These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
133 related articles for article (PubMed ID: 9202333)
1. Aggregation state-dependent activation of the classical complement pathway by the amyloid beta peptide. Webster S; Bradt B; Rogers J; Cooper N J Neurochem; 1997 Jul; 69(1):388-98. PubMed ID: 9202333 [TBL] [Abstract][Full Text] [Related]
2. Inhibiting the formation of classical C3-convertase on the Alzheimer's beta-amyloid peptide. Emmerling MR; Spiegel K; Watson MD Immunopharmacology; 1997 Dec; 38(1-2):101-9. PubMed ID: 9476121 [TBL] [Abstract][Full Text] [Related]
3. Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-beta peptide. Cottingham MG; Hollinshead MS; Vaux DJ Biochemistry; 2002 Nov; 41(46):13539-47. PubMed ID: 12427014 [TBL] [Abstract][Full Text] [Related]
4. Complement activation by the amyloid proteins A beta peptide and beta 2-microglobulin. Nybo M; Nielsen EH; Svehag SE Amyloid; 1999 Dec; 6(4):265-72. PubMed ID: 10611947 [TBL] [Abstract][Full Text] [Related]
5. Alzheimer's beta-amyloid peptides can activate the early components of complement classical pathway in a C1q-independent manner. Bergamaschini L; Canziani S; Bottasso B; Cugno M; Braidotti P; Agostoni A Clin Exp Immunol; 1999 Mar; 115(3):526-33. PubMed ID: 10193429 [TBL] [Abstract][Full Text] [Related]
6. Inhibition of toxicity in the beta-amyloid peptide fragment beta -(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation. Hughes E; Burke RM; Doig AJ J Biol Chem; 2000 Aug; 275(33):25109-15. PubMed ID: 10825171 [TBL] [Abstract][Full Text] [Related]
7. Activation of complement and contact system in Alzheimer's disease. Bergamaschini L; Donarini C; Gobbo G; Parnetti L; Gallai V Mech Ageing Dev; 2001 Nov; 122(16):1971-83. PubMed ID: 11589915 [TBL] [Abstract][Full Text] [Related]