Výsledky vyhledávání - "Kartika Widjaja"

Familial Parkinson's point mutation abolishes multiple system atrophy prion replication

Autor: Steven H. Olson, Sabeen A. Kazmi, Smita S. Patel, Kartika Widjaja, Daniel A. Mordes, Amanda L. Woerman, Atsushi Aoyagi, Stanley B. Prusiner, Abby Oehler

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 115(2)

Significance In Parkinson’s disease (PD) and multiple system atrophy (MSA), the accumulation and spread of α-synuclein prions leads to the progressive degeneration seen in patients. These diseases are thought to arise from unique conformations of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2136521e9b972dbe1e9bd5f1ddef738f
https://pubmed.ncbi.nlm.nih.gov/29279394

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Antiprion compounds that reduce PrPSc levels in dividing and stationary-phase cells

Autor: Joel R. Gever, Matthew P. Jacobson, Kartika Widjaja, Satish Rao, Adam R. Renslo, Sina Ghaemmaghami, Stanley B. Prusiner, John J. Irwin, B. Michael Silber, Zhe Li, Alejandra Gallardo-Godoy

Publikováno v: Bioorganic & Medicinal Chemistry. 21:7999-8012

During prion diseases, a normally benign, host protein, denoted PrPC, undergoes alternative folding into the aberrant isoform, PrPSc. We used ELISA assays to identify and confirm hits in order to develop leads that reduce PrPSc in prion-infected divi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6353c6d30fcbf676bd07b8d3f4d9c35d
https://doi.org/10.1016/j.bmc.2013.09.022

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Propagation of prions causing synucleinopathies in cultured cells

Autor: William W. Seeley, Smita S. Patel, Atsushi Aoyagi, Amanda L. Woerman, Thomas C. Südhof, Joel C. Watts, Zuzana Krejciova, Kurt Giles, Daniel A. Mordes, Jan Stöhr, David W. Sanders, Steve M. Gentleman, Ryan Rampersaud, Kartika Widjaja, Takao Ohyama, Abby Oehler, Lefkos T. Middleton, Stanley B. Prusiner, Marc I. Diamond

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 112, iss 35
Woerman, AL; Stöhr, J; Aoyagi, A; Rampersaud, R; Krejciova, Z; Watts, JC; et al.(2015). Propagation of prions causing synucleinopathies in cultured cells. Proceedings of the National Academy of Sciences of the United States of America, 112(35), E4949-E4958. doi: 10.1073/pnas.1513426112. UCSF: Retrieved from: http://www.escholarship.org/uc/item/4mg1p0r6

© 2015, National Academy of Sciences. All rights reserved. Increasingly, evidence argues that many neurodegenerative diseases, including progressive supranuclear palsy (PSP), are caused by prions, which are alternatively folded proteins undergoing s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b51bd859069006b22593b3cf83b15aae
https://escholarship.org/uc/item/4mg1p0r6

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An integrated strategy for the discovery of drug targets by the analysis of protein–protein interactions

Publikováno v: International Journal of Mass Spectrometry. 238:119-130

Proteomics-based technologies have the potential to accelerate the development of drugs, but such technologies must be well integrated in order to have a positive impact. We describe, herein, a multi-step process for the discovery of protein–protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9666b69be07da92afc0c60bb54db68e8
https://doi.org/10.1016/j.ijms.2003.12.039

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Expression screen by enzyme-linked immunofiltration assay designed for high-throughput purification of affinity-tagged proteins

Autor: David R. Conklin, J. Jay Boniface, Justin Savage, Thomas Zarembinski, Xinghua Long, Kartika Widjaja, Vladimir Kery, Moritz von Rechenberg, Yew-Seng J. Ho, B. Kelly Blake

Publikováno v: Analytical Biochemistry. 317:255-258

High-throughput purification of affinity-tagged fusion proteins is currently one of the fastest developing areas of molecular proteomics. A prerequisite for success in protein purification is sufficient soluble protein expression of the target protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eef968195b55cbeb87d8e63c23282d3f
https://doi.org/10.1016/s0003-2697(03)00116-7

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Novel compounds lowering the cellular isoform of the human prion protein in cultured human cells

Autor: Zhe Li, Casper Wong, Joel R. Gever, Kurt Giles, Kartika Widjaja, Satish Rao, Matthew P. Jacobson, Yevgeniy Freyman, Adam R. Renslo, Manuel Elepano, Stanley B. Prusiner, John J. Irwin, B. Michael Silber

Publikováno v: Bioorganic & medicinal chemistry, vol 22, iss 6
Silber, BM; Gever, JR; Rao, S; Li, Z; Renslo, AR; Widjaja, K; et al.(2014). Novel compounds lowering the cellular isoform of the human prion protein in cultured human cells. Bioorganic and Medicinal Chemistry, 22(6), 1960-1972. doi: 10.1016/j.bmc.2014.01.001. UCSF: Retrieved from: http://www.escholarship.org/uc/item/5r2396fv

