biol 7:916-24. 2011
    ..Together, these results show how the downstream tyrosine phosphatase HePTP regulates p38α and provide for fundamentally new insights into MAPK regulation and specificity...
  13. pmc A CC-SAM, for coiled coil-sterile α motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane
    Dorothy Koveal
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA
    Sci Signal 5:ra94. 2012
    ..Thus, in addition to the atypical C1 domain, the CC-SAM domain is required to target KSR-1 to the plasma membrane...
  14. pmc Detailed structural characterization of unbound protein phosphatase 1 inhibitors
    Barbara Dancheck
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02912, USA
    Biochemistry 47:12346-56. 2008
    ..Together, these interactions enable potent and selective inhibition of PP1...
  15. pmc Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation
    Breann L Brown
    Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, Rhode Island 02912, USA
    J Biol Chem 286:2285-96. 2011
    ..Finally, using a combination of biochemical and NMR studies, we show that the DNA sequence specificity of MqsA is mediated by direct readout...
  16. ncbi request reprint Structural basis for spinophilin-neurabin receptor interaction
    Matthew S Kelker
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, 70 Ship Street, Box G E3, Providence, Rhode Island 02912, USA
    Biochemistry 46:2333-44. 2007
    ..Finally, the ability to bind to glutamate receptor subunits suggests that the PDZ domains of neurabin and spinophilin are important for targeting PP1 to C-terminal phosphorylation sites in AMPA and NMDA receptor subunits...
  17. pmc The Escherichia coli toxin MqsR destabilizes the transcriptional repression complex formed between the antitoxin MqsA and the mqsRA operon promoter
    Breann L Brown
    Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, Rhode Island 02912, USA
    J Biol Chem 288:1286-94. 2013
    ....
  18. pmc Regulation of protein phosphatase 1 by intrinsically disordered proteins
    Meng S Choy
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    Biochem Soc Trans 40:969-74. 2012
    ....
  19. pmc Structural signature of the MYPT1-PP1 interaction
    Anderson S Pinheiro
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02903, USA
    J Am Chem Soc 133:73-80. 2011
    ..Thus, this work adds significant insights to the currently limited data for molecular structures and dynamics of PP1 regulators...
  20. doi request reprint Backbone and side chain 1H, 15N and 13C assignments of the KSR1 CA1 domain
    Dorothy Koveal
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA
    Biomol NMR Assign 5:39-41. 2011
    ..This assignment is the first step towards the determination of the three-dimensional structure of the unique KSR1 CA1 domain...
  21. pmc The Differential Regulation of p38α by the Neuronal Kinase Interaction Motif Protein Tyrosine Phosphatases, a Detailed Molecular Study
    Dana May Francis
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    Structure 21:1612-23. 2013
    ..Together, these results provide insights into molecular regulation of p38α by key regulatory proteins. ..
  22. doi request reprint Backbone and sidechain (1)H, (15)N and (13)C assignments of Tyrosine Phosphatase related to Biofilm formation A (TpbA) of Pseudomonas aeruginosa
    Dorothy Koveal
    Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02903, USA
    Biomol NMR Assign 7:57-9. 2013
    ..This assignment is the first step towards the determination of the 3-dimensional structure of TpbA...
  23. ncbi request reprint Backbone and sidechain (1)H, (15)N and (13)C assignments of the human G-actin binding protein profilin IIa
    Tingting Ju
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    Biomol NMR Assign 1:205-7. 2007
    ..These assignments facilitate further studies of interactions between profilin IIa and its poly-L: -proline rich ligands...
  24. pmc The molecular mechanism of substrate engagement and immunosuppressant inhibition of calcineurin
    Simina Grigoriu
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, USA
    PLoS Biol 11:e1001492. 2013
    ..Collectively, this work presents the first integrated structural model for substrate selection and dephosphorylation by CN and lays the groundwork for structure-based development of new CN inhibitors...
  25. pmc Resting and active states of the ERK2:HePTP complex
    Dana M Francis
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island 02912, USA
    J Am Chem Soc 133:17138-41. 2011
    ..This work experimentally demonstrates that these complexes undergo significant dynamic structural changes in solution and provides the first structural insight into an active state MAPK complex...
  26. pmc Three dimensional structure of the MqsR:MqsA complex: a novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties
    Breann L Brown
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, USA
    PLoS Pathog 5:e1000706. 2009
    ..These studies reveal that TA systems, especially the antitoxins, are significantly more diverse than previously recognized and provide new insights into the role of toxins in maintaining the persister state...
  27. doi request reprint Backbone and sidechain (1)H, (15)N and (13)C assignments of the NLRP7 pyrin domain
    Anderson de Sa Pinheiro
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02903, USA
    Biomol NMR Assign 3:207-9. 2009
    ..This assignment is the first step towards the 3D structure determination of the NLRP7 PYD domain...
  28. ncbi request reprint Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost
    Wolfgang Peti
    Brown University, Department of Molecular Pharmacology, Physiology, and Biotechnology, Box G E3, Providence, RI 02912, USA
    Protein Expr Purif 51:1-10. 2007
    ....
  29. ncbi request reprint NMR assignment of the spinophilin PDZ domain (493-602)
    Matthew S Kelker
    Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA
    J Biomol NMR 36:24. 2006