Year |
Citation |
Score |
2023 |
Träger J, Meister A, Hause G, Harauz G, Hinderberger D. Shaping membrane interfaces in lipid vesicles mimicking the cytoplasmic leaflet of myelin through variation of cholesterol and myelin basic protein contents. Biochimica Et Biophysica Acta. Biomembranes. 184179. PMID 37244538 DOI: 10.1016/j.bbamem.2023.184179 |
0.349 |
|
2020 |
Träger J, Widder K, Kerth A, Harauz G, Hinderberger D. Effect of Cholesterol and Myelin Basic Protein (MBP) Content on Lipid Monolayers Mimicking the Cytoplasmic Membrane of Myelin. Cells. 9. PMID 32106542 DOI: 10.3390/Cells9030529 |
0.442 |
|
2019 |
Widder K, Harauz G, Hinderberger D. Myelin basic protein (MBP) charge variants show different sphingomyelin-mediated interactions with myelin-like lipid monolayers. Biochimica Et Biophysica Acta. Biomembranes. 1862: 183077. PMID 31805269 DOI: 10.1016/J.Bbamem.2019.183077 |
0.414 |
|
2019 |
Avila MD, Vassall K, Smith G, Bamm V, Harauz G. The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19948 |
0.4 |
|
2018 |
Widder K, Träger J, Kerth A, Harauz G, Hinderberger D. Interaction of myelin basic protein with myelin-like lipid monolayers at the air-water interface. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 29722987 DOI: 10.1021/Acs.Langmuir.8B00321 |
0.422 |
|
2017 |
Bamm VV, Henein MEL, Sproul SLJ, Lanthier DK, Harauz G. Potential role of ferric hemoglobin in MS pathogenesis: Effects of oxidative stress and extracellular methemoglobin or its degradation products on myelin components. Free Radical Biology & Medicine. 112: 494-503. PMID 28863941 DOI: 10.1016/J.Freeradbiomed.2017.08.022 |
0.398 |
|
2017 |
Harauz G. And yet it is modified - Holding a candle to the dark matter of white matter. Proteomics. PMID 28851044 DOI: 10.1002/Pmic.201700299 |
0.412 |
|
2017 |
Bessonov K, Vassall KA, Harauz G. Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP) - Insights into a non-canonical and fuzzy interaction. Proteins. PMID 28380689 DOI: 10.1002/Prot.25295 |
0.425 |
|
2016 |
Vassall KA, Bamm VV, Jenkins AD, Velte CJ, Kattnig DR, Boggs JM, Hinderberger D, Harauz G. Substitutions mimicking deimination and phosphorylation of 18.5-kDa myelin basic protein exert local structural effects that subtly influence its global folding. Biochimica Et Biophysica Acta. PMID 26903219 DOI: 10.1016/J.Bbamem.2016.02.024 |
0.477 |
|
2015 |
Vassall KA, Bamm VV, Harauz G. MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis. The Biochemical Journal. 472: 17-32. PMID 26518750 DOI: 10.1042/Bj20150710 |
0.496 |
|
2015 |
Ward ME, Ritz E, Ahmed MA, Bamm VV, Harauz G, Brown LS, Ladizhansky V. Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins. Journal of Biomolecular Nmr. PMID 26494649 DOI: 10.1007/S10858-015-9997-5 |
0.387 |
|
2015 |
Zienowicz A, Bamm VV, Vassall KA, Harauz G. Myelin basic protein is a glial microtubule-associated protein -- characterization of binding domains, kinetics of polymerization, and regulation by phosphorylation and a lipidic environment. Biochemical and Biophysical Research Communications. 461: 136-41. PMID 25862371 DOI: 10.1016/J.Bbrc.2015.03.181 |
0.45 |
|
2015 |
Vassall KA, Jenkins AD, Bamm VV, Harauz G. Thermodynamic analysis of the disorder-to-α-helical transition of 18.5-kDa myelin basic protein reveals an equilibrium intermediate representing the most compact conformation. Journal of Molecular Biology. 427: 1977-92. PMID 25816771 DOI: 10.1016/J.Jmb.2015.03.011 |
0.421 |
|
2015 |
Bamm VV, Lanthier DK, Stephenson EL, Smith GS, Harauz G. In vitro study of the direct effect of extracellular hemoglobin on myelin components. Biochimica Et Biophysica Acta. 1852: 92-103. PMID 25463632 DOI: 10.1016/J.Bbadis.2014.10.009 |
0.36 |
|
2014 |
De Avila M, Vassall KA, Smith GS, Bamm VV, Harauz G. The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro. Bioscience Reports. 34: e00157. PMID 25343306 DOI: 10.1042/Bsr20140149 |
0.439 |
|
2014 |
Boggs JM, Homchaudhuri L, Ranagaraj G, Liu Y, Smith GS, Harauz G. Interaction of myelin basic protein with cytoskeletal and signaling proteins in cultured primary oligodendrocytes and N19 oligodendroglial cells. Bmc Research Notes. 7: 387. PMID 24956930 DOI: 10.1186/1756-0500-7-387 |
0.498 |
|
2014 |
Jaramillo-Tatis S, Bamm VV, Vassall KA, Harauz G. Over-expression in E. coli and purification of functional full-length murine small C-terminal domain phosphatase (SCP1, or Golli-interacting protein). Protein Expression and Purification. 101: 106-14. PMID 24925644 DOI: 10.1016/J.Pep.2014.05.013 |
0.412 |
|
2014 |
