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Cited by 373

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Clearance of amyloid-β by circulating lipoprotein receptors

Sagare, Abhay, Deane, Rashid, Bell, Robert D, Johnson, Bradley, Hamm, Katie, Pendu, Ronan, Marky, Andrew, Lenting, Peter J, Wu, Zhenhua, Zarcone, Troy, Goate, Alison, Mayo, Kevin, Perlmutter, David, Coma, Mireia, Zhong, Zhihui, Zlokovic, Berislav V·2007·Nature Medicine
DOI 10.1038/nm1635
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Integrity signals

Registry

Crossref · 10.1038/nm1635

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

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Claims other papers make about this one

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  • The binding affinity results, as well as the predominant importance of LRP1 at elevated Aβ concentrations, support the idea that maintaining steady Aβ clearance at the BBB by LRP1 could be a potential target for treatment of age-related neurological disorders.

    “The binding affinity results, as well as the predominant importance of LRP1 at elevated Aβ concentrations, support the idea that maintaining steady Aβ clearance at the BBB by LRP1 could be a potential target for treatment of agerelated neurological disorders (51).”

    From Endothelial LRP1 transports amyloid-β1–42 across the blood-brain barrier (2015) · cites this paper as [51]

    The Abstract reports high-affinity Aβ binding by LRP-IV and describes LRP1-mediated Aβ clearance at the BBB. It proposes LRP-IV as a peripheral Aβ-clearance therapy for Alzheimer’s disease, but does not establish that BBB LRP1 is predominantly important at elevated Aβ concentrations or propose maintaining its BBB activity to treat age-related neurological disorders generally. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • At 5 nM, Aβ binding to LRP1 is not yet saturated.

    “It has been shown that, at 5 nM, Aβ binding to LRP1 is not yet saturated (50,51).”

    From Endothelial LRP1 transports amyloid-β1–42 across the blood-brain barrier (2015) · cites this paper as [51]

    The binding-affinity passage (labeled Abstract in our copy; no page given) reports that Aβ40 and Aβ42 bind recombinant LRP cluster IV with dissociation constants of 1.9 and 5.1 nM, respectively. Those values are consistent with binding not being saturated at 5 nM, but the passage does not establish saturation at that concentration for intact LRP1. (LLM, conf=0.78)

    Experimental — accuracy not yet measured

Self-check

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Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 11

  1. Deane, R. et al. Neuron 43, 333–344 (2004). · DOI · Paper page
  2. Tanzi, R.E., Moir, R.D. & Wagner, S.L. Neuron 43, 605–608 (2004).
  3. Tamaki, C. et al. Pharm. Res. 23, 1407–1416 (2006). · DOI · Paper page
  4. Quinn, K.A. et al. J. Biol. Chem. 272, 23946–23951 (1997). · DOI
  5. Westein, E., Denis, C.V., Bouma, B.N. & Lenting, P.J. J. Biol. Chem. 277, 2511–2516 (2002). · DOI
  6. Zerbinatti, C.V. & Bu, G.J. Rev. Neurosci. 16, 123–135 (2005). · DOI
  7. Jensen, G.A. et al. J. Mol. Biol. 362, 700–716 (2006). · DOI
  8. Kumar-Singh, S. et al. Am. J. Pathol. 167, 527–543 (2005). · DOI
  9. Hsiao, K. et al. Science 274, 99–102 (1996). · DOI · Paper page
  10. Fryer, J.D. et al. J. Neurosci. 25, 2803–2810 (2005). · DOI · Paper page
  11. Matsuoka, Y. et al. J. Neurosci. 23, 29–33 (2003). · DOI

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Metadata

Authors
Sagare, A., Deane, R., Bell, R. D., Johnson, B., Hamm, K., Pendu, R., Marky, A., Lenting, P. J., Wu, Z., Zarcone, T., Goate, A., Mayo, K., Perlmutter, D., Coma, M., Zhong, Z., & Zlokovic, B. V.
Venue
Nature Medicine
Publisher
Springer Science and Business Media LLC
Published
2007-08-12
Volume
13
Issue
9
Pages
1029-1031
ISSN
  • 1078-8956
  • 1546-170X
DOI
10.1038/nm1635
Cited by
373
References
4
Language
en
Licence
www.springer.com/tdm (tdm)

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