This data was extracted from Medline abstracts and full texts (when available) in an automated manner.
The table below describes different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in PRIO_HUMAN at position 212 were found are listed after the table.
| Protein | PRIO_HUMAN (P04156) Gene: PRNP (other point mutations) | Swiss-Prot
Cross-reference table
Family page |
| Position | Q212 | |
| General numbering (PrionDB) | - |
| Domain | Not determined |
| Family alignments |
Mammalian prion proteins
Prion proteins (PRP, PRNP)
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| Other point mutations at the same position |
Position 212 in Mammalian prion proteins family
Position 212 in Prion proteins (PRP, PRNP) family
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| Reference #1 | Zuegg J, Gready JE
Biochemistry 1999 Oct 19;38(42):13862-76. | Medline |
| Text source | HTML and PDF full texts |
| Point mutation | Q212P (True positive) | |
| Reference #2 | Tagliavini F, Lievens PM, Tranchant C, Warter JM, Mohr M, Giaccone G, Perini F, Rossi G, Salmona M, Piccardo P, Ghetti B, Beavis RC, Bugiani O, Frangione B, Prelli F
J Biol Chem 2001 Feb 23;276(8):6009-15. | Medline |
| Text source | HTML full text |
| Point mutation | Q212P (True positive) | |
| Reference #3 | Piccardo P, Liepnieks JJ, William A, Dlouhy SR, Farlow MR, Young K, Nochlin D, Bird TD, Nixon RR, Ball MJ, DeCarli C, Bugiani O, Tagliavini F, Benson MD, Ghetti B
Am J Pathol 2001 Jun;158(6):2201-7. | Medline |
| Text source | HTML full text |
| Point mutation | Q212P (True positive) | |
| Reference #4 | Mastrangelo P, Serpell L, Dafforn T, Lesk A, Fraser P, Westaway D
FEBS Lett 2002 Dec 4;532(1-2):21-6. | Medline |
| Text source | HTML and PDF full texts |
| Point mutation | Q212P (True positive) | |
| Reference #5 | Mishra RS, Bose S, Gu Y, Li R, Singh N
J Alzheimers Dis 2003 Feb;5(1):15-23. | Medline |
| Text source | abstract |
| Point mutation | Q212P (True positive) | |
| Reference #6 | Gu Y, Hinnerwisch J, Fredricks R, Kalepu S, Mishra RS, Singh N
Neurobiol Dis 2003 Mar;12(2):133-49. | Medline |
| Text source | HTML full text |
| Point mutation | Q212P (True positive) | |
Reference #1 (Zuegg J et al.): Q212P
- The simulations showed some tendency for the highly conserved hydrophobic segment PrP(112-131) to adopt an (image)-helical conformation and for helix C to split at residues 212-213 , a known disease-associated mutation site (Q212P)
- The amino acid residues in black boxes are mutation sites known to be associated with inherited forms of PrP diseases in humans [CJD , D178N:129V (3) , V180I (3) , T183A (3) , E200K (3) , R208H (3) , V210I (3) , and M232R (3) ; GSS , P102L (3) , P105L (3) , A117V (3) , Y145Stop (3) , H187R (14) , F198S (3) , D202N (13) , Q212P (13) , and Q217R (3) ; FFI , D178N:129M (3) ; schizophrenia , N171S (12) ] , while in light gray boxes residues involved in some polymorphisms influencing these diseases are shown [M129V (3) , E219K (11) ]
- The simulations showed some tendency for the highly conserved hydrophobic segment PrP(112-131) to adopt an R-helical conformation and for helix C to split at residues 212-213 , a known disease-associated mutation site (Q212P)
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Reference #2 (Tagliavini F et al.): Q212P
- INTRODUCTION (image)TOP (image)ABSTRACT (image)INTRODUCTION (image)EXPERIMENTAL PROCEDURES (image)RESULTS (image)DISCUSSION (image)REFERENCES Gerstmann-Sträussler-Scheinker disease (GSS)1 is an adult-onset neurodegenerative disorder (1 , 2 ) that is inherited as an autosomal dominant trait and segregates with variant genotypes resulting from the combination of a pathogenic mutation (P102L , P105L , A117V , F198S , D202N , Q212P , and Q217R) and a common polymorphism at codon 129 (Met / Val) in the prion protein (PrP) gene (PRNP) (3-9 )
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Reference #3 (Piccardo P et al.): Q212P
- 3 GSS is caused by mutations P102L , P105L , A117V , G131V , F198S , D202N , Q212P , and Q217R in PRNP
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Reference #4 (Mastrangelo P et al.): Q212P
- Since the remaining GSS mutations (G131V , H178R , F198S , D202N , Q212P and Q217R) do not result in the creation of amino acid residues that are also conserved in Dpl , the hypothesis that GSS PRNP alleles result in PrPC molecules more Dpl-like than wt PrPC was rejected
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Reference #5 (Mishra RS et al.): Q212P
- To further clarify these mechanisms , we investigated the biogenesis of mutant PrP V203I and E211Q associated with Creutzfeldt-Jakob disease , and PrP Q212P associated with Gerstmann-Straussler-Scheinker syndrome in neuroblastoma cells
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Reference #6 (Gu Y et al.): Q212P
- Examples include PrP178N associated with familial Creutzfeldt Jakob disease (CJD) and fatal familial insomnia that accumulates in aggresome-like structures in the cytosol of COS cells (Ma and Lindquist 1999 and Ma and Lindquist 2001 ) , a PrP217R form that fails to acquire the GPI anchor and is degraded by proteasomes (Jin et al. , 2000 ) , and mutant PrPs V203I , E211Q , and Q212P associated with familial CJD and GSS that form aggresome-like structures in the cytosol of transfected neuroblastoma cells (Mishra et al. , in press )
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2005, PrionDB.
cmbi.ru.nl), 22-Aug-2005