A new look at the decomposition of unipotents and the normal structure of Chevalley groups

A. Stepanov

doi:10.1090/spmj/1456

A new look at the decomposition of unipotents and the normal structure of Chevalley groups

St Petersburg Mathematical Journal ◽

10.1090/spmj/1456 ◽

2017 ◽

Vol 28 (3) ◽

pp. 411-419 ◽

Cited By ~ 2

Author(s):

A. Stepanov

Keyword(s):

Normal Structure ◽

Chevalley Groups ◽

New Look

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Automorphisms and normal structure of unipotent subgroups of finitary Chevalley groups

Proceedings of the Steklov Institute of Mathematics ◽

10.1134/s0081543809070128 ◽

2009 ◽

Vol 267 (S1) ◽

pp. 118-127 ◽

Cited By ~ 1

Author(s):

V. M. Levchuk ◽

G. S. Suleimanova

Keyword(s):

Normal Structure ◽

Chevalley Groups

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Normal Structure of Maximal Parabolic Subgroups in Chevalley Groups over Rings

Algebra Colloquium ◽

10.1142/s1005386709000595 ◽

2009 ◽

Vol 16 (04) ◽

pp. 631-648 ◽

Cited By ~ 6

Author(s):

Anastasia Stavrova

Keyword(s):

Commutative Ring ◽

Parabolic Subgroup ◽

Chevalley Group ◽

Normal Structure ◽

Levi Subgroup ◽

Parabolic Subgroups ◽

Chevalley Groups ◽

Maximal Parabolic Subgroup ◽

Elementary Subgroup ◽

Maximal Parabolic Subgroups

We study the normal structure of maximal parabolic subgroups of a Chevalley group over a commutative ring. More precisely, we describe the subgroups of a maximal parabolic subgroup P normalized by the elementary part of its Levi subgroup. As a corollary, we obtain a description of the subgroups in P normalized by its elementary subgroup EP.

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The microtubule associated protein (MAP) tau forms a new class of triple-stranded left-hand helical fibrous protein polymer

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123106 ◽

1992 ◽

Vol 50 (1) ◽

pp. 540-541

Author(s):

G. C. Ruben ◽

K. Iqbal ◽

I. Grundke-Iqbal ◽

H. Wisniewski ◽

T. L. Ciardelli ◽

...

Keyword(s):

Axial Ratio ◽

Normal Structure ◽

Paired Helical Filaments ◽

Left Hand ◽

New Class ◽

Protein Polymer ◽

Fibrous Protein ◽

Protein Map ◽

Neurotransmitter Transport ◽

Alzheimer Neurofibrillary Tangles

In neurons, the microtubule associated protein, tau, is found in the axons. Tau stabilizes the microtubules required for neurotransmitter transport to the axonal terminal. Since tau has been found in both Alzheimer neurofibrillary tangles (NFT) and in paired helical filaments (PHF), the study of tau's normal structure had to preceed TEM studies of NFT and PHF. The structure of tau was first studied by ultracentrifugation. This work suggested that it was a rod shaped molecule with an axial ratio of 20:1. More recently, paraciystals of phosphorylated and nonphosphoiylated tau have been reported. Phosphorylated tau was 90-95 nm in length and 3-6 nm in diameter where as nonphosphorylated tau was 69-75 nm in length. A shorter length of 30 nm was reported for undamaged tau indicating that it is an extremely flexible molecule. Tau was also studied in relation to microtubules, and its length was found to be 56.1±14.1 nm.

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