Jaramillo-Tatis S, Vassall KA, Bamm VV, Harauz G. Regulatory effect of the glial Golli-BG21 protein on the full-length murine small C-terminal domain phosphatase (SCP1, or Golli-interacting protein). Biochemical and Biophysical Research Communications. 447: 633-7. PMID 24751520 DOI: 10.1016/J.Bbrc.2014.04.050 |
0.414 |
|
2014 |
Lutz D, Loers G, Kleene R, Oezen I, Kataria H, Katagihallimath N, Braren I, Harauz G, Schachner M. Myelin basic protein cleaves cell adhesion molecule L1 and promotes neuritogenesis and cell survival. The Journal of Biological Chemistry. 289: 13503-18. PMID 24671420 DOI: 10.1074/Jbc.M113.530238 |
0.302 |
|
2014 |
Ozgen H, Kahya N, de Jonge JC, Smith GS, Harauz G, Hoekstra D, Baron W. Regulation of cell proliferation by nucleocytoplasmic dynamics of postnatal and embryonic exon-II-containing MBP isoforms. Biochimica Et Biophysica Acta. 1843: 517-30. PMID 24321769 DOI: 10.1016/J.Bbamcr.2013.11.026 |
0.379 |
|
2014 |
Lanthier DK, Vassall KA, Harauz G. Biophysical characterization of 21.5-kDa myelin basic protein (MBP) and the effects of zinc on its structure Surg Journal. 7: 30-41. DOI: 10.21083/Surg.V7I3.2958 |
0.487 |
|
2013 |
Vassall KA, Bessonov K, De Avila M, Polverini E, Harauz G. The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein. Plos One. 8: e68175. PMID 23861868 DOI: 10.1371/Journal.Pone.0068175 |
0.41 |
|
2013 |
Harauz G, Boggs JM. Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoforms. Journal of Neurochemistry. 125: 334-61. PMID 23398367 DOI: 10.1111/Jnc.12195 |
0.491 |
|
2013 |
Rahman LN, McKay F, Giuliani M, Quirk A, Moffatt BA, Harauz G, Dutcher JR. Interactions of Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 with membranes at cold and ambient temperatures-surface morphology and single-molecule force measurements show phase separation, and reveal tertiary and quaternary associations. Biochimica Et Biophysica Acta. 1828: 967-80. PMID 23219803 DOI: 10.1016/J.Bbamem.2012.11.031 |
0.413 |
|
2013 |
Smith GS, Samborska B, Hawley SP, Klaiman JM, Gillis TE, Jones N, Boggs JM, Harauz G. Nucleus-localized 21.5-kDa myelin basic protein promotes oligodendrocyte proliferation and enhances neurite outgrowth in coculture, unlike the plasma membrane-associated 18.5-kDa isoform. Journal of Neuroscience Research. 91: 349-62. PMID 23184356 DOI: 10.1002/Jnr.23166 |
0.433 |
|
2012 |
Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G. Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. Biochemistry. 51: 7475-87. PMID 22947219 DOI: 10.1021/Bi300998X |
0.455 |
|
2012 |
Kattnig DR, Bund T, Boggs JM, Harauz G, Hinderberger D. Lateral self-assembly of 18.5-kDa myelin basic protein (MBP) charge component-C1 on membranes. Biochimica Et Biophysica Acta. 1818: 2636-47. PMID 22728818 DOI: 10.1016/J.Bbamem.2012.06.010 |
0.458 |
|
2012 |
Smith GS, Seymour LV, Boggs JM, Harauz G. The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal. Biochemical and Biophysical Research Communications. 422: 670-5. PMID 22609403 DOI: 10.1016/J.Bbrc.2012.05.051 |
0.493 |
|
2012 |
Nagulapalli M, Parigi G, Yuan J, Gsponer J, Deraos G, Bamm VV, Harauz G, Matsoukas J, de Planque MR, Gerothanassis IP, Babu MM, Luchinat C, Tzakos AG. Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complex. Structure (London, England : 1993). 20: 522-33. PMID 22405011 DOI: 10.1016/J.Str.2012.01.021 |
0.426 |
|
2012 |
Smith GS, Homchaudhuri L, Boggs JM, Harauz G. Classic 18.5- and 21.5-kDa myelin basic protein isoforms associate with cytoskeletal and SH3-domain proteins in the immortalized N19-oligodendroglial cell line stimulated by phorbol ester and IGF-1. Neurochemical Research. 37: 1277-95. PMID 22249765 DOI: 10.1007/S11064-011-0700-2 |
0.504 |
|
2012 |
Smith GS, De Avila M, Paez PM, Spreuer V, Wills MK, Jones N, Boggs JM, Harauz G. Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytes. Journal of Neuroscience Research. 90: 28-47. PMID 21887699 DOI: 10.1002/Jnr.22733 |
0.443 |
|
2011 |
Rahman LN, Smith GS, Bamm VV, Voyer-Grant JA, Moffatt BA, Dutcher JR, Harauz G. Phosphorylation of Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 facilitates cation-induced conformational changes and actin assembly. Biochemistry. 50: 9587-604. PMID 21970344 DOI: 10.1021/Bi201205M |
0.398 |
|
2011 |
Bamm VV, De Avila M, Smith GS, Ahmed MA, Harauz G. Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction. Biophysical Journal. 101: 1248-56. PMID 21889463 DOI: 10.1016/J.Bpj.2011.07.035 |
0.403 |
|
2011 |
Smith GS, Paez PM, Spreuer V, Campagnoni CW, Boggs JM, Campagnoni AT, Harauz G. Classical 18.5-and 21.5-kDa isoforms of myelin basic protein inhibit calcium influx into oligodendroglial cells, in contrast to golli isoforms. Journal of Neuroscience Research. 89: 467-80. PMID 21312222 DOI: 10.1002/Jnr.22570 |
