AAAAAA

   
Results: 1-20 |
Results: 20
Caveat receptor: Proteomes on display
Authors: Stevens, FJ
Citation: Fj. Stevens, Caveat receptor: Proteomes on display, COMB CHEM H, 4(7), 2001, pp. 599-602
Amyloid fibril formation in microwell plates for screening of inhibitors
Authors: Lin, YM Raffen, R Zhou, YS Cassidy, CS Flavin, MT Stevens, FJ
Citation: Ym. Lin et al., Amyloid fibril formation in microwell plates for screening of inhibitors, AMYLOID, 8(3), 2001, pp. 182-193
Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain
Authors: Davis, DP Gallo, G Vogen, SM Dul, JL Sciarretta, KL Kumar, A Raffen, R Stevens, FJ Argon, Y
Citation: Dp. Davis et al., Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain, J MOL BIOL, 313(5), 2001, pp. 1021-1034
Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains
Authors: Dul, JL Davis, DP Williamson, EK Stevens, FJ Argon, Y
Citation: Jl. Dul et al., Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains, J CELL BIOL, 152(4), 2001, pp. 705-715
Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains
Authors: Kim, YS Cape, SP Chi, E Raffen, R Wilkins-Stevens, P Stevens, FJ Manning, MC Randolph, TW Solomon, A Carpenter, JF
Citation: Ys. Kim et al., Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains, J BIOL CHEM, 276(2), 2001, pp. 1626-1633
Immunoglobulin light chains, glycosaminoglycans, and amyloid
Authors: Stevens, FJ Kisilevsky, R
Citation: Fj. Stevens et R. Kisilevsky, Immunoglobulin light chains, glycosaminoglycans, and amyloid, CELL MOL L, 57(3), 2000, pp. 441-449
Four structural risk factors identify most fibril-forming kappa light chains
Authors: Stevens, FJ
Citation: Fj. Stevens, Four structural risk factors identify most fibril-forming kappa light chains, AMYLOID, 7(3), 2000, pp. 200-211
Inhibition of amyloid fiber assembly by both BiP and its target peptide
Authors: Davis, DP Raffen, R Dul, JL Vogen, SM Williamson, EK Stevens, FJ Argon, Y
Citation: Dp. Davis et al., Inhibition of amyloid fiber assembly by both BiP and its target peptide, IMMUNITY, 13(4), 2000, pp. 433-442
Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface
Authors: Pokkuluri, PR Cai, X Johnson, G Stevens, FJ Schiffer, M
Citation: Pr. Pokkuluri et al., Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface, PROTEIN SCI, 9(9), 2000, pp. 1852-1855
Identifying redox-sensitive extra-chloroplastic enzymes by homology modeling
Authors: Anderson, LE Li, AD Muslin, EH Schiffer, M Stevens, FJ
Citation: Le. Anderson et al., Identifying redox-sensitive extra-chloroplastic enzymes by homology modeling, PHYSL PLANT, 110(3), 2000, pp. 296-302
Protein conformation and disease: Pathological consequences of analogous mutations in homologous proteins
Authors: Stevens, FJ Pokkuluri, PR Schiffer, M
Citation: Fj. Stevens et al., Protein conformation and disease: Pathological consequences of analogous mutations in homologous proteins, BIOCHEM, 39(50), 2000, pp. 15291-15296
Oxidation-reduction properties of two engineered redox-sensitive mutant Escherichia coli malate dehydrogenases
Authors: Setterdahl, A Hirasawa, M Bucher, LM Dholakia, CA Jacquot, P Yards, H Miller, F Stevens, FJ Knaff, DB Anderson, LE
Citation: A. Setterdahl et al., Oxidation-reduction properties of two engineered redox-sensitive mutant Escherichia coli malate dehydrogenases, ARCH BIOCH, 382(1), 2000, pp. 15-21
Tertiary structure of human lambda 6 light chains
Authors: Pokkuluri, PR Solomon, A Weiss, DT Stevens, FJ Schiffer, M
Citation: Pr. Pokkuluri et al., Tertiary structure of human lambda 6 light chains, AMYLOID, 6(3), 1999, pp. 165-171
Protein folding in the ER
Authors: Stevens, FJ Argon, Y
Citation: Fj. Stevens et Y. Argon, Protein folding in the ER, SEM CELL D, 10(5), 1999, pp. 443-454
Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains
Authors: Raffen, R Dieckman, LJ Szpunar, M Wunschl, C Pokkuluri, PR Dave, P Stevens, PW Cai, XY Schiffer, M Stevens, FJ
Citation: R. Raffen et al., Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains, PROTEIN SCI, 8(3), 1999, pp. 509-517
Kappa light chain-associated Fanconi's syndrome: molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals
Authors: Deret, S Denoroy, L Lamarine, M Vidal, R Mougenot, B Frangione, B Stevens, FJ Ronco, PM Aucouturier, P
Citation: S. Deret et al., Kappa light chain-associated Fanconi's syndrome: molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals, PROTEIN ENG, 12(4), 1999, pp. 363-369
Pathogenic light chains and the B-cell repertoire
Authors: Stevens, FJ Argon, Y
Citation: Fj. Stevens et Y. Argon, Pathogenic light chains and the B-cell repertoire, IMMUNOL TOD, 20(10), 1999, pp. 451-457
Small zone, high-speed gel filtration chromatography to detect protein aggregation associated with light chain pathologies
Authors: Raffen, R Stevens, FJ
Citation: R. Raffen et Fj. Stevens, Small zone, high-speed gel filtration chromatography to detect protein aggregation associated with light chain pathologies, METH ENZYM, 309, 1999, pp. 318-332
Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain
Authors: Davis, DP Khurana, R Meredith, S Stevens, FJ Argon, Y
Citation: Dp. Davis et al., Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain, J IMMUNOL, 163(7), 1999, pp. 3842-3850
The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
Authors: Hellman, R Vanhove, M Lejeune, A Stevens, FJ Hendershot, LM
Citation: R. Hellman et al., The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP, J CELL BIOL, 144(1), 1999, pp. 21-30
Risultati: 1-20 |