Jan Pieter Abrahams

Current Project

Electron Diffraction of Nanocrystals

Research

The laboratory of Jan Pieter Abrahams, University of Basel, is employing high-resolution electron microscopy to study the structure of 3D nanocrystals.

Biography

Leiden Cambridge Leiden Basel PSI

Publications

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Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.

Tiiman A, Luo J, Wallin C, Olsson L, Lindgren J, Jarvet J, Per R, Sholts SB, Rahimipour S, Abrahams, J., Karlström AE, Gräslund A, Wärmländer SK

J Alzheimers Dis. 54(3), 971-982 (2016)

DOI: 10.3233/JAD-160427

116

Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer's disease.

Wallin C, Kulkarni Y, Abelein A, Jarvet J, Liao Q, Strodel B, Olsson L, Luo J, Abrahams, J., Sholts S, Roos P, Kamerlin S, Gräslund A, Wärmländer S

J Trace Elem Med Biol. 2016 Dec(38), 183-193 (2016)

PubMed

DOI: 10.1016/j.jtemb.2016.03.009

114

A posteriori correction of camera characteristics from large image data sets

Afanasyev, P., Ravelli, R. B. G., Matadeen, R., De Carlo, S., van Duinen, G., Alewijnse, B., Peters, P. J., Abrahams, J., Portugal, R. V., Schatz, M., van Heel, M.

Scientific Reports 5, (2015)

DOI: DOI

110

Non-chaperone proteins can inhibit aggregation and cytotoxicity of Alzheimer amyloid beta peptide

Luo, J., Warmlander, S. K., Graslund, A., Abrahams, J.

J Biol Chem 289(40), 27766-75 (2014)

PubMed

109

Alzheimer peptides aggregate into transient nanoglobules that nucleate fibrils

Luo, J., Warmlander, S. K., Graslund, A., Abrahams, J.

Biochemistry 53(40), 6302-8 (2014)

PubMed

108

The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes

Luo, J. H., Warmlander, S. K. , Yu, C. H., Muhammad, K., Graslund, A., Abrahams, J.

Nanoscale 6(12), 6720-6726 (2014)

PubMed

107

Cyclic peptides as inhibitors of amyloid fibrillation

Luo, J., Abrahams, J.

Chemistry 20(9), 2410-9 (2014)

PubMed

106

The hairpin conformation of the amyloid beta peptide is an important structural motif along the aggregation pathway

Abelein, A., Abrahams, J., Danielsson, J., Graslund, A., Jarvet, J., Luo, J. H., Tiiman, A., Warmlander, S. K.

J Biol Inorg Chem 19(42099), 623-634 (2014)

PubMed

105

Endogenous polyamines reduce the toxicity of soluble abeta peptide aggregates associated with Alzheimer's disease

Luo, J., Mohammed, I., Warmlander, S. K., Hiruma, Y., Graslund, A., Abrahams, J.

Biomacromolecules 15(6), 1985-91 (2014)

PubMed

104

Capture of unstable protein complex on the streptavidin-coated single-walled carbon nanotubes

Liu, Z. F., Voskamp, P., Zhang, Y., Chu, F. Q., Abrahams, J.

J Nanopart Res 15(4), (2013)

DOI: DOI

101

Cellular polyamines promote amyloid-beta (Abeta) peptide fibrillation and modulate the aggregation pathways

Luo, J., Yu, C. H., Yu, H., Borstnar, R., Kamerlin, S. C., Graslund, A., Abrahams, J., Warmlander, S. K.

ACS Chem Neurosci 4(3), 454-62 (2013)

PubMed

100

Imaging protein three-dimensional nanocrystals with cryo-EM

Nederlof, I., Li, Y. W., van Heel, M., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 69(Pt 5), 852-9 (2013)

PubMed

98

Visualizing the localization of transfection complexes during graphene nanoparticle-based transfection

ten Bruggencate, F., Laroche, F., Zhang, Y., Song, G. Q., Yin, S. G., Abrahams, J., Liu, Z. F.

