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Harvard
Christie, G, Markwell, RE, Gray, CW, Smith, L, Godfrey, F, Mansfield, F, Wadsworth, H, King, R, McLaughlin, M, Cooper, DG, Ward, RV, Howlett, DR, Hartmann, T, Lichtenthaler, SF, Beyreuther, K, Underwood, J, Gribble, SK, Cappai, R, Masters, CL, Tamaoka, A, Gardner, RL, Rivett, AJ, Karran, EH
& Allsop, D 1999, '
Alzheimer's Disease: correlation of the suppression of β-Amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome',
Journal of Neurochemistry, vol. 73, no. 1, pp. 195-204.
https://doi.org/10.1046/j.1471-4159.1999.0730195.xAPA
Christie, G., Markwell, R. E., Gray, C. W., Smith, L., Godfrey, F., Mansfield, F., Wadsworth, H., King, R., McLaughlin, M., Cooper, D. G., Ward, R. V., Howlett, D. R., Hartmann, T., Lichtenthaler, S. F., Beyreuther, K., Underwood, J., Gribble, S. K., Cappai, R., Masters, C. L.
, ... Allsop, D. (1999).
Alzheimer's Disease: correlation of the suppression of β-Amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome.
Journal of Neurochemistry,
73(1), 195-204.
https://doi.org/10.1046/j.1471-4159.1999.0730195.xVancouver
Author
Bibtex
@article{b5fa256f3918491f86a1a0ec4f5285e0,
title = "Alzheimer's Disease: correlation of the suppression of β-Amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome",
abstract = "Peptide aldehyde inhibitors of the chymotrypsin-like activity of the proteasome (CLIP) such as N-acetyl-Leu-Leu-Nle-H (or ALLN) have been shown previously to inhibit the secretion of β-amyloid peptide (Aβ) from cells. To evaluate more fully the role of the proteasome in this process, we have tested the effects on Aβ formation of a much wider range of peptide-based inhibitors of CLIP than published previously. The inhibitors tested included several peptide boronates, some of which proved to be the most potent peptide-based inhibitors of β-amyloid production reported so far. We found that the ability of the peptide aldehyde and boronate inhibitors to suppress Aβ formation from cells correlated extremely well with their potency as CLIP inhibitors. Thus, we conclude that the proteasome may be involved either directly or indirectly in Aβ formation.",
author = "G. Christie and Markwell, {R. E.} and Gray, {C. W.} and L. Smith and F. Godfrey and F. Mansfield and H. Wadsworth and R. King and M. McLaughlin and Cooper, {D. G.} and Ward, {R. V.} and Howlett, {D. R.} and T. Hartmann and Lichtenthaler, {S. F.} and K. Beyreuther and J. Underwood and Gribble, {S. K.} and R. Cappai and Masters, {C. L.} and A. Tamaoka and Gardner,, {R. L.} and Rivett, {A. J.} and Karran, {E. H.} and David Allsop",
year = "1999",
month = jul,
doi = "10.1046/j.1471-4159.1999.0730195.x",
language = "English",
volume = "73",
pages = "195--204",
journal = "Journal of Neurochemistry",
issn = "0022-3042",
publisher = "Wiley-Blackwell",
number = "1",
}
RIS
TY - JOUR
T1 - Alzheimer's Disease
T2 - correlation of the suppression of β-Amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome
AU - Christie, G.
AU - Markwell, R. E.
AU - Gray, C. W.
AU - Smith, L.
AU - Godfrey, F.
AU - Mansfield, F.
AU - Wadsworth, H.
AU - King, R.
AU - McLaughlin, M.
AU - Cooper, D. G.
AU - Ward, R. V.
AU - Howlett, D. R.
AU - Hartmann, T.
AU - Lichtenthaler, S. F.
AU - Beyreuther, K.
AU - Underwood, J.
AU - Gribble, S. K.
AU - Cappai, R.
AU - Masters, C. L.
AU - Tamaoka, A.
AU - Gardner,, R. L.
AU - Rivett, A. J.
AU - Karran, E. H.
AU - Allsop, David
PY - 1999/7
Y1 - 1999/7
N2 - Peptide aldehyde inhibitors of the chymotrypsin-like activity of the proteasome (CLIP) such as N-acetyl-Leu-Leu-Nle-H (or ALLN) have been shown previously to inhibit the secretion of β-amyloid peptide (Aβ) from cells. To evaluate more fully the role of the proteasome in this process, we have tested the effects on Aβ formation of a much wider range of peptide-based inhibitors of CLIP than published previously. The inhibitors tested included several peptide boronates, some of which proved to be the most potent peptide-based inhibitors of β-amyloid production reported so far. We found that the ability of the peptide aldehyde and boronate inhibitors to suppress Aβ formation from cells correlated extremely well with their potency as CLIP inhibitors. Thus, we conclude that the proteasome may be involved either directly or indirectly in Aβ formation.
AB - Peptide aldehyde inhibitors of the chymotrypsin-like activity of the proteasome (CLIP) such as N-acetyl-Leu-Leu-Nle-H (or ALLN) have been shown previously to inhibit the secretion of β-amyloid peptide (Aβ) from cells. To evaluate more fully the role of the proteasome in this process, we have tested the effects on Aβ formation of a much wider range of peptide-based inhibitors of CLIP than published previously. The inhibitors tested included several peptide boronates, some of which proved to be the most potent peptide-based inhibitors of β-amyloid production reported so far. We found that the ability of the peptide aldehyde and boronate inhibitors to suppress Aβ formation from cells correlated extremely well with their potency as CLIP inhibitors. Thus, we conclude that the proteasome may be involved either directly or indirectly in Aβ formation.
U2 - 10.1046/j.1471-4159.1999.0730195.x
DO - 10.1046/j.1471-4159.1999.0730195.x
M3 - Journal article
VL - 73
SP - 195
EP - 204
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
SN - 0022-3042
IS - 1
ER -
