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•  Bih-Hwa Shieh

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Publications

• The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S.
  Noel JP, Hamm HE, Sigler PB
  (1993) Nature 366: 654-63
• Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser.
  Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, Barty A, White TA, Yefanov O, Han GW, Xu Q, de Waal PW, Ke J, Tan MH, Zhang C, Moeller A, West GM, Pascal BD, Van Eps N, Caro LN, Vishnivetskiy SA, Lee RJ, Suino-Powell KM, Gu X, Pal K, Ma J, Zhi X, Boutet S, Williams GJ, Messerschmidt M, Gati C, Zatsepin NA, Wang D, James D, Basu S, Roy-Chowdhury S, Conrad CE, Coe J, Liu H, Lisova S, Kupitz C, Grotjohann I, Fromme R, Jiang Y, Tan M, Yang H, Li J, Wang M, Zheng Z, Li D, Howe N, Zhao Y, Standfuss J, Diederichs K, Dong Y, Potter CS, Carragher B, Caffrey M, Jiang H, Chapman HN, Spence JC, Fromme P, Weierstall U, Ernst OP, Katritch V, Gurevich VV, Griffin PR, Hubbell WL, Stevens RC, Cherezov V, Melcher K, Xu HE
  (2015) Nature 523: 561-7
• Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors.
  Zhou XE, He Y, de Waal PW, Gao X, Kang Y, Van Eps N, Yin Y, Pal K, Goswami D, White TA, Barty A, Latorraca NR, Chapman HN, Hubbell WL, Dror RO, Stevens RC, Cherezov V, Gurevich VV, Griffin PR, Ernst OP, Melcher K, Xu HE
  (2017) Cell 170: 457-469.e13
• Molecular basis for interactions of G protein betagamma subunits with effectors.
  Ford CE, Skiba NP, Bae H, Daaka Y, Reuveny E, Shekter LR, Rosal R, Weng G, Yang CS, Iyengar R, Miller RJ, Jan LY, Lefkowitz RJ, Hamm HE
  (1998) Science 280: 1271-4
• Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit.
  Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, Hofmann KP
  (1988) Science 241: 832-5
• Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.
  Nair KS, Hanson SM, Mendez A, Gurevich EV, Kennedy MJ, Shestopalov VI, Vishnivetskiy SA, Chen J, Hurley JB, Gurevich VV, Slepak VZ
  (2005) Neuron 46: 555-67
• Influence of Arrestin on the Photodecay of Bovine Rhodopsin.
  Chatterjee D, Eckert CE, Slavov C, Saxena K, Fürtig B, Sanders CR, Gurevich VV, Wachtveitl J, Schwalbe H
  (2015) Angew Chem Int Ed Engl 54: 13555-60
• Contribution of Cotranslational Folding Defects to Membrane Protein Homeostasis.
  Roushar FJ, Gruenhagen TC, Penn WD, Li B, Meiler J, Jastrzebska B, Schlebach JP
  (2019) J Am Chem Soc 141: 204-215
• Structure and function of the visual arrestin oligomer.
  Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV
  (2007) EMBO J 26: 1726-36
• Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.
  Hanson SM, Francis DJ, Vishnivetskiy SA, Kolobova EA, Hubbell WL, Klug CS, Gurevich VV
  (2006) Proc Natl Acad Sci U S A 103: 4900-5
• Conformation of receptor-bound visual arrestin.
  Kim M, Vishnivetskiy SA, Van Eps N, Alexander NS, Cleghorn WM, Zhan X, Hanson SM, Morizumi T, Ernst OP, Meiler J, Gurevich VV, Hubbell WL
  (2012) Proc Natl Acad Sci U S A 109: 18407-12
• Identification of key factors that reduce the variability of the single photon response.
  Caruso G, Bisegna P, Andreucci D, Lenoci L, Gurevich VV, Hamm HE, DiBenedetto E
  (2011) Proc Natl Acad Sci U S A 108: 7804-7
• Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina.
  Moaven H, Koike Y, Jao CC, Gurevich VV, Langen R, Chen J
  (2013) Proc Natl Acad Sci U S A 110: 9463-8
• Each rhodopsin molecule binds its own arrestin.
  Hanson SM, Gurevich EV, Vishnivetskiy SA, Ahmed MR, Song X, Gurevich VV
  (2007) Proc Natl Acad Sci U S A 104: 3125-8
• Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit.
  Van Eps N, Preininger AM, Alexander N, Kaya AI, Meier S, Meiler J, Hamm HE, Hubbell WL
  (2011) Proc Natl Acad Sci U S A 108: 9420-4
• Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin.
  Zhuang T, Chen Q, Cho MK, Vishnivetskiy SA, Iverson TM, Gurevich VV, Sanders CR
  (2013) Proc Natl Acad Sci U S A 110: 942-7
• Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins.