J Mater Chem B 1(46), 6353-6358 (2013)

DOI: DOI

97

Inhibiting and reversing amyloid-beta peptide (1-40) fibril formation with gramicidin S and engineered analogues

Luo, J., Otero, J. M., Yu, C. H., Warmlander, S. K., Graslund, A., Overhand, M., Abrahams, J.

Chemistry 19(51), 17338-48 (2013)

PubMed

96

Single-walled carbon nanotubes as scaffolds to concentrate DNA for the study of DNA-protein interactions

Liu, Z. F., Galli, F., Waterreus, W. J., Meulenbroek, E., Koning, R. I., Lamers, G. E. M., Olsthoorn, R. C. L., Pannu, N., Oosterkamp, T. H., Koster, A. J., Dame, R. T., Abrahams, J.

Chemphyschem 13(6), 1569-1575 (2012)

PubMed

95

Characterisation of a counting imaging detector for electron detection in the energy range 10-20 keV

Moldovan, G., Sikharulidze, I., Matheson, J., Derbyshire, G., Kirkland, A. I., Abrahams, J.

Nucl Instrum Meth A 681, 21-24 (2012)

DOI: DOI

94

Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato

Meulenbroek, E. M., Thomassen, E. A. J., Pouvreau, L., Abrahams, J., Gruppen, H., Pannu, N. S.

Acta Crystallogr D Biol Crystallogr 68, 794-799 (2012)

PubMed

93

Ultra-small graphene oxide functionalized with polyethylenimine (PEI) for very efficient gene delivery in cell and zebrafish embryos

Zhou, X., Laroche, F., Lamers, G. E. M., Torraca, V., Voskamp, P., Lu, T., Chu, F. Q., Spaink, H. P., Abrahams, J., Liu, Z. F.

Nano Research 5(10), 703-709 (2012)

DOI: DOI

92

4D Biology for health and disease workshop report

Abrahams, J., Apweiler, R., Balling, R., Bertero, M. G., Bujnicki, J. M., Chayen, N. E., Chene, P., Corthals, G. L., Dylag, T., Forster, F., Heck, A. J., Henderson, P. J., Herwig, R., Jehenson, P., Kokalj, S. J., Laue, E., Legrain, P., Martens, L., Migliorini, C., Musacchio, A., Podob

N Biotechnol 28(4), 291-3 (2011)

PubMed

91

A straightforward and robust method for introducing human hair as a nucleant into high throughput crystallization trials

Nederlof, I., Hosseini, R., Georgieva, D., Luo, J. H., Li, D. F., Abrahams, J.

Crystal Growth & Design 11(4), 1170-1176 (2011)

DOI: DOI

90

Recent advances in the CRANK software suite for experimental phasing

Pannu, N. S., Waterreus, W. J., Skubak, P., Sikharulidze, I., Abrahams, J., de Graaff, R. A. G.

Acta Crystallogr D Biol Crystallogr 67, 331-337 (2011)

DOI: DOI

89

Evaluation of Medipix2 detector for recording electron diffraction data in low dose conditions

Georgieva, D., Jansen, J., Sikharulidze, I., Jiang, L., Zandbergen, H. W., Abrahams, J.

J Instrum 6, (2011)

DOI: DOI

87

Image processing and lattice determination for three-dimensional nanocrystals

Jiang, L., Georgieva, D., Nederlof, I., Liu, Z., Abrahams, J.

Microsc Microanal 17(6), 879-85 (2011)

PubMed

86

Low energy electron microscopy imaging using Medipix2 detector

Sikharulidze, I., van Gastel, R., Schramm, S., Abrahams, J., Poelsema, B., Tromp, R. M., van der Molen, S. J.

Nucl Instrum Meth A 633, S239-S242 (2011)

DOI: DOI

85

A graphene oxide center dot streptavidin complex for biorecognition - towards affinity purification

Liu, Z. F., Jiang, L. H., Galli, F., Nederlof, I., Olsthoorn, R. C. L., Lamers, G. E. M., Oosterkamp, T. H., Abrahams, J.

