The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Demonstration by Fluorescence Resonance Energy Transfer of Two Sites of Interaction between the Low-Density Lipoprotein Receptor-Related Protein and the Amyloid Precursor Protein: Role of the Intracellular Adapter Protein Fe65
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FRET experiments have shown close opposition of extracellular domains of KPI-containing APP and LRP that is RAP sensitive.
“because fluorescence resonance energy transfer experiments have shown that there is a close opposition of the extracellular domains of KPI-containing APP and LRP that is RAP sensitive (Kinoshita et al., 2001).”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Kinoshita et al., 2001
An interaction between the C-terminal domain of APP and LRP, mediated by the cytoplasmic adaptor protein Fe65, impacts APP internalization.
“In addition, an interaction between the C-terminal domain of APP and LRP, mediated by the cytoplasmic adaptor protein Fe65, impacts APP internalization (18 -23).”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [22]
The LRP C-terminal domain mediates an interaction with APP in similar cell compartments.
“The LRP C-terminal domain also mediates an interaction with APP in similar cell compartments (22).”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [22]
APP-LRP interactions in CHO cells have shown that decreased LRP activity by genetic deletion or by addition of exogenous RAP could result in decreased Aβ production from hAPP770 transfected cells, and these ectodomain interactions alter the endocytic pathway.
“APP-LRP interactions in CHO cells have shown that decreased LRP activity by genetic deletion or by addition of exogenous RAP could result in decreased A production from hAPP770transfected cells, and these ectodomain interactions alter the endocytic pathway (Kinoshita et al., 2001).”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Kinoshita et al., 2001
The C-terminal site of APP interacts with LRP via the adapter protein Fe65.
“Furthermore, the C-terminal site of APP interacts with LRP via the adapter protein Fe65”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Kinoshita et al., 2001
The association of LRP with forms of APP that contain the KPI domain alters APP processing, leading to altered Aβ production.
“The association of LRP with forms of APP that contain the KPI domain alters APP processing, leading to altered A production (Kinoshita et al., 2001).”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Kinoshita et al., 2001
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Fiore, F., Zambrano, N., Minopoli, G., Donini, V., Duilio, A., & Russo, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.30853 · Cited by 294
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Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168
Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782
The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate
von Arnim, C. A. F., Kinoshita, A., Peltan, I. D., Tangredi, M. M., Herl, L., Lee, B. M., Spoelgen, R., Hshieh, T. T., Ranganathan, S., Battey, F. D., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414248200 · Cited by 258
Self-citationPietrzik, C. U., Busse, T., Merriam, D. E., Weggen, S., & Koo, E. H. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf568 · Cited by 198
Andersen, O. M., Schmidt, V., Spoelgen, R., Gliemann, J., Behlke, J., Galatis, D., McKinstry, W. J., Parker, M. W., Masters, C. L., Hyman, B. T., et al. (2006) · Biochemistry · doi:10.1021/bi052120v · Cited by 178
Self-citationCastellano, J. M., Deane, R., Gottesdiener, A. J., Verghese, P. B., Stewart, F. R., West, T., Paoletti, A. C., Kasper, T. R., DeMattos, R. B., Zlokovic, B. V., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206446109 · Cited by 154
Zerbinatti, C. V., Wozniak, D. F., Cirrito, J., Cam, J. A., Osaka, H., Bales, K. R., Zhuo, M., Paul, S. M., Holtzman, D. M., & Bu, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305803101 · Cited by 133
Zerbinatti, C. V., Wahrle, S. E., Kim, H., Cam, J. A., Bales, K., Paul, S. M., Holtzman, D. M., & Bu, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604436200 · Cited by 129
Hoe, H.-S., Wessner, D., Beffert, U., Becker, A. G., Matsuoka, Y., & Rebeck, G. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9259-9268.2005 · Cited by 122
Self-citationFunctional Roles of the Interaction of APP and Lipoprotein Receptors
Pohlkamp, T., Wasser, C. R., & Herz, J. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00054 · Cited by 92
Van Uden, E., Mallory, M., Veinbergs, I., Alford, M., Rockenstein, E., & Masliah, E. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-21-09298.2002 · Cited by 91
Drugs targeting alzheimer’s disease: Some things old and some things new
Michaelis, M. L. (2003) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.035840 · Cited by 78
FE65 interaction with the ApoE receptor ApoEr2
Hoe, H.-S., Magill, L. A., Guenette, S., Fu, Z., Vicini, S., & Rebeck, G. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600728200 · Cited by 69
Self-citationThe generation and function of soluble apoE receptors in the CNS
Rebeck, G. W., LaDu, M. J., Estus, S., Bu, G., & Weeber, E. J. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-15 · Cited by 66
Self-citationRanganathan, S., Noyes, N. C., Migliorini, M., Winkles, J. A., Battey, F. D., Hyman, B. T., Smith, E., Yepes, M., Mikhailenko, I., & Strickland, D. K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5065-10.2011 · Cited by 49
“LRP1 was discovered to bind to the amyloid precursor protein (APP) (Kounnas et al., 1995; Knauer et al., 1996; Kinoshita et al., 2001), a transmembrane protein that is proteolytically processed to generate the -amyloid (A ) peptide that is a major component of plaques in Alzheimer’s patients.”
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Metadata
- Authors
- Kinoshita, A., Whelan, C. M., Smith, C. J., Mikhailenko, I., Rebeck, G. W., Strickland, D. K., & Hyman, B. T.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2001-11-01
- Volume
- 21
- Issue
- 21
- Pages
- 8354-8361
- ISSN
- 0270-6474
- 1529-2401
- Cited by
- 113
- References
- 1
- Language
- en
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