Autoren-Indexdatei meiner TSE-Literatur-Datenbank

File of the authors index for my TSE-Literature-Collection

Baskakov,I.V.

AUGL - Anderson,M.; Bocharova,O.V.; Makarava,N.; Breydo,L.; Salnikov,V.V.; Baskakov,I.V. - Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. - Journal of Molecular Biology 2006 Apr 28; 358(2): 580-96

AYAD - Baskakov,I.V. - Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils - The FEBS Journal 2007 Aug; 274(15): 3756-65

AYAE - Baskakov,I.V.; Breydo,L. - Converting the prion protein: what makes the protein infectious. - Biochimica et Biophysica Acta - Molecular Basis of Disease 2007 Jun; 1772(6): 692-703

AWTX - Baskakov,I.V. - The reconstitution of mammalian prion infectivity de novo - The FEBS Journal 2007 Feb; 274(3): 576-87

AVHD - Baskakov,I.V.; Breydo,L. - Converting the prion protein: What makes the protein infectious. - Biochimica et Biophysica Acta 2006 Jul 25

ASIN - Baskakov,I.V.; Disterer,P.; Breydo,L.; Shaw,M.; Gill,A.; James,W.; Tahiri-Alaoui,A. - The presence of valine at residue 129 in human prion protein accelerates amyloid formation - FEBS Letters 2005 May 9; 579(12): 2589-96

ARNS - Baskakov,I.V.; Bocharova,O.V. - In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features - Biochemistry 2005 Feb 22; 44(7): 2339-48

AQGS - Baskakov,I.V.; Legname,G.; Gryczynski,Z.; Prusiner,S.B. - The peculiar nature of unfolding of the human prion protein - Protein Science 2004 Mar; 13(3): 586-95

AQGT - Baskakov,I.V. - Autocatalytic conversion of recombinant prion proteins displays a species barrier - The Journal of Biological Chemistry 2004 Feb 27; 279(9): 7671-7

APQJ - Baskakov,I.V. - Autocatalytic conversion of recombinant prion proteins discplays a species barrier - The Journal of Biological Chemistry 2003 Dec 10

AOQD - Baskakov,I.V. - In vitro conversion of recombinant prion protein into a fibrillar form displays species-specificity - International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - BR-105

ABAX - Baskakov,I.V.; Legname,G.; Baldwin,M.A.; Prusiner,S.B.; Cohen,F.E. - Pathway complexity of prion protein assembly into amyloid - The Journal of Biological Chemistry 2002 Jun 14; 277(24): 21140-8

ABAY - Baskakov,I.V.; Legname,G.; Prusiner,S.B.; Cohen,F.E. - Folding of prion protein to its native alpha-helical conformation is under kinetic control - The Journal of Biological Chemistry 2001 Jun 8; 276(23): 19687-90

ABAZ - Baskakov,I.V.; Aagaard,C.; Mehlhorn,I.; Wille,H.; Groth,D.; Baldwin,M.A.; Prusiner,S.B.; Cohen,F.E. - Self-assembly of recombinant prion protein of 106 residues - Biochemistry 2000 Mar 14; 39(10): 2792-804

ATZD - Bocharova,O.V.; Makarava,N.; Breydo,L.; Anderson,M.; Salnikov,V.V.; Baskakov,I.V. - Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core - The Journal of Biological Chemistry 2006 Jan 27; 281(4): 2373-9

ASOD - Bocharova,O.V.; Breydo,L.; Salnikov,V.V.; Baskakov,I.V. - Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils - Biochemistry 2005 May 10; 44(18): 6776-87

ASOE - Bocharova,O.V.; Breydo,L.; Salnikov,V.V.; Gill,A.C.; Baskakov,I.V. - Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPsc from sporadic Creutzfeldt-Jakob Disease - Protein Science 2005 May; 14(5): 1222-32

ARNV - Bocharova,O.V.; Breydo,L.; Parfenov,A.S.; Salnikov,V.V.; Baskakov,I.V. - In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPsc - Journal of Molecular Biology 2005 Feb 18; 346(2): 645-59

AVVS - Breydo,L.; Sun,Y.; Makarava,N.; Lee,C.I.; Novitskaia,V.; Bocharova,O.V.; Kao,J.P.; Baskakov,I.V. - Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation - Biochemistry 2007 Jan 23; 46(3): 852-61