Adv Funct Mater 20(17), 2857-2865 (2010)

DOI: DOI

84

A novel approximation method of CTF amplitude correction for 3D single particle reconstruction

Jiang, L. H., Liu, Z. F., Georgieva, D., Kuil, M. E., Abrahams, J.

Ultramicroscopy 110(4), 350-358 (2010)

PubMed

83

Stable single-walled carbon nanotube-streptavidin complex for biorecognition

Liu, Z. F., Galli, F., Janssen, K. G. H., Jiang, L. H., van der Linden, H. J., de Geus, D. C., Voskamp, P., Kuil, M. E., Olsthoorn, R. C. L., Oosterkamp, T. H., Hankemeier, T., Abrahams, J.

J Phys Chem C 114(10), 4345-4352 (2010)

82

An intelligent peak search program for digital electron diffraction images of 3D nano-crystals

Jiang, L. H., Georgieva, D., IJspeert, K., Abrahams, J.

NMR Analysis , (2009)

80

Recycling of aborted ribosomal 50S subunit-nascent chain-tRNA complexes by the heat shock protein Hsp15

Jiang, L., Schaffitzel, C., Bingel-Erlenmeyer, R., Ban, N., Korber, P., Koning, R. I., de Geus, D. C., Plaisier, J. R., Abrahams, J.

J Mol Biol 386(5), 1357-67 (2009)

PubMed

79

An intelligent peak search program for digital electron diffraction images of 3D nano-crystals

Jiang, L. H., Georgieva, D., IJspeert, K., Abrahams, J.

Proceedings of the 2009 2nd International Congress on Image and Signal Processing, Vols 1-9 , 468-472 (2009)

DOI: DOI

78

Characterization of a diagnostic Fab fragment binding trimeric Lewis X

de Geus, D. C., van Roon, A. M. M., Thomassen, E. A. J., Hokke, C. H., Deelder, A. M., Abrahams, J.

Proteins 76(2), 439-447 (2009)

PubMed

77

Crystal structure of chlorite dismutase, a detoxifying enzyme producing molecular oxygen

de Geus, D. C., Thomassen, E. A. J., Hagedoorn, P. L., Pannu, N. S., van Duijn, E., Abrahams, J.

J Mol Biol 387(1), 192-206 (2009)

PubMed

76

The Max-Inf2/Lorentz Center workshop on New algorithms in macromolecular crystallography and electron microscopy

Pannu, N. S., Ravelli, R. B., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 65(Pt 7), 623-4 (2009)

PubMed

75

Unit-cell determination from randomly oriented electron-diffraction patterns

Jiang, L., Georgieva, D., Zandbergen, H. W., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 65(Pt 7), 625-32 (2009)

PubMed

74

Involvement of a carboxylated lysine in UV damage endonuclease

Meulenbroek, E. M., Paspaleva, K., Thomassen, E. A. J., Abrahams, J., Goosen, N., Pannu, N. S.

Protein Sci 18(3), 549-558 (2009)

PubMed

73

Mammalian Navigators are microtubule plus-end tracking proteins that can reorganize the cytoskeleton to induce neurite-like extensions

van Haren, J., Draegestein, K., Keijzer, N., Abrahams, J., Grosveld, F., Peeters, P. J., Moechars, D., Galjart, N.

Cell Motil Cytoskeleton 66(10), 824-38 (2009)

PubMed

72

Medipix 2 detector applied to low energy electron microscopy

van Gastel, R., Sikharulidze, I., Schramm, S., Abrahams, J., Poelsema, B., Tromp, R. M., van der Molen, S. J.

Ultramicroscopy 110(1), 33-5 (2009)

PubMed

71

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of chlorite dismutase: a detoxifying enzyme producing molecular oxygen

de Geus, D. C., Thomassen, E. A. J., van der Feltz, C. L., Abrahams, J.

Acta Crystallogr Sect F Struct Biol Cryst Commun 64, 730-732 (2008)

PubMed

70

Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts

Zovko, S., Abrahams, J., Koster, A. J., Galjart, N., Mommaas, A. M.