0.377 |
|
2011 |
Boggs JM, Rangaraj G, Heng YM, Liu Y, Harauz G. Myelin basic protein binds microtubules to a membrane surface and to actin filaments in vitro: effect of phosphorylation and deimination. Biochimica Et Biophysica Acta. 1808: 761-73. PMID 21185260 DOI: 10.1016/J.Bbamem.2010.12.016 |
0.426 |
|
2011 |
Polverini E, Coll EP, Tieleman DP, Harauz G. Conformational choreography of a molecular switch region in myelin basic protein--molecular dynamics shows induced folding and secondary structure type conversion upon threonyl phosphorylation in both aqueous and membrane-associated environments. Biochimica Et Biophysica Acta. 1808: 674-83. PMID 21130728 DOI: 10.1016/J.Bbamem.2010.11.030 |
0.481 |
|
2011 |
Rahman LN, Bamm VV, Voyer JA, Smith GS, Chen L, Yaish MW, Moffatt BA, Dutcher JR, Harauz G. Zinc induces disorder-to-order transitions in free and membrane-associated Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2: a solution CD and solid-state ATR-FTIR study. Amino Acids. 40: 1485-502. PMID 20924623 DOI: 10.1007/S00726-010-0759-0 |
0.374 |
|
2011 |
De Avila M, Ahmed MA, Smith GS, Boggs JM, Harauz G. Modes of SH3-Domain Interactions of 18.5 kDa Myelin Basic Protein IN Vitro and in Oligodendrocytes Biophysical Journal. 100: 229a. DOI: 10.1016/J.Bpj.2010.12.1466 |
0.467 |
|
2010 |
Bund T, Boggs JM, Harauz G, Hellmann N, Hinderberger D. Copper uptake induces self-assembly of 18.5 kDa myelin basic protein (MBP). Biophysical Journal. 99: 3020-8. PMID 21044600 DOI: 10.1016/J.Bpj.2010.08.022 |
0.426 |
|
2010 |
Homchaudhuri L, De Avila M, Nilsson SB, Bessonov K, Smith GS, Bamm VV, Musse AA, Harauz G, Boggs JM. Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein. Biochemistry. 49: 8955-66. PMID 20831157 DOI: 10.1021/Bi100988P |
0.475 |
|
2010 |
Ahmed MA, Bamm VV, Harauz G, Ladizhansky V. Solid-state NMR spectroscopy of membrane-associated myelin basic protein--conformation and dynamics of an immunodominant epitope. Biophysical Journal. 99: 1247-55. PMID 20713009 DOI: 10.1016/J.Bpj.2010.06.022 |
0.473 |
|
2010 |
Bamm VV, Ahmed MA, Harauz G. Interaction of myelin basic protein with actin in the presence of dodecylphosphocholine micelles. Biochemistry. 49: 6903-15. PMID 20593886 DOI: 10.1021/Bi100308D |
0.481 |
|
2010 |
Libich DS, Ahmed MA, Zhong L, Bamm VV, Ladizhansky V, Harauz G. Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 143-55. PMID 20453917 DOI: 10.1139/o09-123 |
0.333 |
|
2010 |
Smith GS, Chen L, Bamm VV, Dutcher JR, Harauz G. The interaction of zinc with membrane-associated 18.5 kDa myelin basic protein: an attenuated total reflectance-Fourier transform infrared spectroscopic study. Amino Acids. 39: 739-50. PMID 20169373 DOI: 10.1007/S00726-010-0513-7 |
0.496 |
|
2010 |
Bessonov K, Bamm VV, Harauz G. Misincorporation of the proline homologue Aze (azetidine-2-carboxylic acid) into recombinant myelin basic protein. Phytochemistry. 71: 502-7. PMID 20064647 DOI: 10.1016/J.Phytochem.2009.12.010 |
0.4 |
|
2010 |
Baran C, Smith GS, Bamm VV, Harauz G, Lee JS. Divalent cations induce a compaction of intrinsically disordered myelin basic protein. Biochemical and Biophysical Research Communications. 391: 224-9. PMID 19903451 DOI: 10.1016/J.Bbrc.2009.11.036 |
0.476 |
|
2010 |
Bessonov K, Harauz G. Molecular dynamics investigation of myelin basic protein stability on lipid membranes Surg Journal. 4: 79-86. DOI: 10.21083/Surg.V4I1.1102 |
0.421 |
|
2010 |
Homchaudhuri L, De Avila M, Nilsson SB, Bamm VV, Musse AA, Smith GS, Harauz G, Boggs JM. SDSL-EPR Study of a C-terminal Segment of Myelin Basic Protein in a Myelin Mimetic Environment Biophysical Journal. 98: 232a-233a. DOI: 10.1016/J.Bpj.2009.12.1258 |
0.498 |
|
2009 |
Harauz G, Ladizhansky V, Boggs JM. Structural polymorphism and multifunctionality of myelin basic protein. Biochemistry. 48: 8094-104. PMID 19642704 DOI: 10.1021/Bi901005F |
0.509 |
|
2009 |
Harauz G, Libich DS. The classic basic protein of myelin--conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions. Current Protein & Peptide Science. 10: 196-215. PMID 19519451 DOI: 10.2174/138920309788452218 |
0.504 |
|
2009 |
Homchaudhuri L, Polverini E, Gao W, Harauz G, Boggs JM. Influence of membrane surface charge and post-translational modifications to myelin basic protein on its ability to tether the Fyn-SH3 domain to a membrane in vitro. Biochemistry. 48: 2385-93. PMID 19178193 DOI: 10.1021/Bi8022587 |
0.399 |
|
2009 |
Ahmed MA, Bamm VV, Shi L, Steiner-Mosonyi M, Dawson JF, Brown L, Harauz G, Ladizhansky V. Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin. Biophysical Journal. 96: 180-91. PMID 19134474 DOI: 10.1016/J.Bpj.2008.10.003 |
0.47 |
