Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Pascal Krotee"'
Autor:
Pascal Krotee, Jose A Rodriguez, Michael R Sawaya, Duilio Cascio, Francis E Reyes, Dan Shi, Johan Hattne, Brent L Nannenga, Marie E Oskarsson, Stephan Philipp, Sarah Griner, Lin Jiang, Charles G Glabe, Gunilla T Westermark, Tamir Gonen, David S Eisenberg
Publikováno v:
eLife, Vol 6 (2017)
hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic β-cells, leading us to determine the structure and cytot
Externí odkaz:
https://doaj.org/article/f0207c5ac18e49debe0019586fe78051
Autor:
Michael R. Sawaya, Pascal Krotee, Paul M. Seidler, Dan Shi, Charles G. Glabe, Sarah Griner, Lorena Saelices, David Eisenberg, Kevin A. Murray, Duilio Cascio, Ji Lee, Stephan Philipp, Tamir Gonen, Lin Jiang, Jose Rodriguez
Publikováno v:
The Journal of biological chemistry, vol 293, iss 8
Amyloid-β (Aβ) and human islet amyloid polypeptide (hIAPP) aggregate to form amyloid fibrils that deposit in tissues and are associated with Alzheimer's disease (AD) and type II diabetes (T2D), respectively. Individuals with T2D have an increased r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc55315e7d7fe3dd55c6418227010826
https://escholarship.org/uc/item/6368r0x1
https://escholarship.org/uc/item/6368r0x1
Autor:
David Eisenberg, Pascal Krotee, Stephan Philipp, Michael R. Sawaya, Jose A. Rodriguez, Tamir Gonen, Marie E. Oskarsson, Gunilla T. Westermark, Duilio Cascio, Sarah Griner, Dan Shi, Charles G. Glabe, Brent L. Nannenga, Francis E. Reyes, Johan Hattne, Lin Jiang
Publikováno v:
eLife
eLife, Vol 6 (2017)
eLife, Vol 6 (2017)
hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic β-cells, leading us to determine the structure and cytot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fad9cbcca775396d40dce43913666132
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-316042
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-316042
Autor:
Michael R. Sawaya, Lin Jiang, Stephan Philipp, Sarah Griner, Jose A. Rodriguez, David Eisenberg, Dan Shi, Gunilla T. Westermark, Pascal Krotee, Charles G. Glabe, Duilio Cascio, Marie E. Oskarsson, Tamir Gonen, Johan Hattne, Francis E. Reyes, Brent L. Nannenga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f2ff67c8a0d43506d6d2be6f7e6dc50
https://doi.org/10.7554/elife.19273.026
https://doi.org/10.7554/elife.19273.026
Autor:
Thomas G. Graeber, Carolina Espindola Camacho, Siavash K. Kurdistani, Wen Gu, Brian Gardner, Iman Saramipoor Behbahan, Ingo K. Mellinghoff, Lee Goodglick, Steven M. Dubinett, David Chia, Nicholas A. Graham, Heather R. Christofk, Steve Horvath, Susan E. Critchlow, Mohammed Alavi, Lora Bagryanova, Sara A. Hurvitz, Pascal Krotee, Erin L. Maresh, Daniel Braas, Candice Sun Hong, Vei Mah
Publikováno v:
Cell reports, vol 14, iss 7
Hong, CS; Graham, NA; Gu, W; Espindola Camacho, C; Mah, V; Maresh, EL; et al.(2016). MCT1 Modulates Cancer Cell Pyruvate Export and Growth of Tumors that Co-express MCT1 and MCT4. Cell Reports, 14(7), 1590-1601. doi: 10.1016/j.celrep.2016.01.057. UCLA: Retrieved from: http://www.escholarship.org/uc/item/92p5w832
Hong, CS; Graham, NA; Gu, W; Espindola Camacho, C; Mah, V; Maresh, EL; et al.(2016). MCT1 Modulates Cancer Cell Pyruvate Export and Growth of Tumors that Co-express MCT1 and MCT4. Cell Reports, 14(7), 1590-1601. doi: 10.1016/j.celrep.2016.01.057. UCLA: Retrieved from: http://www.escholarship.org/uc/item/92p5w832