Mol Biol Cell 19(7), 3138-46 (2008)

PubMed

69

Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease

Paspaleva, K., Thomassen, E., Pannu, N. S., Lwai, S., Moolenaar, G. F., Goosen, N., Abrahams, J.

Structure 15(10), 1316-1324 (2007)

PubMed

DOI: DOI

68

Cyclops: new modular software suite for cryo-EM

Plaisier, J. R., Jiang, L., Abrahams, J.

J Struct Biol 157(1), 19-27 (2007)

PubMed

67

Heterogeneous nucleation of three-dimensional protein nanocrystals

Georgieva, D. G., Kuil, M. E., Oosterkamp, T. H., Zandbergen, H. W., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 63(Pt 5), 564-70 (2007)

PubMed

66

Malingering on the Social Security disability consultative exam: a new rating scale

Chafetz, M. D., Abrahams, J., Kohlmaier, J.

Arch Clin Neuropsychol 22(1), 42018 (2007)

PubMed

65

Nano-dispensing by electrospray for biotechnology

Kuil, M. E., Abrahams, J., Marijnissen, J. C.

Biotechnol J 1(9), 969-75 (2006)

PubMed

64

Structure of the E-coli signal recognition particle bound to a translating ribosome

Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J., Koerten, H. K., Koning, R. I., Ban, N.

Nature 444(7118), 503-506 (2006)

PubMed

63

The impact of single amino acid substitutions in CD3 gamma on the CD3 epsilon gamma interaction and T-cell receptor-CD3 complex formation

Thomassen, E. A. J., Dekking, E. H. A., Thompson, A., Franken, K. L., Sanal, O., Abrahams, J., van Tol, M. J. D., Koning, F.

Hum Immunol 67(8), 579-588 (2006)

PubMed

62

Relevance of apoptin's integrity for its functional behavior

Rohn, J. L., Zhang, Y. H., Leliveld, S. R., Danen-van Oorschot, A. A. A. M., Henriquez, N. V., Abrahams, J., Noteborn, M. H. M.

J Virol 79(2), 1337-1338 (2005)

PubMed

DOI: DOI

61

The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin

Thomassen, E. A. J., van Veen, H. A., van Berkel, P. H. C., Nuijens, J. H., Abrahams, J.

Transgenic Research 14(4), 397-405 (2005)

PubMed

60

FCS in non-ideal solutions

Schmauder, R., van Rijn, R., Abrahams, J., Kuil, M. E., Schmidt, T.

Biophys J 88(1), 655A-655A (2005)

59

Apoptin's functional N- and C-termini independently bind DNA

Leliveld, S. R., Dame, R. T., Rohn, J. L., Noteborn, M. H. M., Abrahams, J.

FEBS Lett 557(42007), 155-158 (2004)

PubMed

58

Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen

van Roon, A. M., Pannu, N. S., de Vrind, J. P., van der Marel, G. A., van Boom, J. H., Hokke, C. H., Deelder, A. M., Abrahams, J.

Structure 12(7), 1227-36 (2004)

PubMed

57

CRANK: new methods for automated macromolecular crystal structure solution

Ness, S. R., de Graaff, R. A., Abrahams, J., Pannu, N. S.

Structure 12(10), 1753-61 (2004)

PubMed

56

Crystal structure of an empty capsid of turnip yellow mosaic virus

van Roon, A. M., Bink, H. H., Plaisier, J. R., Pleij, C. W., Abrahams, J., Pannu, N. S.

J Mol Biol 341(5), 1205-14 (2004)

PubMed

55

Crystallization and preliminary X-ray crystallographic studies on a Kunitz-type potato serine protease inhibitor

Thomassen, E. A. J., Pouvreau, L., Gruppen, H., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 60, 1464-1466 (2004)

PubMed

54

Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor

Bos, I. G. A., Lubbers, Y. T. P., Eldering, E., Abrahams, J., Hack, C. E.

Biochim Biophys Acta-Proteins Proteom 1699(42006), 139-144 (2004)

PubMed

53

TYSON: robust searching, sorting, and selecting of single particles in electron micrographs

Plaisier, J. R., Koning, R. I., Koerten, H. K., van Heel, M., Abrahams, J.

