Membrane interactions in nerve myelin. I. Determination of surface charge from effects of pH and ionic strength on period.

Por Inouye, H., Kirschner, D. A.
Publicado em 1988

Membrane interactions in nerve myelin: II. Determination of surface charge from biochemical data.

Por Inouye, H, Kirschner, D A
Publicado em 1988

Myelin structure transformed by dimethylsulfoxide.

Por Kirschner, D A, Caspar, D L
Publicado em 1975

Membrane structure in isolated and intact myelins.

Por Inouye, H, Karthigasan, J, Kirschner, D A
Publicado em 1989

X-ray diffraction study of the kinetics of myelin lattice swelling. Effect of divalent cations.

Por Padrón, R, Mateu, L, Kirschner, D A
Publicado em 1979

X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

Por Kirschner, D A, Abraham, C, Selkoe, D J
Publicado em 1986

Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

Por Inouye, H., Fraser, P. E., Kirschner, D. A.
Publicado em 1993

Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.

Por Malinchik, S B, Inouye, H, Szumowski, K E, Kirschner, D A
Publicado em 1998

pH-dependent structural transitions of Alzheimer amyloid peptides.

Por Fraser, P E, Nguyen, J T, Surewicz, W K, Kirschner, D A
Publicado em 1991

Tetrameric assembly of full-sequence protein zero myelin glycoprotein by synchrotron x-ray scattering.

Por Inouye, H, Tsuruta, H, Sedzik, J, Uyemura, K, Kirschner, D A
Publicado em 1999

On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.

Por Lomakin, A, Chung, D S, Benedek, G B, Kirschner, D A, Teplow, D B
Publicado em 1996

Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro.

Por Kirschner, D A, Inouye, H, Duffy, L K, Sinclair, A, Lind, M, Selkoe, D J
Publicado em 1987