ATWP - Breydo,L.; Bocharova,O.V.; Makarava,N.; Salnikov,V.V.; Anderson,M.; Baskakov,I.V. - Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation - Biochemistry 2005 Nov 29; 44(47): 15534-43

ARUY - Breydo,L.; Bocharova,O.V.; Baskakov,I.V. - Semiautomated cell-free conversion of prion protein: applications for high-throughput screening of potential antiprion drugs. - Analytical Biochemistry 2005 Apr 1; 339(1): 165-73

AYHM - Lee,C.I.; Yang,Q.; Perrier,V.; Baskakov,I.V. - The dominant-negative effect of the Q218K variant of the prion protein does not require protein X - Protein Science 2007 Oct; 16(10): 2166-73

AWIX - Legname,G.; Baskakov,I.V.; Nguyen,H.O.B.; Cohen,F.E.; DeArmond,S.J.; Prusiner,S.B. - Mouse synthetic prions from full-length prion protein - International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Poster sessions S-16

ARRH - Legname,G.; Nguyen,H.O.B.; Baskakov,I.V.; Cohen,F.E.; DeArmond,S.J.; Prusiner,S.B. - Strain-specified characteristics of mouse synthetic prions - Proceedings of the National Academy of Sciences of the United States of America 2005 Feb 8; 102(6): 2168-73

AQUT - Legname,G.; Baskakov,I.V.; Nguyen,H.O.B.; Riesner,D.; Cohen,F.E.; DeArmond,S.J.; Prusiner,S.B. - Synthetic mammalian prions - Science 2004 Jul 30; 305(5684): 673-6

AUYM - Makarava,N.; Bocharova,O.V.; Salnikov,V.V.; Breydo,L.; Anderson,M.; Baskakov,I.V. - Dichotomous versus palm-type mechanisms of lateral assembly of amyloid fibrils - Protein Science 2006 Jun; 15(6): 1334-41

ATDO - Makarava,N.; Parfenov,A.; Baskakov,I.V. - Water-soluble hybrid nanoclusters with extra bright and photostable emissions: a new tool for biological imaging. - Biophysical Journal 2005 Jul; 89(1): 572-80

AXSU - Mohorko,N.; Makarava,N.; Baskakov,I.V.; Petric,A.; Kepe,V.; Barrio,J.R.; Bresjanac,M. - FDDNP Labelling of Prion Amyloid Fibrils in Vitro - International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Pathology and Pathogenesis P03.75

AVPG - Nishina,K.A.; Deleault,N.R.; Mahal,S.P.; Baskakov,I.V.; Lührs,T.; Riek,R.; Supattapone,S. - The stoichiometry of host PrPc glycoforms modulates the efficiency of PrPsc formation in vitro - Biochemistry 2006 Nov 28; 45(47): 14129-39

AYCZ - Novitskaya,V.; Makarava,N.; Sylvester,I.; Bronstein,I.B.; Baskakov,I.V. - Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2-derived terminally differentiated neurons - Journal of Neurochemistry 2007 Jul; 102(2): 398-407

AWLF - Novitskaya,V.; Makarava,N.; Bellon,A.; Bocharova,O.V.; Bronstein,I.B.; Williamson,R.A.; Baskakov,I.V. - Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay - International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Oral sessions ORAL-14

AUZM - Novitskaya,V.; Makarava,N.; Bellon,A.; Bocharova,O.V.; Bronstein,I.B.; Williamson,R.A.; Baskakov,I.V. - Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay - The Journal of Biological Chemistry 2006 Jun 2; 281(22): 15536-45

AUWF - Novitskaya,V.; Bocharova,O.V.; Bronstein,I.B.; Baskakov,I.V. - Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons - The Journal of Biological Chemistry 2006 May 12; 281(19): 13828-36

AVVC - Sun,Y.; Breydo,L.; Makarava,N.; Yang,Q.; Bocharova,O.V.; Baskakov,I.V. - Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure - The Journal of Biological Chemistry 2007 Mar 23; 282(12): 9090-7

AVES - Ter-Avanesyan,M.D.; Derkatch,I.; Baskakov,I.V.; Kushnirov,V. - Unraveling prion structures and biological functions - Genome Biology 2005; 6(13): 366

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