  Oldham WM, Van Eps N, Preininger AM, Hubbell WL, Hamm HE
  (2007) Proc Natl Acad Sci U S A 104: 7927-32
• How activated receptors couple to G proteins.
  Hamm HE
  (2001) Proc Natl Acad Sci U S A 98: 4819-21
• Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation.
  Song X, Vishnivetskiy SA, Gross OP, Emelianoff K, Mendez A, Chen J, Gurevich EV, Burns ME, Gurevich VV
  (2009) Curr Biol 19: 700-5
• Insights into congenital stationary night blindness based on the structure of G90D rhodopsin.
  Singhal A, Ostermaier MK, Vishnivetskiy SA, Panneels V, Homan KT, Tesmer JJ, Veprintsev D, Deupi X, Gurevich VV, Schertler GF, Standfuss J
  (2013) EMBO Rep 14: 520-6
• Custom-designed proteins as novel therapeutic tools? The case of arrestins.
  Gurevich VV, Gurevich EV
  (2010) Expert Rev Mol Med 12: e13
• EM-fold: De novo folding of alpha-helical proteins guided by intermediate-resolution electron microscopy density maps.
  Lindert S, Staritzbichler R, Wötzel N, Karakaş M, Stewart PL, Meiler J
  (2009) Structure 17: 990-1003
• Integrated Structural Biology for α-Helical Membrane Protein Structure Determination.
  Xia Y, Fischer AW, Teixeira P, Weiner B, Meiler J
  (2018) Structure 26: 657-666.e2
• Interaction of rhodopsin with the G-protein, transducin.
  Hargrave PA, Hamm HE, Hofmann KP
  (1993) Bioessays 15: 43-50
• Intracellular topography of rhodopsin regeneration in vertebrate rods.
  Williams TP, Penn JS
  (1985) J Gen Physiol 86: 413-22
• Interaction of transducin with light-activated rhodopsin protects It from proteolytic digestion by trypsin.
  Mazzoni MR, Hamm HE
  (1996) J Biol Chem 271: 30034-40
• Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction.
  Gurevich VV, Benovic JL
  (1992) J Biol Chem 267: 21919-23
• A monoclonal antibody against the rod outer segment guanyl nucleotide-binding protein, transducin, blocks the stimulatory and inhibitory G proteins of adenylate cyclase.
  Hamm HE, Deretic D, Mazzoni MR, Moore CA, Takahashi JS, Rasenick MM
  (1989) J Biol Chem 264: 11475-82
• Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin.
  Gurevich VV, Benovic JL
  (1995) J Biol Chem 270: 6010-6
• Visual arrestin binding to rhodopsin. Intramolecular interaction between the basic N terminus and acidic C terminus of arrestin may regulate binding selectivity.
  Gurevich VV, Chen CY, Kim CM, Benovic JL
  (1994) J Biol Chem 269: 8721-7
• Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition.
  Krupnick JG, Gurevich VV, Schepers T, Hamm HE, Benovic JL
  (1994) J Biol Chem 269: 3226-32
• Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin.
  Krupnick JG, Gurevich VV, Benovic JL
  (1997) J Biol Chem 272: 18125-31
• The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms.
  Gurevich VV
  (1998) J Biol Chem 273: 15501-6
• Antagonists of the receptor-G protein interface block Gi-coupled signal transduction.
  Gilchrist A, Mazzoni MR, Dineen B, Dice A, Linden J, Proctor WR, Lupica CR, Dunwiddie TV, Hamm HE
  (1998) J Biol Chem 273: 14912-9
• How does arrestin respond to the phosphorylated state of rhodopsin?
  Vishnivetskiy SA, Paz CL, Schubert C, Hirsch JA, Sigler PB, Gurevich VV
  (1999) J Biol Chem 274: 11451-4
• Structural requirements for the stabilization of metarhodopsin II by the C terminus of the alpha subunit of transducin.
  Aris L, Gilchrist A, Rens-Domiano S, Meyer C, Schatz PJ, Dratz EA, Hamm HE
  (2001) J Biol Chem 276: 2333-9
• Functional roles of the two domains of phosducin and phosducin-like protein.
  Savage JR, McLaughlin JN, Skiba NP, Hamm HE, Willardson BM
  (2000) J Biol Chem 275: 30399-407
• Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge.
  Vishnivetskiy SA, Hirsch JA, Velez MG, Gurevich YV, Gurevich VV
  (2002) J Biol Chem 277: 43961-7
• Visual arrestin binding to microtubules involves a distinct conformational change.
  Hanson SM, Francis DJ, Vishnivetskiy SA, Klug CS, Gurevich VV
  (2006) J Biol Chem 281: 9765-72
• Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding.
  Bayburt TH, Vishnivetskiy SA, McLean MA, Morizumi T, Huang CC, Tesmer JJ, Ernst OP, Sligar SG, Gurevich VV
  (2011) J Biol Chem 286: 1420-8