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•  Galina Lepesheva

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Publications

• Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.
  Marinko JT, Huang H, Penn WD, Capra JA, Schlebach JP, Sanders CR
  (2019) Chem Rev 119: 5537-5606
• NMR structure and mutagenesis of the FADD (Mort1) death-effector domain.
  Eberstadt M, Huang B, Chen Z, Meadows RP, Ng SC, Zheng L, Lenardo MJ, Fesik SW
  (1998) Nature 392: 941-5
• Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase.
  Van Horn WD, Kim HJ, Ellis CD, Hadziselimovic A, Sulistijo ES, Karra MD, Tian C, Sönnichsen FD, Sanders CR
  (2009) Science 324: 1726-9
• A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.
  Krantz BA, Melnyk RA, Zhang S, Juris SJ, Lacy DB, Wu Z, Finkelstein A, Collier RJ
  (2005) Science 309: 777-81
• The structure of human 5-lipoxygenase.
  Gilbert NC, Bartlett SG, Waight MT, Neau DB, Boeglin WE, Brash AR, Newcomer ME
  (2011) Science 331: 217-9
• A sperm cytoskeletal protein that signals oocyte meiotic maturation and ovulation.
  Miller MA, Nguyen VQ, Lee MH, Kosinski M, Schedl T, Caprioli RM, Greenstein D
  (2001) Science 291: 2144-7
• Islet amyloid polypeptide, islet amyloid, and diabetes mellitus.
  Westermark P, Andersson A, Westermark GT
  (2011) Physiol Rev 91: 795-826
• Asymmetries in the nucleosome core particle at 2.5 A resolution.
  Harp JM, Hanson BL, Timm DE, Bunick GJ
  (2000) Acta Crystallogr D Biol Crystallogr 56: 1513-34
• Side-chain orientation and hydrogen-bonding imprint supra-Tau(c) motion on the protein backbone of ubiquitin.
  Lakomek NA, Farès C, Becker S, Carlomagno T, Meiler J, Griesinger C
  (2005) Angew Chem Int Ed Engl 44: 7776-8
• Peptide influences the folding and intracellular transport of free major histocompatibility complex class I heavy chains.
  Machold RP, Andrée S, Van Kaer L, Ljunggren HG, Ploegh HL
  (1995) J Exp Med 181: 1111-22
• Cole-Carpenter syndrome is caused by a heterozygous missense mutation in P4HB.
  Rauch F, Fahiminiya S, Majewski J, Carrot-Zhang J, Boudko S, Glorieux F, Mort JS, Bächinger HP, Moffatt P
  (2015) Am J Hum Genet 96: 425-31
• UNC-45a promotes myosin folding and stress fiber assembly.
  Lehtimäki JI, Fenix AM, Kotila TM, Balistreri G, Paavolainen L, Varjosalo M, Burnette DT, Lappalainen P
  (2017) J Cell Biol 216: 4053-4072
• ERAD-icating mutant insulin promotes functional insulin secretion.
  Moore DJ
  (2017) Sci Transl Med 9:
• Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients.
  Schonhoft JD, Monteiro C, Plate L, Eisele YS, Kelly JM, Boland D, Parker CG, Cravatt BF, Teruya S, Helmke S, Maurer M, Berk J, Sekijima Y, Novais M, Coelho T, Powers ET, Kelly JW
  (2017) Sci Transl Med 9:
• 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
• Potential of fragment recombination for rational design of proteins.
  Eisenbeis S, Proffitt W, Coles M, Truffault V, Shanmugaratnam S, Meiler J, Höcker B
  (2012) J Am Chem Soc 134: 4019-22
• Conformational Stability and Pathogenic Misfolding of the Integral Membrane Protein PMP22.
  Schlebach JP, Narayan M, Alford C, Mittendorf KF, Carter BD, Li J, Sanders CR
  (2015) J Am Chem Soc 137: 8758-68
• Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier.
  Bachmann A, Kiefhaber T, Boudko S, Engel J, Bächinger HP
  (2005) Proc Natl Acad Sci U S A 102: 13897-902
• Structure of a DNA glycosylase that unhooks interstrand cross-links.
  Mullins EA, Warren GM, Bradley NP, Eichman BF
  (2017) Proc Natl Acad Sci U S A 114: 4400-4405
• Origin and prediction of free-solution interaction studies performed label-free.
