The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Degradation of Soluble and Fibrillar Amyloid β-Protein by Matrix Metalloproteinase (MT1-MMP) in Vitro
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The recombinant catalytic domain of MT1-MMP degraded amyloid plaques when incubated ex vivo on brain slices of transgenic AD Tg2576 mice.
“In addition, the recombinant catalytic domain of MT1-MMP could degrade amyloid plaques when incubated ex vivo on brain slices of transgenic AD Tg2576 mice (Liao and Van Nostrand, 2010).”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Liao and Van Nostrand, 2010
There are only two MMPs in Drosophila, the secreted dMMP-1 and membrane-anchored dMMP-2.
“There are only two MMPs in Drosophila, the secreted dMMP-1 and membrane-anchored dMMP-2 (32,48).”
From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [32]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
DeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Adult mouse astrocytes degrade amyloid-β in vitro and in situ
Wyss-Coray, T., Loike, J. D., Brionne, T. C., Lu, E., Anankov, R., Yan, F., Silverstein, S. C., & Husemann, J. (2003) · Nature Medicine · doi:10.1038/nm838 · Cited by 909
Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ
Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380 · cited 12×
“MMP9, like MT1-MMP, cleaves between residues Ala30-Ile31 (37).”
BackgroundMethodInfluentialDavis, J., Xu, F., Deane, R., Romanov, G., Previti, M. L., Zeigler, K., Zlokovic, B. V., & Van Nostrand, W. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312946200 · Cited by 373
Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-24-07910.1996 · Cited by 331 · cited 10×
“MMP9, like MT1-MMP, cleaves between residues Ala30-Ile31 (37).”
InfluentialImmune reactive cells in senile plaques and cognitive decline in Alzheimer’s disease
Vehmas, A. K., Kawas, C. H., Stewart, W. F., & Troncoso, J. C. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00090-8 · Cited by 230
Flagged first, then by citations
Research works printed but not linked: 38
- Mattson M. P., 2004, Nature, 430, 631, 10.1038/nature02621 · DOI · Paper page
- Evin G., 2002, Peptides, 23, 1285, 10.1016/S0196-9781(02)00063-3 · DOI
- Saido T. C., 1998, Neurobiol. Aging, 19, S69, 10.1016/S0197-4580(98)00033-5 · DOI
- Zlokovic B. V., 2004, J. Neurochem., 89, 807, 10.1111/j.1471-4159.2004.02385.x · DOI · Paper page
- Iwata N., 2000, Nat. Med., 6, 143, 10.1038/72237 · DOI · Paper page
- Iwata N., 2001, Science, 292, 1550, 10.1126/science.1059946 · DOI
- Qiu W. Q., 1998, J. Biol. Chem., 273, 32730, 10.1074/jbc.273.49.32730 · DOI · Paper page
- Ledesma M. D., 2000, EMBO Rep., 1, 530, 10.1093/embo-reports/kvd107 · DOI
- Eckman E. A., 2001, J. Biol. Chem., 276, 24540, 10.1074/jbc.M007579200 · DOI
- Hu J., 2001, J. Biol. Chem., 276, 47863, 10.1074/jbc.M104068200 · DOI
- Liao M. C., 2009, J. Biol. Chem., 284, 28917, 10.1074/jbc.M109.050856 · DOI
- Yamada T., 1995, Acta Neuropathol., 89, 199, 10.1007/BF00309334 · DOI
- Roher A. E., 1994, Biochem. Biophys. Res. Commun., 205, 1755, 10.1006/bbrc.1994.2872 · DOI
- Jung S. S., 2003, J. Neurochem., 85, 1208, 10.1046/j.1471-4159.2003.01745.x · DOI
- Gottschall P. E., 1995, J. Neurosci. Res., 42, 335, 10.1002/jnr.490420307 · DOI
- Muir E. M., 2002, Brain Res., 100, 103
- Deb S., 1996, J. Neurochem., 66, 1641, 10.1046/j.1471-4159.1996.66041641.x · DOI
- Deb S., 2003, Brain Res., 970, 205, 10.1016/S0006-8993(03)02344-8 · DOI · Paper page
- Deb S., 1999, J. Neurosci. Res., 55, 44, 10.1002/(SICI)1097-4547(19990101)55:1<44::AID-JNR6>3.0.CO;2-G · DOI
- Strongin A. Y., 1995, J. Biol. Chem., 270, 5331, 10.1074/jbc.270.10.5331 · DOI
- Sato H., 1994, Nature, 370, 61, 10.1038/370061a0 · DOI
- Deryugina E. I., 2001, Exp. Cell Res., 263, 209, 10.1006/excr.2000.5118 · DOI
- Yamada T., 1995, Acta Neuropathol., 90, 421, 10.1007/BF00294800 · DOI
- Sternlicht M. D., 2001, Annu. Rev. Cell Dev. Biol., 17, 463, 10.1146/annurev.cellbio.17.1.463 · DOI · Paper page