|
2009 |
Musse AA, Gao W, Rangaraj G, Boggs JM, Harauz G. Myelin basic protein co-distributes with other PI(4,5)P2-sequestering proteins in Triton X-100 detergent-resistant membrane microdomains. Neuroscience Letters. 450: 32-6. PMID 19026719 DOI: 10.1016/J.Neulet.2008.11.022 |
0.448 |
|
2008 |
Musse AA, Li Z, Ackerley CA, Bienzle D, Lei H, Poma R, Harauz G, Moscarello MA, Mastronardi FG. Peptidylarginine deiminase 2 (PAD2) overexpression in transgenic mice leads to myelin loss in the central nervous system. Disease Models & Mechanisms. 1: 229-40. PMID 19093029 DOI: 10.1242/Dmm.000729 |
0.362 |
|
2008 |
Musse AA, Gao W, Homchaudhuri L, Boggs JM, Harauz G. Myelin basic protein as a "PI(4,5)P2-modulin": a new biological function for a major central nervous system protein. Biochemistry. 47: 10372-82. PMID 18767817 DOI: 10.1021/Bi801302B |
0.407 |
|
2008 |
Bamm VV, Harauz G. Expression and purification of the active variant of recombinant murine Golli-interacting protein (GIP)--characterization of its phosphatase activity and interaction with Golli-BG21. Protein Expression and Purification. 62: 36-43. PMID 18625321 DOI: 10.1016/J.Pep.2008.06.004 |
0.392 |
|
2008 |
Libich DS, Harauz G. Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP). European Biophysics Journal : Ebj. 37: 1015-29. PMID 18449534 DOI: 10.1007/S00249-008-0334-8 |
0.39 |
|
2008 |
Libich DS, Harauz G. Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site. Biophysical Journal. 94: 4847-66. PMID 18326633 DOI: 10.1529/Biophysj.107.125823 |
0.465 |
|
2008 |
Peng X, Libich D, Janik R, Harauz G, Ladizhansky V. Dipolar chemical shift correlation spectroscopy for homonuclear carbon distance measurements in proteins in the solid state: application to structure determination and refinement. Journal of the American Chemical Society. 130: 359-69. PMID 18072776 DOI: 10.1021/Ja076658V |
0.36 |
|
2008 |
Polverini E, Rangaraj G, Libich DS, Boggs JM, Harauz G. Binding of the proline-rich segment of myelin basic protein to SH3 domains: spectroscopic, microarray, and modeling studies of ligand conformation and effects of posttranslational modifications. Biochemistry. 47: 267-82. PMID 18067320 DOI: 10.1021/Bi701336N |
0.418 |
|
2007 |
Libich DS, Monette MM, Robertson VJ, Harauz G. NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein. Biomolecular Nmr Assignments. 1: 61-3. PMID 19636827 DOI: 10.1007/S12104-007-9016-1 |
0.458 |
|
2007 |
Zhong L, Bamm VV, Ahmed MA, Harauz G, Ladizhansky V. Solid-state NMR spectroscopy of 18.5 kDa myelin basic protein reconstituted with lipid vesicles: spectroscopic characterisation and spectral assignments of solvent-exposed protein fragments. Biochimica Et Biophysica Acta. 1768: 3193-205. PMID 17920035 DOI: 10.1016/J.Bbamem.2007.08.013 |
0.473 |
|
2007 |
Ahmed MA, Bamm VV, Harauz G, Ladizhansky V. The BG21 isoform of Golli myelin basic protein is intrinsically disordered with a highly flexible amino-terminal domain. Biochemistry. 46: 9700-12. PMID 17676872 DOI: 10.1021/Bi700632X |
0.463 |
|
2007 |
Musse AA, Harauz G. Molecular "negativity" may underlie multiple sclerosis: role of the myelin basic protein family in the pathogenesis of MS. International Review of Neurobiology. 79: 149-72. PMID 17531841 DOI: 10.1016/S0074-7742(07)79007-4 |
0.463 |
|
2007 |
Bamm VV, Ahmed MA, Ladizhansky V, Harauz G. Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein. Journal of Neuroscience Research. 85: 272-84. PMID 17131428 DOI: 10.1002/Jnr.21129 |
0.459 |
|
2007 |
Debruin LS, Harauz G. White matter rafting--membrane microdomains in myelin. Neurochemical Research. 32: 213-28. PMID 17031566 DOI: 10.1007/S11064-006-9137-4 |
0.396 |
|
2007 |
Harauz G, Musse AA. A tale of two citrullines--structural and functional aspects of myelin basic protein deimination in health and disease. Neurochemical Research. 32: 137-58. PMID 16900293 DOI: 10.1007/S11064-006-9108-9 |
0.456 |
|
2006 |
DeBruin LS, Haines JD, Bienzle D, Harauz G. Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 84: 993-1005. PMID 17215885 DOI: 10.1139/o06-180 |
0.308 |
|
2006 |
Musse AA, Boggs JM, Harauz G. Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope. Proceedings of the National Academy of Sciences of the United States of America. 103: 4422-7. PMID 16537438 DOI: 10.1073/Pnas.0509158103 |
0.462 |
|
2006 |
Farès C, Libich DS, Harauz G. Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. The Febs Journal. 273: 601-14. PMID 16420483 DOI: 10.1111/J.1742-4658.2005.05093.X |
0.479 |
|
2005 |
Hill CM, Libich DS, Harauz G. Assembly of tubulin by classic myelin basic protein isoforms and regulation by post-translational modification. Biochemistry. 44: 16672-83. PMID 16342957 DOI: 10.1021/Bi050646+ |