J Struct Biol 145(42006), 76-83 (2004)

PubMed

52

Prevalent conformations and subunit exchange in the biologically active apoptin protein multimer

Leliveld, S. R., Noteborn, M. H. M., Abrahams, J.

Eur J Biochem 270(17), 3619-3627 (2003)

PubMed

51

Recombinant Apoptin multimers kill tumor cells but are nontoxic and epitope-shielded in a normal-cell-specific fashion

Zhang, Y. H., Leliveld, S. R., Kooistra, K., Molenaar, C., Rohn, J. L., Tanke, H. J., Abrahams, J., Noteborn, M. H. M.

Exp Cell Res 289(1), 36-46 (2003)

PubMed

50

Apoptin induces tumor-specific apoptosis as a globular multimer

Leliveld, S. R., Zhang, Y. H., Rohn, J. L., Noteborn, M. H. M., Abrahams, J.

J Biol Chem 278(11), 9042-9051 (2003)

PubMed

49

Apoptin protein multimers form distinct higher-order nucleoprotein complexes with DNA

Leliveld, S. R., Dame, R. T., Mommaas, M. A., Koerten, H. K., Wyman, C., Danen-van Oorschot, A. A. A. M., Rohn, J. L., Noteborn, M. H. M., Abrahams, J.

Nucleic Acids Res 31(16), 4805-4813 (2003)

PubMed

48

Area detectors in structural biology

Plaisier, J. R., Koning, R. I., Koerten, H. K., van Roon, A. M., Thomassen, E. A. J., Kuil, M. E., Hendrix, J., Broennimann, C., Pannu, N. S., Abrahams, J.

Nucl Instrum Meth A 509(42007), 274-282 (2003)

DOI: DOI

47

ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase

Hilge, M., Siegal, G., Vuister, G. W., Guntert, P., Gloor, S. M., Abrahams, J.

Nat Struct Biol 10(6), 468-74 (2003)

PubMed

46

Structure of beta-antithrombin and the effect of glycosylation on antithrombin's heparin affinity and activity

McCoy, A. J., Pei, X. Y., Skinner, R., Abrahams, J., Carrell, R. W.

J Mol Biol 326(3), 823-33 (2003)

PubMed

45

Crystallization and preliminary X-ray analysis of an anti-LewisX Fab fragment with and without its LewisX antigen

van Roon, A. M. M., Pannu, N. S., Hokke, C. H., Deelder, A. M., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 59, 1306-1309 (2003)

PubMed

44

The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant

Bos, I. G. A., Lubbers, Y. T. P., Roem, D., Abrahams, J., Hack, C. E., Eldering, E.

J Biol Chem 278(32), 29463-29470 (2003)

PubMed

43

The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold

Thomassen, E., Gielen, G., Schutz, M., Schoehn, G., Abrahams, J., Miller, S., van Raaij, M. J.

J Mol Biol 331(2), 361-73 (2003)

PubMed

42

Visualization by cryo-electron microscopy of genomic RNA that binds to the protein capsid inside bacteriophage MS2

Koning, R., van den Worm, S., Plaisier, J. R., van Duin, J., Abrahams, J., Koerten, H.

J Mol Biol 332(2), 415-422 (2003)

PubMed

41

Importance of nuclear localization of apoptin for tumor-specific induction of apoptosis

Danen-van Oorschot, A. A. A. M., Zhang, Y. H., Leliveld, S. R., Rohn, J. L., Seelen, M. C. M. J., Bolk, M. W., van Zon, A., Erkeland, S. J., Abrahams, J., Mumberg, D., Noteborn, M. H. M.

J Biol Chem 278(30), 27729-27736 (2003)

PubMed

40

Mechanism of thrombin's enigmatic sodium switch revealed

Abrahams, J., Thomassen, E. A. J.

