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 105 were found are listed after the table.
| Protein | PRIO_HUMAN (P04156) Gene: PRNP (other point mutations) | Swiss-Prot
Cross-reference table
Family page |
| Position | P105 | |
| 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 105 in Mammalian prion proteins family
Position 105 in Prion proteins (PRP, PRNP) family
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| Reference #1 | Yamada M, Itoh Y, Inaba A, Wada Y, Takashima M, Satoh S, Kamata T, Okeda R, Kayano T, Suematsu N, Kitamoto T, Otomo E, Matsushita M, Mizusawa H
Neurology 1999 Jul 13;53(1):181-8. | Medline |
| Text source | HTML and PDF full texts |
| Point mutation | P105L (True positive) | |
| Reference #2 | Zuegg J, Gready JE
Biochemistry 1999 Oct 19;38(42):13862-76. | Medline |
| Text source | HTML and PDF full texts |
| Point mutation | P105L (True positive) | |
| Reference #3 | 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 | P105L (True positive) | |
| Reference #4 | 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 | P105L (True positive) | |
| Reference #5 | Spielhaupter C, Schatzl HM
J Biol Chem 2001 Nov 30;276(48):44604-12. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (True positive) | |
| Reference #6 | Kovacs GG, Trabattoni G, Hainfellner JA, Ironside JW, Knight RS, Budka H
J Neurol 2002 Nov;249(11):1567-82. | Medline |
| Text source | abstract |
| Point mutation | P105L (True positive) | |
| Reference #7 | 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 | P105L (True positive) | |
| Reference #8 | Cohen E, Taraboulos A
EMBO J 2003 Feb 3;22(3):404-17. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (Not yet checked) | |
| Reference #9 | Harris DA
Br Med Bull 2003;66:71-85. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (Not yet checked) | |
| Reference #10 | Gambetti P, Kong Q, Zou W, Parchi P, Chen SG
Br Med Bull 2003;66:213-39. | Medline |
| Text source | HTML full text |
| Point mutation | P105T (True positive) | |
| Reference #11 | Apetri AC, Surewicz K, Surewicz WK
J Biol Chem 2004 Apr 23;279(17):18008-14. Epub 2004 Feb 2. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (True positive) | |
| Reference #12 | Ishida C, Okino S, Kitamoto T, Yamada M
J Neurol Neurosurg Psychiatry 2005 Mar;76(3):325-9. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (Not yet checked) | |
| Reference #13 | Tateishi J, Kitamoto T, Hoque MZ, Furukawa H
Neurology 1996 Feb;46(2):532-7. | Medline |
| Text source | abstract |
| Point mutation | P105L (True positive) | |
| Reference #14 | Parchi P, Chen SG, Brown P, Zou W, Capellari S, Budka H, Hainfellner J, Reyes PF, Golden GT, Hauw JJ, Gajdusek DC, Gambetti P
Proc Natl Acad Sci U S A 1998 Jul 7;95(14):8322-7. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (Not yet checked) | |
| Reference #15 | Yamada M, Tomimitsu H, Yokota T, Tomi H, Sunohara N, Mukoyama M, Itoh Y, Suematsu N, Otomo E, Okeda R, Matsushita M, Mizusawa H
Neurology 1999 Jan 15;52(2):260-5. | Medline |
| Text source | HTML full text |
| Point mutation | P105L (Not yet checked) | |
Reference #1 (Yamada M et al.): P105L
- Alert me when: new articles cite this article Download to Citation Manager Neurology 1999 ; 53:181 © 1999 American Academy of Neurology ------------------------------------------------------------------------ Articles An inherited prion disease with a PrP P105L mutation Clinicopathologic and PrP heterogeneity M
- 1 A variant form of GSS associated with a missense mutation at codon 105 (P105L ; GSS105) was first described in 1993 in Japanese patients
- As for the allelic distribution of the codon 129 polymorphism , the Val codon was coupled with the P105L mutation
- Kitamoto T , Amano N , Terao Y , et al. A new inherited prion disease (PrP-P105L mutation) showing spastic paraparesis
- A case of variant Gerstmann-Sträussler-Scheinker disease with the mutation of codon P105L
- An inherited prion disease with a PrP P105L mutation Clinicopathologic and PrP heterogeneity M
- NEUROLOGY 1999 ; 53:181188 Human prion diseases are classified into three categories: infectious prion diseases , inherited prion diseases , and prion diseases of unknown etiology.1 Inherited prion diseases are found to be associated with mutations of the prion protein (PrP) gene , and they present with several clinical phenotypes , including classic and variant forms of GerstmannStra¨usslerScheinker disease (GSS) , familial CreutzfeldtJakob disease (CJD) , and familial fatal insomnia.1 A variant form of GSS associated with a missense mutation at codon 105 (P105L ; GSS105) was first described in 1993 in Japanese patients.2 , 3 Clinically , GSS105 has been reported to be characterized by spastic paraparesis and dementia , 2 , 3 and is distinct from the classic form of GSS associated with a missense mutation at codon 102 (P102L) , which is characterized by cerebellar ataxia and dementia.4 , 5 GSS105 has been referred to as the 'spastic paraparesis' type.3 Recently we experienced an autopsy case of GSS105 from a Japanese family in which we described the original patient.2 , 6 Despite the identical codon 105 mutation and codon 129 polymorphism of the PrP gene , we found remarkable differences in clinical and neuropathologic phenotypes , and detergentinsoluble PrP fragments between the family members
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Reference #2 (Zuegg J et al.): P105L
- 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) ]