0.453 |
|
2005 |
DeBruin LS, Haines JD, Wellhauser LA, Radeva G, Schonmann V, Bienzle D, Harauz G. Developmental partitioning of myelin basic protein into membrane microdomains Journal of Neuroscience Research. 80: 211-225. PMID 15772981 DOI: 10.1002/Jnr.20452 |
0.454 |
|
2005 |
Boggs JM, Rangaraj G, Hill CM, Bates IR, Heng YM, Harauz G. Effect of arginine loss in myelin basic protein, as occurs in its deiminated charge isoform, on mediation of actin polymerization and actin binding to a lipid membrane in vitro. Biochemistry. 44: 3524-34. PMID 15736962 DOI: 10.1021/Bi0473760 |
0.667 |
|
2005 |
Hill CM, Harauz G. Charge effects modulate actin assembly by classic myelin basic protein isoforms. Biochemical and Biophysical Research Communications. 329: 362-9. PMID 15721315 DOI: 10.1016/J.Bbrc.2005.01.151 |
0.425 |
|
2004 |
Polverini E, Boggs JM, Bates IR, Harauz G, Cavatorta P. Electron paramagnetic resonance spectroscopy and molecular modelling of the interaction of myelin basic protein (MBP) with calmodulin (CaM)-diversity and conformational adaptability of MBP CaM-targets. Journal of Structural Biology. 148: 353-69. PMID 15522783 DOI: 10.1016/J.Jsb.2004.08.004 |
0.668 |
|
2004 |
Libich DS, Robertson VJ, Monette MM, Harauz G. Backbone resonance assignments of the 18.5 kDa isoform of murine myelin basic protein (MBP). Journal of Biomolecular Nmr. 29: 545-6. PMID 15243191 DOI: 10.1023/B:Jnmr.0000034348.99658.D7 |
0.458 |
|
2004 |
Harauz G, Ishiyama N, Hill CM, Bates IR, Libich DS, Farès C. Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron (Oxford, England : 1993). 35: 503-42. PMID 15219899 DOI: 10.1016/J.Micron.2004.04.005 |
0.712 |
|
2004 |
Bates IR, Feix JB, Boggs JM, Harauz G. An immunodominant epitope of myelin basic protein is an amphipathic alpha-helix. The Journal of Biological Chemistry. 279: 5757-64. PMID 14630913 DOI: 10.1074/jbc.M311504200 |
0.639 |
|
2003 |
Nesper J, Hill CM, Paiment A, Harauz G, Beis K, Naismith JH, Whitfield C. Translocation of group 1 capsular polysaccharide in Escherichia coli serotype K30. Structural and functional analysis of the outer membrane lipoprotein Wza. The Journal of Biological Chemistry. 278: 49763-72. PMID 14522970 DOI: 10.1074/Jbc.M308775200 |
0.421 |
|
2003 |
Libich DS, Hill CM, Haines JD, Harauz G. Myelin basic protein has multiple calmodulin-binding sites. Biochemical and Biophysical Research Communications. 308: 313-9. PMID 12901870 DOI: 10.1016/S0006-291X(03)01380-9 |
0.409 |
|
2003 |
Bates IR, Harauz G. Molecular dynamics exposes alpha-helices in myelin basic protein. Journal of Molecular Modeling. 9: 290-7. PMID 12898292 DOI: 10.1007/S00894-003-0145-X |
0.672 |
|
2003 |
Libich DS, Hill CM, Bates IR, Hallett FR, Armstrong S, Siemiarczuk A, Harauz G. Interaction of the 18.5-kD isoform of myelin basic protein with Ca2+ -calmodulin: effects of deimination assessed by intrinsic Trp fluorescence spectroscopy, dynamic light scattering, and circular dichroism. Protein Science : a Publication of the Protein Society. 12: 1507-21. PMID 12824496 DOI: 10.1110/Ps.0303603 |
0.663 |
|
2003 |
Bates IR, Boggs JM, Feix JB, Harauz G. Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling. The Journal of Biological Chemistry. 278: 29041-7. PMID 12748174 DOI: 10.1074/Jbc.M302766200 |
0.685 |
|
2003 |
Hill CM, Haines JD, Antler CE, Bates IR, Libich DS, Harauz G. Terminal deletion mutants of myelin basic protein: new insights into self-association and phospholipid interactions. Micron (Oxford, England : 1993). 34: 25-37. PMID 12694855 DOI: 10.1016/S0968-4328(02)00058-6 |
0.722 |
|
2003 |
Kaur J, Libich DS, Campagnoni CW, Wood DD, Moscarello MA, Campagnoni AT, Harauz G. Expression and properties of the recombinant murine Golli-myelin basic protein isoform J37. Journal of Neuroscience Research. 71: 777-84. PMID 12605403 DOI: 10.1002/Jnr.10547 |
0.469 |
|
2002 |
Libich DS, Harauz G. Interactions of the 18.5 kDa isoform of myelin basic protein with Ca2+-calmodulin: in vitro studies using gel shift assays. Molecular and Cellular Biochemistry. 241: 45-52. PMID 12482024 DOI: 10.1023/A:1020883409176 |
0.416 |
|
2002 |
Hill CM, Bates IR, White GF, Hallett FR, Harauz G. Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and two-dimensional crystallization of myelin basic protein. Journal of Structural Biology. 139: 13-26. PMID 12372316 DOI: 10.1016/S1047-8477(02)00513-0 |
0.702 |
|
2002 |
Libich DS, Harauz G. Interactions of the 18.5-kDa isoform of myelin basic protein with Ca(2+)-calmodulin: in vitro studies using fluorescence microscopy and spectroscopy. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 80: 395-406. PMID 12234092 DOI: 10.1139/O02-020 |