Structure 11(4), 363-364 (2003)

PubMed

38

A novel pH-dependent dimerization motif in beta-lactoglobulin from pig (Sus scrofa)

Hoedemaeker, F. J., Visschers, R. W., Alting, A. C., de Kruif, K. G., Kuil, M. E., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 58(Pt 3), 480-6 (2002)

PubMed

37

Protein nano-crystallogenesis

Kuil, M. E., Bodenstaff, E. R., Hoedemaeker, F. J., Abrahams, J.

Enzyme Microb Technol 30(3), 262-5 (2002)

PubMed

36

Screening crystallisation conditions using fluorescence correlation spectroscopy

Schmauder, R., Schmidt, T., Abrahams, J., Kuil, M. E.

Acta Crystallogr D Biol Crystallogr 58(Pt 10 Pt 1), 1536-41 (2002)

PubMed

35

Structural and functional aspects of C1-Inhibitor

Bos, I. G. A., Hack, C. E., Abrahams, J.

Immunobiology 205(42099), 518-533 (2002)

PubMed

34

The prospects of protein nanocrystallography

Bodenstaff, E. R., Hoedemaeker, F. J., Kuil, M. E., de Vrind, H. P. M., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 58, 1901-1906 (2002)

PubMed

33

Structure elucidation of beta-mannanase: from the electron-density map to the DNA sequence

Hilge, M., Perrakis, A., Abrahams, J., Winterhalter, K., Piontek, K., Gloor, S. M.

Acta Crystallogr D Biol Crystallogr 57(Pt 1), 37-43 (2001)

PubMed

32

Matrix methods for solving protein substructures of chlorine and sulfur from anomalous data

de Graaff, R. A. G., Hilge, M., van der Plas, J. L., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 57, 1857-1862 (2001)

PubMed

31

Crystal structure of wildtype alpha(1)-antitrypsin

Elliott, P. R., Abrahams, J., Lomas, D. A.

American Journal of Respiratory and Critical Care Medicine 159(3), A192-A192 (1999)

28

New developments in phase refinement

Abrahams, J., De Graaff, R. A. G.

Current Opin Struct Biol 8(5), 601-605 (1998)

PubMed

27

Implications for function and therapy of a 2.9 angstrom structure of binary-complexed antithrombin

Skinner, R., Chang, W. S. W., Jin, L., Pei, X., Huntington, J. A., Abrahams, J., Carrell, R. W., Lomas, D. A.

J Mol Biol 283(1), 42261 (1998)

26

Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation

Elliott, P. R., Abrahams, J., Lomas, D. A.

J Mol Biol 275(3), 419-25 (1998)

PubMed

25

Structural mobility of antithrombin and its modulation by heparin

Carrell, R., Skinner, R., Jin, L., Abrahams, J.

Thromb Haemost 78(1), 516-9 (1997)

PubMed

23

The 2.6 Angstrom structure of antithrombin indicates a conformational change at the heparin binding site

Skinner, R., Abrahams, J., Whisstock, J. C., Lesk, A. M., Carrell, R. W., Wardell, M. R.

J Mol Biol 266(3), 601-609 (1997)

PubMed

22

The anticoagulant activation of antithrombin by heparin

Jin, L., Abrahams, J., Skinner, R., Petitou, M., Pike, R. N., Carrell, R. W.

Proc Natl Acad Sci U S A 94(26), 14683-8 (1997)

PubMed

21

The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F-1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer

Shirakihara, Y., Leslie, A. G. W., Abrahams, J., Walker, J. E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y., Yoshida, M.

Structure 5(6), 825-836 (1997)

PubMed

20

Improved diffraction of antithrombin crystals grown in microgravity

Wardell, M. R., Skinner, R., Carter, D. C., Twigg, P. D., Abrahams, J.

Acta Crystallogr D Biol Crystallogr 53(Pt 5), 622-5 (1997)

PubMed

19

The structure of bovine F-1-ATPase complexed with the antibiotic inhibitor aurovertin B

vanRaaij, M. J., Abrahams, J., Leslie, A. G. W., Walker, J. E.

Proc Natl Acad Sci U S A 93(14), 6913-6917 (1996)

PubMed

18

The structure of bovine mitochondrial F1-ATPase - An insight into ATP synthesis

Abrahams, J., Leslie, A. G. W., Lutter, R., Walker, J. E.

