Cited by 79

The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.

Chapter 5 Autophagic Clearance of Aggregate‐Prone Proteins Associated with Neurodegeneration

Sarkar, Sovan, Ravikumar, Brinda, Rubinsztein, David C.·2009·Methods in Enzymology

Abstract

Autophagy has emerged as a field of rapidly growing interest with implications in several disease conditions, such as cancer, infectious diseases, and neurodegenerative diseases. Autophagy is a major degradation pathway for aggregate-prone, intracytosolic proteins causing neurodegenerative disorders, such as Huntington's disease and forms of Parkinson's disease. Up-regulating autophagy may be a tractable therapeutic intervention for clearing these disease-causing proteins. The identification of autophagy-enhancing compounds would be beneficial not only in neurodegenerative diseases but also in other conditions where up-regulating autophagy may act as a protective pathway. Furthermore, small molecule modulators of autophagy may also be useful in dissecting pathways governing mammalian autophagy. In this chapter, we highlight assays that can be used for the identification of autophagy regulators, such as measuring the clearance of mutant aggregate-prone proteins or of autophagic flux with bafilomycin A(1). Using these methods, we recently described several mTOR-independent autophagy-enhancing compounds that have protective effects in various models of Huntington's disease.

Overview

Integrity signals

Registry

Crossref · 10.1016/s0076-6879(08)04005-6

Cites

15 of 15 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Research works printed but not linked: 29

  1. Bampton, 2005, The dynamics of autophagy visualised in live cells: From autophagosome formation to fusion with endo/lysosomes, Autophagy, 1, 23, 10.4161/auto.1.1.1495 · DOI
  2. Berger, 2006, Rapamycin alleviates toxicity of different aggregate‐prone proteins, Hum. Mol. Genet., 15, 433, 10.1093/hmg/ddi458 · DOI · Paper page
  3. Carmichael, 2002, Glycogen synthase kinase‐3β inhibitors prevent cellular polyglutamine toxicity caused by the Huntington's disease mutation, J. Biol. Chem., 277, 33791, 10.1074/jbc.M204861200 · DOI
  4. Ekstrom, 1984, Inhibition of fast axonal transport by erythro‐9‐[3‐(2‐hydroxynonyl)]adenine, J. Neurochem., 43, 1342, 10.1111/j.1471-4159.1984.tb05392.x · DOI
  5. Goll, 2003, The calpain system, Physiol. Rev., 83, 731, 10.1152/physrev.00029.2002 · DOI
  6. Hara, 2006, Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice, Nature, 441, 885, 10.1038/nature04724 · DOI · Paper page
  7. Kabeya, 2000, LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing, EMBO J., 19, 5720, 10.1093/emboj/19.21.5720 · DOI · Paper page
  8. Klionsky, 2008, Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes, Autophagy, 4, 151, 10.4161/auto.5338 · DOI · Paper page
  9. Komatsu, 2006, Loss of autophagy in the central nervous system causes neurodegeneration in mice, Nature, 441, 880, 10.1038/nature04723 · DOI · Paper page
  10. Levine, 2004, Development by self‐digestion: Molecular mechanisms and biological functions of autophagy, Dev. Cell, 6, 463, 10.1016/S1534-5807(04)00099-1 · DOI
  11. Meijer, 2006, Signalling and autophagy regulation in health, aging and disease, Mol. Aspects Med., 27, 411, 10.1016/j.mam.2006.08.002 · DOI
  12. Mizushima, 2004, Methods for monitoring autophagy, Int. J. Biochem. Cell Biol., 36, 2491, 10.1016/j.biocel.2004.02.005 · DOI
  13. Mizushima, 2008, Autophagy fights disease through cellular self‐digestion, Nature, 451, 1069, 10.1038/nature06639 · DOI · Paper page
  14. Narain, 1999, A molecular investigation of true dominance in Huntington's disease, J. Med. Genet., 36, 739, 10.1136/jmg.36.10.739 · DOI
  15. Noda, 1998, Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast, J. Biol. Chem., 273, 3963, 10.1074/jbc.273.7.3963 · DOI
  16. Petiot, 2000, Distinct classes of phosphatidylinositol 3′‐kinases are involved in signaling pathways that control macroautophagy in HT‐29 cells, J. Biol. Chem., 275, 992, 10.1074/jbc.275.2.992 · DOI
  17. Ravikumar, 2005, Dynein mutations impair autophagic clearance of aggregate‐prone proteins, Nat. Genet., 37, 771, 10.1038/ng1591 · DOI · Paper page
  18. Ravikumar, 2002, Aggregate‐prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy, Hum. Mol. Genet., 11, 1107, 10.1093/hmg/11.9.1107 · DOI
  19. Ross, 2005, What is the role of protein aggregation in neurodegeneration?, Nat. Rev. Mol. Cell Biol., 6, 891, 10.1038/nrm1742 · DOI
  20. Rubinsztein, 2007, Potential therapeutic applications of autophagy, Nat. Rev. Drug Discov., 6, 304, 10.1038/nrd2272 · DOI · Paper page
  21. Sarbassov, 2005, Growing roles for the mTOR pathway, Curr. Opin. Cell Biol., 17, 596, 10.1016/j.ceb.2005.09.009 · DOI
  22. Sarkar, 2007, Trehalose, a novel mTOR‐independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α‐synuclein, J. Biol. Chem., 282, 5641, 10.1074/jbc.M609532200 · DOI · Paper page
  23. Sarkar, 2005, Lithium induces autophagy by inhibiting inositol monophosphatase, J. Cell Biol., 170, 1101, 10.1083/jcb.200504035 · DOI · Paper page
  24. Sarkar, 2008, A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin, Hum. Mol. Genet., 17, 170, 10.1093/hmg/ddm294 · DOI
  25. Sarkar, 2007, Small molecules enhance autophagy and reduce toxicity in Huntington's disease models, Nat. Chem. Biol., 3, 331, 10.1038/nchembio883 · DOI
  26. Tanida, 2004, HsAtg4B/HsApg4B/autophagin‐1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule‐associated protein light chain 3‐ and GABAA receptor‐associated protein‐phospholipid conjugates, J. Biol. Chem., 279, 36268, 10.1074/jbc.M401461200 · DOI · Paper page
  27. Wyttenbach, 2002, Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin, Hum. Mol. Genet., 11, 1137, 10.1093/hmg/11.9.1137 · DOI
  28. Wyttenbach, 2001, Polyglutamine expansions cause decreased CRE‐mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease, Hum. Mol. Genet., 10, 1829, 10.1093/hmg/10.17.1829 · DOI
  29. Xie, 2007, Autophagosome formation: core machinery and adaptations, Nat. Cell Biol., 9, 1102, 10.1038/ncb1007-1102 · DOI

Cited by

Sorted by citations

See all 79

Metadata

Authors
Sarkar, S., Ravikumar, B., & Rubinsztein, D. C.
Venue
Methods in Enzymology
Publisher
Elsevier
Published
2009
Pages
83-110
ISSN
0076-6879
Cited by
79
References
15
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review