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Reference #3 (Tagliavini F et al.): P105L
- 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 #4 (Piccardo P et al.): P105L
- 3 GSS is caused by mutations P102L , P105L , A117V , G131V , F198S , D202N , Q212P , and Q217R in PRNP
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Reference #5 (Spielhaupter C et al.): P105L
- The location of the putative SH3 recognition motif XPXXP is indicated by an asterisk , and the two known pathologic mutations P102L and P105L in this region are indicated with arrowheads
- Grb2 coprecipitates with wild type PrP-(90-231) (lane 9) as well as with the constructs bearing the GSS point mutations P102L (lane 10) and P105L (lane 11)
- Such a site is present in wild type PrP at position 101-105 , but absent in two mutations leading to Gerstmann-Sträussler-Scheinker syndrome (GSS) in humans (P102L and P105L , respectively) (1 )
- P102L and P105L both result in GSS with slightly different clinicopathologic patterns (50 )
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Reference #6 (Kovacs GG et al.): P105L
- P105L , D178N-129M , T183A)
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Reference #7 (Mastrangelo P et al.): P105L
- In the case of GSS it was not possible to undertake meaningful analyses for the causative P102L , P105L and A117V mutations as these are located within an area of PrP that has no cognate in Dpl [16 ]
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Reference #8 (Cohen E et al.): P105L
- Because there is an abundance of prolines in PrP , and since two proline substitutions (P102L and P105L) are linked with familial GSS (Hsiao et al. , 1989 ; Yamazaki et al. , 1999 ) , we wondered whether cis-trans isomerization of peptidylprolyl bonds might participate either in the folding of PrP C or in its disposal
- (B) Model for the generation of misfolded PrP by wtPrP and by the P102L and P105L mutants
- Upper panel: in all cases the majority of both wild-type and mutant (P102L and P105L) PrP is formed with predominantly trans X-Pro (or trans X-Leu) peptide bonds (which are energetically favored)
- The substitutions P102L and P105L are linked , separately , to familial GSS (Hsiao et al. , 1989 ; Yamazaki et al. , 1999 ) , but the etiology is poorly understood
- Although this could apply to any of the X-Pro bonds in mature wild-type huPrP , it is tempting to focus on P102 and P105 , the two proline residues that are linked to familial GSS [P102L (Hsiao et al. , 1989 ) ; P105L (Yamazaki et al. , 1999 )]
- It is thus plausible that P102L- and P105L-PrP are sometimes (even if rarely) synthesized with cis X-Leu bonds at positions 102 or 105
- (i) It forecasts that while a small number of P102L or P105L PrP molecules may acquire prion-like properties , the vast majority of these mutant molecules will form in the native conformation
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Reference #9 (Harris D et al.): P105L
- However , mutations within or near the transmembrane domain , including A117V and P105L mutations linked to GSS as well as several `artificial’ mutations not seen in human patients , increase the relative proportion of CtmPrP to as much as 20-30% of the total59 , 61 , 63 -65
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Reference #11 (Apetri AC et al.): P105L
- A similar behavior would be expected for prion protein variants P105L and , likely , A117V
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Reference #12 (Ishida C et al.): P105L
- Methods: Eight patients with prion diseases were examined: three with sporadic Creutzfeldt-Jakob disease (sCJD) , two with dural graft associated CJD (dCJD) , one with Gerstmann-Sträussler-Scheinker disease (GSS) with a PrP P102L mutation (GSS102) , and two with a P105L mutation (GSS105)
- METHODS (image)TOP (image)ABSTRACT (image)METHODS (image)RESULTS (image)DISCUSSION (image)REFERENCES Patients We studied eight patients with necropsy confirmed prion diseases: three with sCJD , two with dCJD , 11 , 12 one with GSS with a PrP P102L mutation (GSS102) , and two with a PrP P105L mutation (GSS105) (table 1(image) )
- (D) Patient 8 with GSS having a P105L mutation showed only plaque type PrP deposits
- Yamada M , Itoh Y , Inaba A , et al. An inherited prion disease with a PrP P105L mutation: clinicopathologic and PrP heterogeneity
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Reference #13 (Tateishi J et al.): P105L
- Hereditary cases with P102L , P105L , A117V , Y145stop , and insertions had different features but all demonstrated a long clinical duration and the presence of PrP plaques
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Reference #14 (Parchi P et al.): P105L
- Mizusawa An inherited prion disease with a PrP P105L mutation: Clinicopathologic and PrP heterogeneity Neurology , July 1 , 1999 ; 53(1): 181 - 181
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Reference #15 (Yamada M et al.): P105L
- We also compared the findings of GSS102 with those of another type of GSS associated with a missense mutation at codon 105 (P105L) of the PrP gene (GSS105)
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Reference #10 (Gambetti P et al.): P105T
- Q160Stop-129M103 , E196K-129M101 , V203I-129M101 , T188K103 , and probably P238S104 , T188R103 , 104 , and P105T (http: / / www.mad-cow.org / prion_point_ mutations.html ) display some signs of neurodegeneration
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2005, PrionDB.
cmbi.ru.nl), 22-Aug-2005