Biophys J 70(2), Mams3-Mams3 (1996)

17

Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

Elliott, P. R., Lomas, D. A., Carrell, R. W., Abrahams, J.

Nat Struct Biol 3(8), 676-81 (1996)

PubMed

16

Methods used in the structure determination of bovine mitochondrial F-1 ATPase

Abrahams, J., Leslie, A. G. W.

Acta Crystallogr D Biol Crystallogr 52, 30-42 (1996)

PubMed

15

Structure at 2.8-Å resolution of F1-ATPase from bovine heart mitochondria

Abrahams, J., Leslie, A. G. W., Lutter, R., Walker, J. E.

Nature 370(6491), 621-628 (1994)

PubMed

14

Crystallization and preliminary-X-ray diffraction analysis of 2 conformations of intact human antithrombin

Wardell, M. R., Abrahams, J., Bruce, D., Skinner, R., Leslie, A. G. W.

J Mol Biol 234(4), 1253-1258 (1993)

PubMed

13

Crystallization of F(1)-Atpase from bovine heart-mitochondria

Lutter, R., Abrahams, J., Vanraaij, M. J., Todd, R. J., Lundqvist, T., Buchanan, S. K., Leslie, A. G. W., Walker, J. E.

J Mol Biol 229(3), 787-790 (1993)

PubMed

12

Inherent asymmetry of the structure of F1-atpase from bovine Heart-Mitochondria at 6.5 Angstrom resolution

Abrahams, J., Lutter, R., Todd, R. J., Vanraaij, M. J., Leslie, A. G. W., Walker, J. E.

EMBO J. 12(5), 1775-1780 (1993)

PubMed

11

The influence of tRNA located at the P-site on the turnover of EF-Tu.GTP on ribosomes

Abrahams, J., Acampo, J. J. C., Kraal, B., Bosch, L.

Biochimie 73(42193), 1089-1092 (1991)

PubMed

10

Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA

Abrahams, J., Kraal, B., Clark, B. F. C., Bosch, L.

Nucleic Acids Res 19(3), 553-557 (1991)

PubMed

9

Kirromycin drastically reduces the affinity of Escherichia-Coli elongation-factor Tu for aminoacyl-tRNA

Abrahams, J., van Raaij, M. J., Ott, G., Kraal, B., Bosch, L.

Biochemistry 30(27), 6705-6710 (1991)

PubMed

8

Prediction of RNA secondary structure, including pseudoknotting, by computer-simulation

Abrahams, J., Vandenberg, M., Vanbatenburg, E., Pleij, C.

Nucleic Acids Research 18(10), 3035-3044 (1990)

PubMed

7

The interaction between aminoacyl-tRNA and the mutant elongation factor Tu AR and BO

Abrahams, J., Acampo, J. J. C., Ott, G., Sprinzl, M., Degraaf, J. M., Talens, A., Kraal, B.

Biochim Biophys Acta 1050(42007), 226-229 (1990)

PubMed

6

The spatial folding of the 3' noncoding region of aminoacylatable Plant viral RNAs

Pleij, C. W. A., Abrahams, J., Vanbelkum, A., Rietveld, K., Bosch, L.

J Cellular Biochem , 274-274 (1986)

3

5 pseudoknots are present at the 204 nucleotides long 3' noncoding region of tobacco mosaic virus RNA

Vanbelkum, A., Abrahams, J., Pleij, C. W. A., Bosch, L.

Nucleic Acids Research 13(21), 7673-7686 (1985)

2

Qualitative differences in vocabulary performance of Alzheimer versus depressed patients

Houlihan, J. P., Abrahams, J., LaRue, A. A., Jarvik, L. F.

Developmental Neuropsychology 1(2), 139-144 (1985)

DOI: DOI

1

Professor

+41 61 387 32 17

C-CINA, Biozentrum, Universität Basel, Mattenstrasse 20, Room P.24, CH-4058 Basel, Switzerland

jp.abrahams@unibas.ch