Purpose: Previous studies showed that lowering PrPC concomitantly reduced PrPSc in the brains of mice inoculated with prions. We aimed to develop assays that measure PrPC on the surface of human T98G glioblastoma and IMR32 neuroblastoma cells. Using

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c464fd6f59b5218affb72b4a8c4a6d8
https://escholarship.org/uc/item/5r2396fv

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Towards optimization of arylamides as novel, potent, and brain-penetrant antiprion lead compounds

Autor: Joel R. Gever, Zhe Li, Stanley B. Prusiner, Kartika Widjaja, Satish Rao, B. Michael Silber

Publikováno v: Li, Z; Rao, S; Gever, JR; Widjaja, K; Prusiner, SB; & Michael Silber, B. (2013). Towards optimization of arylamides as novel, potent, and brain-penetrant antiprion lead compounds. ACS Medicinal Chemistry Letters, 4(7), 647-650. doi: 10.1021/ml300454k. UCSF: Retrieved from: http://www.escholarship.org/uc/item/85p0892q

The prion diseases caused by PrPSc, an alternatively folded form of the cellular prion protein (PrPC), are rapidly progressive, fatal, and untreatable neurodegenerative disorders. We employed HTS ELISA assays to identify compounds that lower the leve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79c9507677646bb264dc6cc7f70dcf83
http://www.escholarship.org/uc/item/85p0892q

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2-Aminothiazoles with improved pharmacotherapeutic properties for treatment of prion disease

Autor: Satish Rao, Joel R. Gever, Zhe Li, Clifford Bryant, Stanley B. Prusiner, Elena Dolghih, Alejandra Gallardo-Godoy, Manuel Elepano, Adam R. Renslo, Matthew P. Jacobson, Kartika Widjaja, B. Michael Silber

Publikováno v: ChemMedChem, vol 8, iss 5
Li, Z; Silber, BM; Rao, S; Gever, JR; Bryant, C; Gallardo-Godoy, A; et al.(2013). 2-Aminothiazoles with Improved Pharmacotherapeutic Properties for Treatment of Prion Disease. ChemMedChem, 8(5), 847-857. doi: 10.1002/cmdc.201300007. UCSF: Retrieved from: http://www.escholarship.org/uc/item/33t9f431

Recently, we described the aminothiazole lead (4-biphenyl-4-ylthiazol-2-yl)-(6-methylpyridin-2-yl)-amine (1), which exhibits many desirable properties, including excellent stability in liver microsomes, oral bioavailability of ∼40%, and high exposu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c0f661215216cd16384f92e82bc0d7f
https://escholarship.org/uc/item/33t9f431

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Discovery and Preliminary Structure–Activity Relationship of Arylpiperazines as Novel, Brain-Penetrant Antiprion Compounds

Autor: Stanley B. Prusiner, Kartika Widjaja, Zhe Li, Joel R. Gever, B. Michael Silber, Satish Rao

Publikováno v: Li, Z; Gever, JR; Rao, S; Widjaja, K; Prusiner, SB; & Silber, BM. (2013). Discovery and preliminary structure-activity relationship of arylpiperazines as novel, brain-penetrant antiprion compounds. ACS Medicinal Chemistry Letters, 4(4), 397-401. doi: 10.1021/ml300472n. UCSF: Retrieved from: http://www.escholarship.org/uc/item/6zc5651q

Creutzfeldt-Jakob disease and kuru in humans, BSE in cattle, and scrapie in sheep are fatal neurodegenerative disorders. Such illnesses are caused by the conversion and accumulation of a misfolded pathogenic isoform (termed PrPSc) of a normally benig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bb45bdc4c4156a02881f12edf109083
https://europepmc.org/articles/PMC3704178/

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Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure

Autor: Tina Tran, Siddhartha Mitra, Jason Miller, Earl E. Rutenber, Karl H. Weisgraber, Danny M. Hatters, Dean Taylor, Kartika Widjaja, Kenneth Cheung, Yvonne M. Newhouse, Clare Peters-Libeu, Luis A. Mosquera, Steven Finkbeiner, Preethi Krishnan, Elizabeth Brooks, Montserrat Arrasate

Publikováno v: Journal of molecular biology, vol 421, iss 4-5
Peters-Libeu, C; Miller, J; Rutenber, E; Newhouse, Y; Krishnan, P; Cheung, K; et al.(2012). Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure. Journal of Molecular Biology, 421(4-5), 587-600. doi: 10.1016/j.jmb.2012.01.034. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/6tr8t4jw

Abnormal polyglutamine (polyQ) tracts are the only common feature in nine proteins that each cause a dominant neurodegenerative disorder. In Huntington's disease, tracts longer than 36 glutamines in the protein huntingtin (htt) cause degeneration. In

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ccdc082ba23917bc657b0ed36d874c0
https://europepmc.org/articles/PMC3358578/

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