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Presenilins: in search of functionality

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Presenilins: in search of functionality. / Karran, E H; Allsop, D; Christie, G et al.
In: Biochemical Society Transactions, Vol. 26, No. 3, 08.1998, p. 491-496.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Karran, EH, Allsop, D, Christie, G, Davis, J, Gray, C, Mansfield, F & Ward, RV 1998, 'Presenilins: in search of functionality', Biochemical Society Transactions, vol. 26, no. 3, pp. 491-496. https://doi.org/10.1042/bst0260491

APA

Karran, E. H., Allsop, D., Christie, G., Davis, J., Gray, C., Mansfield, F., & Ward, R. V. (1998). Presenilins: in search of functionality. Biochemical Society Transactions, 26(3), 491-496. https://doi.org/10.1042/bst0260491

Vancouver

Karran EH, Allsop D, Christie G, Davis J, Gray C, Mansfield F et al. Presenilins: in search of functionality. Biochemical Society Transactions. 1998 Aug;26(3):491-496. doi: 10.1042/bst0260491

Author

Karran, E H ; Allsop, D ; Christie, G et al. / Presenilins : in search of functionality. In: Biochemical Society Transactions. 1998 ; Vol. 26, No. 3. pp. 491-496.

Bibtex

@article{bc2c942f9222449d9cf4ae5244a7c47c,
title = "Presenilins: in search of functionality",
abstract = "The discovery of the PS proteins, the complexities of their biochemistry and their potential involvement in signalling pathways and in apoptosis have galvanized research into AD. To date, the aspect of the functionality of the PSs most relevant to the pathology of AD is the effect of PS FAD mutants to increase the proportion of A beta 42 produced from cells. This, coupled to the observation that gamma-secretase cleavage is considerably reduced in neurons derived from PS-1 knockout mice, argues strongly that PS plays a very direct role in the proteolytic processing of APP.",
keywords = "Alzheimer Disease, Amino Acid Sequence, Animals, Cell Membrane, Humans, Membrane Proteins, Mice, Mice, Knockout, Models, Molecular, Molecular Sequence Data, Neurons, Point Mutation, Presenilin-1, Presenilin-2, Protein Conformation, Signal Transduction",
author = "Karran, {E H} and D Allsop and G Christie and J Davis and C Gray and F Mansfield and Ward, {R V}",
year = "1998",
month = aug,
doi = "10.1042/bst0260491",
language = "English",
volume = "26",
pages = "491--496",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - Presenilins

T2 - in search of functionality

AU - Karran, E H

AU - Allsop, D

AU - Christie, G

AU - Davis, J

AU - Gray, C

AU - Mansfield, F

AU - Ward, R V

PY - 1998/8

Y1 - 1998/8

N2 - The discovery of the PS proteins, the complexities of their biochemistry and their potential involvement in signalling pathways and in apoptosis have galvanized research into AD. To date, the aspect of the functionality of the PSs most relevant to the pathology of AD is the effect of PS FAD mutants to increase the proportion of A beta 42 produced from cells. This, coupled to the observation that gamma-secretase cleavage is considerably reduced in neurons derived from PS-1 knockout mice, argues strongly that PS plays a very direct role in the proteolytic processing of APP.

AB - The discovery of the PS proteins, the complexities of their biochemistry and their potential involvement in signalling pathways and in apoptosis have galvanized research into AD. To date, the aspect of the functionality of the PSs most relevant to the pathology of AD is the effect of PS FAD mutants to increase the proportion of A beta 42 produced from cells. This, coupled to the observation that gamma-secretase cleavage is considerably reduced in neurons derived from PS-1 knockout mice, argues strongly that PS plays a very direct role in the proteolytic processing of APP.

KW - Alzheimer Disease

KW - Amino Acid Sequence

KW - Animals

KW - Cell Membrane

KW - Humans

KW - Membrane Proteins

KW - Mice

KW - Mice, Knockout

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Neurons

KW - Point Mutation

KW - Presenilin-1

KW - Presenilin-2

KW - Protein Conformation

KW - Signal Transduction

U2 - 10.1042/bst0260491

DO - 10.1042/bst0260491

M3 - Journal article

C2 - 9765902

VL - 26

SP - 491

EP - 496

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 3

ER -