0.4 |
|
2002 |
Wood DD, She YM, Freer AD, Harauz G, Moscarello MA. Primary structure of equine myelin basic protein by mass spectrometry. Archives of Biochemistry and Biophysics. 405: 137-46. PMID 12176067 DOI: 10.1016/S0003-9861(02)00340-5 |
0.378 |
|
2002 |
Bates IR, Libich DS, Wood DD, Moscarello MA, Harauz G. An Arg/Lys-->Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis. Protein Expression and Purification. 25: 330-41. PMID 12135568 DOI: 10.1016/S1046-5928(02)00017-7 |
0.693 |
|
2002 |
Ishiyama N, Hill CM, Bates IR, Harauz G. The formation of helical tubular vesicles by binary monolayers containing a nickel-chelating lipid and phosphoinositides in the presence of basic polypeptides. Chemistry and Physics of Lipids. 114: 103-11. PMID 11841829 DOI: 10.1016/S0009-3084(02)00002-6 |
0.705 |
|
2002 |
Hill C, Nesper J, Whitfield C, Harauz G. Electron Crystallography of the E. coli Outer Membrane Protein WzaK30 Microscopy and Microanalysis. 8: 836-837. DOI: 10.1017/S1431927602102534 |
0.369 |
|
2002 |
Hill CM, Bates IR, Antler CE, White GF, Hallett FR, Harauz G. Strategies to Optimize Order within Planar Arrays of Myelin Basic Protein for Electron Crystallography Microscopy and Microanalysis. 8: 834-835. DOI: 10.1017/S1431927602102522 |
0.662 |
|
2002 |
Bates IR, Libich DS, Wood DD, Moscarello MA, Harauz G. An Arg/Lys → Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis Protein Expression and Purification. 25: 330-341. DOI: 10.1016/S1046-5928(02)00017-7 |
0.658 |
|
2001 |
Ishiyama N, Bates IR, Hill CM, Wood DD, Matharu P, Viner NJ, Moscarello MA, Harauz G. The effects of deimination of myelin basic protein on structures formed by its interaction with phosphoinositide-containing lipid monolayers. Journal of Structural Biology. 136: 30-45. PMID 11858705 DOI: 10.1006/Jsbi.2001.4421 |
0.726 |
|
2001 |
Ridsdale RA, Palaniyar N, Possmayer F, Harauz G. Formation of folds and vesicles by dipalmitoylphosphatidylcholine monolayers spread in excess Journal of Membrane Biology. 180: 21-32. PMID 11284201 DOI: 10.1007/S002320010055 |
0.656 |
|
2000 |
Li W, Ottensmeyer FP, Harauz G. Quaternary organization of the Staphylothermus marinus phosphoenolpyruvate synthase: Angular reconstitution from cryoelectron micrographs with molecular modeling Journal of Structural Biology. 132: 226-240. PMID 11243891 DOI: 10.1006/Jsbi.2000.4322 |
0.666 |
|
2000 |
Bates IR, Matharu P, Ishiyama N, Rochon D, Wood DD, Polverini E, Moscarello MA, Viner NJ, Harauz G. Characterization of a recombinant murine 18.5-kDa myelin basic protein. Protein Expression and Purification. 20: 285-99. PMID 11049752 DOI: 10.1006/Prep.2000.1307 |
0.721 |
|
2000 |
Harauz G, Ishiyama N, Bates IR. Analogous structural motifs in myelin basic protein and in MARCKS. Molecular and Cellular Biochemistry. 209: 155-63. PMID 10942213 DOI: 10.1023/A:1007176216360 |
0.703 |
|
2000 |
Mac Millan SV, Ishiyama N, White GF, Palaniyar N, Hallett FR, Harauz G. Myelin basic protein component C1 in increasing concentrations can elicit fusion, aggregation, and fragmentation of myelin-like membranes European Journal of Cell Biology. 79: 327-335. PMID 10887963 DOI: 10.1078/S0171-9335(04)70036-9 |
0.662 |
|
2000 |
Palaniyar N, McCormack FX, Possmayer F, Harauz G. Three-dimensional structure of rat surfactant protein A trimers in association with phospholipid monolayers Biochemistry. 39: 6310-6316. PMID 10828943 DOI: 10.1021/Bi992793B |
0.691 |
|
2000 |
Pritzker LB, Joshi S, Harauz G, Moscarello MA. Deimination of myelin basic protein. 2. Effect of methylation of MBP on its deimination by peptidylarginine deiminase. Biochemistry. 39: 5382-8. PMID 10820009 DOI: 10.1021/Bi9925571 |
0.389 |
|
2000 |
Pritzker LB, Joshi S, Gowan JJ, Harauz G, Moscarello MA. Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Biochemistry. 39: 5374-81. PMID 10820008 DOI: 10.1021/Bi9925569 |
0.444 |
|
2000 |
Li W, Ottensmeyer FP, Harauz G. Angular reconstitution of the Staphylothermus marinus phosphoenolpyruvate synthase Microscopy Research and Technique. 49: 233-244. PMID 10816265 DOI: 10.1002/(Sici)1097-0029(20000501)49:3<233::Aid-Jemt3>3.0.Co;2-W |
0.595 |
|
2000 |
Beniac DR, Wood DD, Palaniyar N, Ottensmeyer FP, Moscarello MA, Harauz G. Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination. Journal of Structural Biology. 129: 80-95. PMID 10675299 DOI: 10.1006/Jsbi.1999.4200 |
0.775 |
|
2000 |
Ishiyama N, Matharu P, Bates IR, Wood DD, Moscarello MA, Viner NJ, Harauz G. Electron Microscopy of Myelin Basic Protein (MBP) Organized as Planar Arrays on a Lipid Monolayer Surface: Deimination of MBP Hinders Its Organizational Properties Microscopy and Microanalysis. 6: 250-251. DOI: 10.1017/S1431927600033742 |