- McCawley L. J., 2001, Curr. Opin. Cell Biol., 13, 534, 10.1016/S0955-0674(00)00248-9 · DOI · Paper page
- Leppert D., 2001, Brain Res. Brain Res. Rev., 36, 249, 10.1016/S0165-0173(01)00101-1 · DOI
- Ahmad M., 2006, J. Biochem., 139, 517, 10.1093/jb/mvj054 · DOI · Paper page
- Dickson D. W., 1990, Acta Neuropathol., 79, 486, 10.1007/BF00296107 · DOI
- Ross S. A., 1996, Br. J. Neurosurg., 10, 471, 10.1080/02688699647104 · DOI
- Yin K. J., 2006, J. Neurosci., 26, 10939, 10.1523/JNEUROSCI.2085-06.2006 · DOI · Paper page
- Davis J., 1999, Amyloid, 6, 157, 10.3109/13506129909007321 · DOI
- Cao J., 1995, J. Biol. Chem., 270, 801, 10.1074/jbc.270.2.801 · DOI
- Tucker H. M., 2000, J. Neurosci., 20, 3937, 10.1523/JNEUROSCI.20-11-03937.2000 · DOI
- Wetzel R., 2002, Structure, 10, 1031, 10.1016/S0969-2126(02)00809-2 · DOI
- Crouch P. J., 2009, J. Neurochem., 108, 1198, 10.1111/j.1471-4159.2009.05870.x · DOI
- Roher A. E., 1994, Biochem. Biophys. Res. Commun., 205, 1755, 10.1006/bbrc.1994.2872 · DOI
- Lee J. M., 2003, Ann. Neurol., 54, 379, 10.1002/ana.10671 · DOI
- Baig S., 2008, Neuropathol. Appl. Neurobiol., 34, 205, 10.1111/j.1365-2990.2007.00897.x · DOI
Cited by
Sorted by citations
Proteolytic Degradation of Amyloid -Protein
Saido, T., & Leissring, M. A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006379 · Cited by 368
Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease
Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331
Oxidative stress and β-amyloid protein in Alzheimer’s disease
Cai, Z., Zhao, B., & Ratka, A. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-011-8155-9 · Cited by 279
Aβ-degrading enzymes: potential for treatment of Alzheimer disease
Miners, J. S., Barua, N., Kehoe, P. G., Gill, S., & Love, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182345e46 · Cited by 265
Brkic, M., Balusu, S., Libert, C., & Vandenbroucke, R. E. (2015) · Mediators of Inflammation · doi:10.1155/2015/620581 · Cited by 205
Andrus, B. M., Blizinsky, K., Vedell, P. T., Dennis, K., Shukla, P. K., Schaffer, D. J., Radulovic, J., Churchill, G. A., & Redei, E. E. (2012) · Molecular Psychiatry · doi:10.1038/mp.2010.119 · Cited by 178
Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges
Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94
García-González, L., Pilat, D., Baranger, K., & Rivera, S. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00244 · Cited by 88
ECM in brain aging and dementia
Morawski, M., Filippov, M., Tzinia, A., Tsilibary, E., & Vargova, L. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00010-4 · Cited by 84
Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection
Brown, M. R., Radford, S. E., & Hewitt, E. W. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.609073 · Cited by 67
Nitric oxide‐mediated regulation of ‐amyloid clearance via alterations of MMP‐9/TIMP‐1
Ridnour, L. A., Dhanapal, S., Hoos, M., Wilson, J., Lee, J., Cheng, R. Y. S., Brueggemann, E. E., Hines, H. B., Wilcock, D. M., Vitek, M. P., et al. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12028 · Cited by 54
Sutinen, E. M., Korolainen, M. A., Häyrinen, J., Alafuzoff, I., Petratos, S., Salminen, A., Soininen, H., Pirttilä, T., & Ojala, J. O. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00214 · Cited by 34
Yang, C.-N., Wu, M.-F., Liu, C.-C., Jung, W.-H., Chang, Y.-C., Lee, W.-P., Shiao, Y.-J., Wu, C.-L., Liou, H.-H., Lin, S.-K., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx278 · Cited by 27
Kamboj, S., Harms, C., Wright, D., Nash, A., Klein-Seetharaman, J., & Sarkar, S. K. (2022) · doi:10.21203/rs.3.rs-1258797/v1 · Cited by 1
Metadata
- Authors
- Liao, M.-C., & Van Nostrand, W. E.
- Affiliations
- Departments of Neurosurgery and Medicine, Stony Brook University, Health Sciences Center, Stony Brook, New York 11794-8122
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-01-20
- Volume
- 49
- Issue
- 6
- Pages
- 1127-1136
- ISSN
- 0006-2960
- 1520-4995
- PMC
- PMC2819544
- Cited by
- 92
- References
- 9
- 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
