Page last updated: 2024-10-21

urea and Dementias, Transmissible

urea has been researched along with Dementias, Transmissible in 5 studies

pseudourea: clinical use; structure
isourea : A carboximidic acid that is the imidic acid tautomer of urea, H2NC(=NH)OH, and its hydrocarbyl derivatives.

Research Excerpts

ExcerptRelevanceReference
"Transmissible spongiform encephalopathies are associated with accumulation of PrP(Sc), a conformer of a cellular protein called PrP(C)."1.31Binding of disease-associated prion protein to plasminogen. ( Aguzzi, A; Fischer, MB; Parizek, P; Roeckl, C; Schwarz, HP, 2000)
"The main hypothesis for prion diseases proposes that the cellular protein (PrP(C)) can be altered into a misfolded, beta-sheet-rich isoform (PrP(Sc)), which in most cases undergoes aggregation."1.31DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. ( Brentani, RR; Cordeiro, Y; Foguel, D; Juliano, L; Juliano, MA; Machado, F; Silva, JL, 2001)

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (60.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Sweeting, B2
Brown, E1
Khan, MQ2
Chakrabartty, A2
Pai, EF2
Mulligan, VK1
Arslan, PE1
Cashman, NR1
Cordeiro, Y2
Lima, LM1
Gomes, MP1
Foguel, D2
Silva, JL2
Fischer, MB1
Roeckl, C1
Parizek, P1
Schwarz, HP1
Aguzzi, A1
Machado, F1
Juliano, L1
Juliano, MA1
Brentani, RR1

Clinical Trials (1)

Trial Overview

TrialPhaseEnrollmentStudy TypeStart DateStatus
The Role of the Coagulation Pathway at the Synapse in Prion Diseases[NCT02480725]50 participants (Anticipated)Observational2015-06-30Not yet recruiting
[information is prepared from clinicaltrials.gov, extracted Sep-2024]

Other Studies

5 other studies available for urea and Dementias, Transmissible

ArticleYear
N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.
    PloS one, 2013, Volume: 8, Issue:5

    Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Asparagine; Circular Dichroism; Cricetinae; Hydroge

2013
Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP.
    Proceedings of the National Academy of Sciences of the United States of America, 2010, Nov-16, Volume: 107, Issue:46

    Topics: Amino Acid Motifs; Amino Acids; Animals; Cell Death; Circular Dichroism; Crystallography, X-Ray; Dis

2010
Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ANS).
    The Journal of biological chemistry, 2004, Feb-13, Volume: 279, Issue:7

    Topics: Anilino Naphthalenesulfonates; Animals; Circular Dichroism; Cricetinae; Dose-Response Relationship,

2004
Binding of disease-associated prion protein to plasminogen.
    Nature, 2000, Nov-23, Volume: 408, Issue:6811

    Topics: Animals; Blotting, Western; Guanidine; Humans; Magnetics; Mice; Mice, Inbred C57BL; Mice, Transgenic

2000
DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation.
    The Journal of biological chemistry, 2001, Dec-28, Volume: 276, Issue:52

    Topics: Animals; Circular Dichroism; DNA; DNA-Binding Proteins; Humans; Nucleic Acid Conformation; Oligonucl

2001