  Bornhop DJ, Kammer MN, Kussrow A, Flowers RA, Meiler J
  (2016) Proc Natl Acad Sci U S A 113: E1595-604
• Coupled prediction of protein secondary and tertiary structure.
  Meiler J, Baker D
  (2003) Proc Natl Acad Sci U S A 100: 12105-10
• Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1.
  Betz SF, Schnuchel A, Wang H, Olejniczak ET, Meadows RP, Lipsky BP, Harris EA, Staunton DE, Fesik SW
  (1998) Proc Natl Acad Sci U S A 95: 7909-14
• Rapid protein fold determination using unassigned NMR data.
  Meiler J, Baker D
  (2003) Proc Natl Acad Sci U S A 100: 15404-9
• How activated receptors couple to G proteins.
  Hamm HE
  (2001) Proc Natl Acad Sci U S A 98: 4819-21
• Insulin gene mutations as a cause of permanent neonatal diabetes.
  Støy J, Edghill EL, Flanagan SE, Ye H, Paz VP, Pluzhnikov A, Below JE, Hayes MG, Cox NJ, Lipkind GM, Lipton RB, Greeley SA, Patch AM, Ellard S, Steiner DF, Hattersley AT, Philipson LH, Bell GI, Neonatal Diabetes International Collaborative Group
  (2007) Proc Natl Acad Sci U S A 104: 15040-4
• Assay strategies for identification of therapeutic leads that target protein trafficking.
  Conn PM, Spicer TP, Scampavia L, Janovick JA
  (2015) Trends Pharmacol Sci 36: 498-505
• Hybrid approaches: applying computational methods in cryo-electron microscopy.
  Lindert S, Stewart PL, Meiler J
  (2009) Curr Opin Struct Biol 19: 218-25
• Proteasome inhibition drastically but reversibly impairs murine lymphocyte development.
  Maseda D, Meister S, Neubert K, Herrmann M, Voll RE
  (2008) Cell Death Differ 15: 600-12
• Structural basis for the Trembler-J phenotype of Charcot-Marie-Tooth disease.
  Sakakura M, Hadziselimovic A, Wang Z, Schey KL, Sanders CR
  (2011) Structure 19: 1160-9
• 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
• EM-fold: de novo atomic-detail protein structure determination from medium-resolution density maps.
  Lindert S, Alexander N, Wötzel N, Karakaş M, Stewart PL, Meiler J
  (2012) Structure 20: 464-78
• BCL::MP-fold: folding membrane proteins through assembly of transmembrane helices.
  Weiner BE, Woetzel N, Karakaş M, Alexander N, Meiler J
  (2013) Structure 21: 1107-17
• Crystal structure and mechanism of a carbon-carbon bond hydrolase.
  Timm DE, Mueller HA, Bhanumoorthy P, Harp JM, Bunick GJ
  (1999) Structure 7: 1023-33
• 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
• De novo high-resolution protein structure determination from sparse spin-labeling EPR data.
  Alexander N, Bortolus M, Al-Mestarihi A, Mchaourab H, Meiler J
  (2008) Structure 16: 181-95
• Structural basis for ligand recognition and activation of RAGE.
  Koch M, Chitayat S, Dattilo BM, Schiefner A, Diez J, Chazin WJ, Fritz G
  (2010) Structure 18: 1342-52
• Electrospray droplet exposure to gaseous acids for the manipulation of protein charge state distributions.
  Kharlamova A, Prentice BM, Huang TY, McLuckey SA
  (2010) Anal Chem 82: 7422-9
• Finding the needle in the haystack: towards solving the protein-folding problem computationally.
  Li B, Fooksa M, Heinze S, Meiler J
  (2018) Crit Rev Biochem Mol Biol 53: 1-28
• Histone folds mediate selective heterodimerization of yeast TAF(II)25 with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7.
  Gangloff YG, Sanders SL, Romier C, Kirschner D, Weil PA, Tora L, Davidson I
  (2001) Mol Cell Biol 21: 1841-53
• Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity.
  Hansen WJ, Ohh M, Moslehi J, Kondo K, Kaelin WG, Welch WJ
  (2002) Mol Cell Biol 22: 1947-60