0.433 |
|
1999 |
Beniac DR, Wood DD, Palaniyar N, Ottensmeyer FP, Moscarello MA, Harauz G. Marburg's variant of multiple sclerosis correlates with a less compact structure of myelin basic protein. Molecular Cell Biology Research Communications : McBrc. 1: 48-51. PMID 10329477 DOI: 10.1006/Mcbr.1999.0111 |
0.755 |
|
1999 |
Palaniyar N, Ridsdale RA, Hearn SA, Possmayer F, Harauz G. Formation of membrane lattice structures and their specific interactions with surfactant protein A American Journal of Physiology - Lung Cellular and Molecular Physiology. 276. PMID 10198362 DOI: 10.1152/Ajplung.1999.276.4.L642 |
0.672 |
|
1999 |
Palaniyar N, Ridsdale RA, Hearn SA, Heng YM, Ottensmeyer FP, Possmayer F, Harauz G. Filaments of surfactant protein A specifically interact with corrugated surfaces of phospholipid membranes American Journal of Physiology - Lung Cellular and Molecular Physiology. 276. PMID 10198361 DOI: 10.1152/Ajplung.1999.276.4.L631 |
0.75 |
|
1999 |
Ridsdale RA, Palaniyar N, Holterman CE, Inchley K, Possmayer F, Harauz G. Cation-mediated conformational variants of surfactant protein A Biochimica Et Biophysica Acta - Molecular Basis of Disease. 1453: 23-34. PMID 9989242 DOI: 10.1016/S0925-4439(98)00057-X |
0.636 |
|
1998 |
Palaniyar N, Semotok JL, Wood DD, Moscarello MA, Harauz G. Human proteolipid protein (PLP) mediates winding and adhesion of phospholipid membranes but prevents their fusion. Biochimica Et Biophysica Acta. 1415: 85-100. PMID 9858696 DOI: 10.1016/S0005-2736(98)00180-1 |
0.668 |
|
1998 |
Palaniyar N, Ridsdale RA, Holterman CE, Inchley K, Possmayer F, Harauz G. Structural changes of surfactant protein a induced by cations reorient the protein on lipid bilayers Journal of Structural Biology. 122: 297-310. PMID 9774534 DOI: 10.1006/Jsbi.1998.4004 |
0.67 |
|
1998 |
Palaniyar N, Ridsdale RA, Possmayer F, Harauz G. Surfactant protein A (SP-A) forms a novel supraquaternary structure in the form of fibers Biochemical and Biophysical Research Communications. 250: 131-136. PMID 9735345 DOI: 10.1006/Bbrc.1998.9284 |
0.641 |
|
1998 |
Harauz G, Li W. Three-dimensional cryoelectron microscopic reconstruction of the 2.25-MDa homomultimeric phosphoenolpyruvate synthase from Staphylothermus marinus. Biochemical and Biophysical Research Communications. 241: 599-605. PMID 9425318 DOI: 10.1006/Bbrc.1997.7851 |
0.365 |
|
1998 |
Ridsdale RA, Semotok JL, Larson DE, Rothblum LI, Harauz G. Topology of recombinant rat upstream binding factor Biochemistry and Cell Biology. 76: 649-655. DOI: 10.1139/Bcb-76-4-649 |
0.325 |
|
1998 |
Harauz G. Symmetry in the 2.25 MDa homomultimeric phosphoenolpyruvate synthase fromStaphylothermus marinus: Analyses of negatively stained preparations Micron. 29: 161-173. DOI: 10.1016/S0968-4328(97)00069-3 |
0.349 |
|
1997 |
Beniac DR, Czarnota GJ, Rutherford BL, Ottensmeyer FP, Harauz G. The in situ architecture of Escherichia coli ribosomal RNA derived by electron spectroscopic imaging and three-dimensional reconstruction. Journal of Microscopy. 188: 24-35. PMID 9369019 DOI: 10.1046/J.1365-2818.1997.2370795.X |
0.692 |
|
1997 |
Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G. Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis. The Journal of Biological Chemistry. 272: 4269-75. PMID 9020143 DOI: 10.1074/Jbc.272.7.4269 |
0.461 |
|
1997 |
Beniac DR, Luckevich MD, Czarnota GJ, Tompkins TA, Ridsdale RA, Ottensmeyer FP, Moscarello MA, Harauz G. Three-dimensional structure of myelin basic protein. I. Reconstruction via angular reconstitution of randomly oriented single particles. The Journal of Biological Chemistry. 272: 4261-8. PMID 9020142 DOI: 10.1074/Jbc.272.7.4261 |
0.748 |
|
1997 |
Beniac DR, Czarnota GJ, Rutherford BL, Ottensmeyer FP, Harauz G. Probing Ribosomal RNA By Electron Spectroscopic Imaging and Three-Dimensional Reconstruction Microscopy Today. 5: 10-11. DOI: 10.1017/S1551929500059940 |
0.635 |
|
1997 |
Beniac DR, Czarnota GJ, Rutherford BL, Ottensmeyer FP, Harauz G. Three-dimensional architecture of Thermomyces lanuginosus small subunit ribosomal RNA Micron. 28: 13-20. DOI: 10.1016/S0968-4328(97)00009-7 |
0.668 |
|
1996 |
Neil KJ, Ridsdale RA, Rutherford B, Taylor L, Larson DE, Glibetic M, Rothblum LI, Harauz G. Structure of recombinant rat UBF by electron image analysis and homology modelling. Nucleic Acids Research. 24: 1472-80. PMID 8628680 DOI: 10.1093/Nar/24.8.1472 |
0.402 |
|
1996 |
Beniac DR, Harauz G. Structures of small subunit ribosomal RNAs in situ from Escherichia coli and Thermomyces lanuginosus. Molecular and Cellular Biochemistry. 148: 165-81. PMID 8594421 DOI: 10.1007/Bf00928154 |