© 2016 The Authors. Monocarboxylate transporter 1 (MCT1) inhibition is thought to block tumor growth through disruption of lactate transport and glycolysis. Here, we show MCT1 inhibition impairs proliferation of glycolytic breast cancer cells co-exp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::561d2c663223b9c9462134d4401b6775
https://escholarship.org/uc/item/92p5w832
https://escholarship.org/uc/item/92p5w832
Autor:
Nichole E. LaPointe, Michael T. Bowers, David B. Teplow, Pascal Krotee, David Eisenberg, Sarah Quan, Brittany Ulrich, Joan-Emma Shea, Thanh D. Do, Stuart C. Feinstein, Rebecca Nelson, Eric Y. Hayden
Publikováno v:
Journal of the American Chemical Society, vol 138, iss 2
In order to evaluate potential therapeutic targets for treatment of amyloidoses such as Alzheimer’s disease (AD), it is essential to determine the structures of toxic amyloid oligomers. However, for the amyloid β-protein peptide (Aβ), thought to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::276932668262d1800df625cd16a484ff
https://escholarship.org/uc/item/2dz88741
https://escholarship.org/uc/item/2dz88741
Autor:
Marie E. Oskarsson, Gunilla T. Westermark, Pascal Krotee, Michael R. Sawaya, Jose A. Rodriguez, Johan Hattne, Tamir Gonen, Francis E. Reyes, Dan Shi, David Eisenberg, Lin Jiang, Duilio Cascio, Brent L. Nannenga
Publikováno v:
Biophysical Journal. 112:14a
The Cryo-EM Method Micro-ED Structure Determination of Type II Diabetes-Related Protein Segments
Autor:
Robyn M. Kaake, Pascal Krotee, Vishal R. Patel, Thomas Whisenant, Lan Huang, William Gordon, Lee Bardwell, Elizabeth A. Gordon, Michael Zeller, Pierre Baldi
Publikováno v:
Cellular signalling, vol 25, iss 12
Gordon, EA; Whisenant, TC; Zeller, M; Kaake, RM; Gordon, WM; Krotee, P; et al.(2013). Combining docking site and phosphosite predictions to find new substrates: Identification of smoothelin-like-2 (SMTNL2) as a c-Jun N-terminal kinase (JNK) substrate. Cellular Signalling, 25(12), 2518-2529. doi: 10.1016/j.cellsig.2013.08.004. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4qw9c50p
Gordon, EA; Whisenant, TC; Zeller, M; Kaake, RM; Gordon, WM; Krotee, P; et al.(2013). Combining docking site and phosphosite predictions to find new substrates: Identification of smoothelin-like-2 (SMTNL2) as a c-Jun N-terminal kinase (JNK) substrate. Cellular Signalling, 25(12), 2518-2529. doi: 10.1016/j.cellsig.2013.08.004. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4qw9c50p
Specific docking interactions between mitogen-activated protein kinases (MAPKs), their regulators, and their downstream substrates, are crucial for efficient and accurate signal transmission. To identify novel substrates of the c-Jun N-terminal kinas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2141c1b7733606ff4249e4ea1e39973
https://escholarship.org/uc/item/4qw9c50p
https://escholarship.org/uc/item/4qw9c50p
Autor:
S.H. Choi, Trias Thireou, J.P. Fuhrer, Spiros D. Dimitratos, Brigida Rusconi, F. Grun, Daniel F. Woods, A.C. Maranhao, Elias Eliopoulos, Osvaldo Marinotti, Pascal Krotee, Marika F. Walter
Publikováno v:
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics; Vol 1824
The major malaria vector in Sub-Saharan Africa is the Anopheles gambiae mosquito. This species is a key target of malaria control measures. Mosquitoes find humans primarily through olfaction, yet the molecular mechanisms associated with host-seeking