0.324 |
|
1995 |
Harauz G, Evans DH, Beniac DR, Arsenault AL, Rutherford B, Ottensmeyer FP. Electron spectroscopic imaging of encapsidated DNA in vaccinia virus Canadian Journal of Microbiology. 41: 889-894. PMID 8590404 DOI: 10.1139/M95-122 |
0.64 |
|
1995 |
Harauz G, Zuzan H, Kim PT, Holbrook JA. SECReT of the eukaryotic large ribosomal subunit. Biochemical and Biophysical Research Communications. 207: 848-51. PMID 7864880 DOI: 10.1006/Bbrc.1995.1263 |
0.324 |
|
1995 |
Harauz G, Beniac DR, Wu J, Zuzan H. Does the eukaryotic large ribosomal subunit have a channel passing through it? Biochemical and Biophysical Research Communications. 205: 1869-74. PMID 7811276 DOI: 10.1006/Bbrc.1994.2888 |
0.328 |
|
1995 |
Wu J, Beniac DR, Harauz G. Ribosomal proteins of Thermomyces lanuginosus--characterisation by two-dimensional gel electrophoresis and differential disassembly. Molecular and Cellular Biochemistry. 143: 21-34. PMID 7776955 DOI: 10.1007/Bf00925923 |
0.373 |
|
1994 |
Marcone MF, Beniac DR, Harauz G, Yada RY. Quaternary structure and model for the oligomeric seed globulin from Amaranthus hypochondriacus K343 Journal of Agricultural and Food Chemistry. 42: 2675-2678. DOI: 10.1021/Jf00048A005 |
0.326 |
|
1993 |
Kyle KM, Harauz G. Electron microscopic visualisation of the 5S rRNA-YL3 complex from Saccharomyces cerevisiae. Molecular and Cellular Biochemistry. 117: 11-21. PMID 1480161 DOI: 10.1007/Bf00230406 |
0.334 |
|
1993 |
Beniac DR, Harauz G. Visualisation of E. coli ribosomal RNA in situ by electron spectroscopic imaging and image analysis Micron. 24: 163-171. DOI: 10.1016/0968-4328(93)90069-D |
0.321 |
|
1993 |
Chiu DK, Harauz G. A method for inferring probabilistic consensus structure with applications to molecular sequence data Pattern Recognition. 26: 643-654. DOI: 10.1016/0031-3203(93)90117-F |
0.304 |
|
1992 |
Harauz G, Flannigan D. Characteristic electron microscopical projections of the small ribosomal subunit from Thermomyces lanuginosus. Biochimica Et Biophysica Acta. 1130: 289-96. PMID 1562605 DOI: 10.1016/0167-4781(92)90441-2 |
0.311 |
|
1992 |
Harauz G. Electron microscopical projections of the large ribosomal subunit from Thermomyces lanuginosus. Biochimica Et Biophysica Acta. 1132: 58-66. PMID 1511012 DOI: 10.1016/0167-4781(92)90052-2 |
0.335 |
|
1992 |
Harauz G, Letvenuk L, Flannigan D. Electron image analysis of ribosomal subunits from Thermus aquaticus. Biochimica Et Biophysica Acta. 1129: 207-14. PMID 1370377 DOI: 10.1016/0167-4781(92)90489-M |
0.314 |
|
1992 |
Kyle KM, Harauz G. Structures of ribosomal subunits from Saccharomyces cerevisiae Micron and Microscopica Acta. 23: 273-286. DOI: 10.1016/0739-6260(92)90030-H |
0.338 |
|
1990 |
Harauz G, Flannigan D. Structure of ribosomes from Thermomyces lanuginosus by electron microscopy and image processing. Biochimica Et Biophysica Acta. 1038: 260-7. PMID 2184898 DOI: 10.1016/0167-4838(90)90214-Z |
0.349 |
|
1988 |
Harauz G, Boekema E, Van Heel M. Statistical image analysis of electron micrographs of ribosomal subunits Methods in Enzymology. 164: 35-49. PMID 3241550 DOI: 10.1016/S0076-6879(88)64033-X |
0.584 |
|
1988 |
Borland L, Harauz G, Bahr G, van Heel M. Packing of the 30 nm chromatin fiber in the human metaphase chromosome Chromosoma. 97: 159-163. PMID 3229179 DOI: 10.1007/BF00327373 |
0.544 |
|
1988 |
Harauz G. Pattern Recognition and Artificial Intelligence in Molecular Biology Machine Intelligence and Pattern Recognition. 7: 437-447. DOI: 10.1016/B978-0-444-87137-4.50036-9 |
0.306 |
|
1987 |
Harauz G, Borland L, Bahr GF, Zeitler E, van Heel M. Three-dimensional reconstruction of a human metaphase chromosome from electron micrographs. Chromosoma. 95: 366-74. PMID 3652820 DOI: 10.1007/BF00293184 |
0.554 |
|
1984 |
Harauz G, Ottensmeyer FP. Nucleosome reconstruction via phosphorus mapping Science. 226: 936-940. PMID 6505674 DOI: 10.1126/science.6505674 |
0.577 |
|
1983 |
Harauz G, Ottensmeyer FP. Interpolation in computing forward projections in direct three-dimensional reconstruction Physics in Medicine and Biology. 28: 1419-1427. PMID 6665035 DOI: 10.1088/0031-9155/28/12/007 |
0.545 |
|
1983 |
Harauz G, Andrews DW, Ottensmeyer FP. Electron microscopic visualization of the sidechains of the poly-L-lysine alpha helix. Ultramicroscopy. 12: 59-64. PMID 6659150 DOI: 10.1016/0304-3991(83)90305-4 |
0.541 |
|
1983 |
Harauz G, Ottensmeyer FP. Direct three-dimensional reconstruction for macromolecular complexes from electron micrographs Ultramicroscopy. 12: 309-319. DOI: 10.1016/0304-3991(83)90245-0 |
0.543 |
|
Show low-probability matches. |