Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Eric L. Bell"'
Publikováno v:
Cell Reports, Vol 17, Iss 3, Pp 809-820 (2016)
The enhancer landscape is dramatically restructured as naive preimplantation epiblasts transition to the post-implantation state of primed pluripotency. A key factor in this process is Otx2, which is upregulated during the early stages of this transi
Externí odkaz:
https://doaj.org/article/41073b814cba4fd8995271518bee3ab1
Autor:
Petra Simic, Eric O. Williams, Eric L. Bell, Jing Jing Gong, Michael Bonkowski, Leonard Guarente
Publikováno v:
Cell Reports, Vol 3, Iss 4, Pp 1175-1186 (2013)
The epithelial-to-mesenchymal transition (EMT) is important for the development of cancer metastases and organ fibrosis, conditions prevalent in aging. Because sirtuins affect the pathology of aging, we tested the effect of SirT1 on EMT. Reduced SIRT
Externí odkaz:
https://doaj.org/article/73d53392cf324778b58da00d7df77e7c
Publikováno v:
Trends in Molecular Medicine. 29:152-172
Adenosine triphosphate (ATP)-binding cassette (ABC) transporters are a 48-member superfamily of membrane proteins that actively transport a variety of biological substrates across lipid membranes. Their functional diversity defines an expansive invol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd7abe7f4ed4225e463d9aad8748ea20
https://doi.org/10.1016/j.molmed.2022.11.001
https://doi.org/10.1016/j.molmed.2022.11.001
Autor:
Gregory Stephanopoulos, Matthew G. Vander Heiden, Aria F. Olumi, Michael N. Pollak, John Blenis, Leonard Guarente, Lewis C. Cantley, Marie Jose Blouin, Akash Patnaik, Alfredo Csibi, Gary Bellinger, Matthias Schwab, Jared R. Mayers, Brian Fiske, Gregory J. Wirth, Shawn M. Davidson, Mark A. Keibler, Eric L. Bell, Sarah-Maria Fendt
Metformin inhibits cancer cell proliferation, and epidemiology studies suggest an association with increased survival in patients with cancer taking metformin; however, the mechanism by which metformin improves cancer outcomes remains controversial.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4536ff225804a4ce53cfb8506478efac
https://doi.org/10.1158/0008-5472.c.6504660.v1
https://doi.org/10.1158/0008-5472.c.6504660.v1
Autor:
Ross Fredenburg, Matthew M. Goddeeris, Jennifer K Truong, Effie Tozzo, Dominique Stickens, Robert W. Shine, Eric L. Bell, Peter Dwyer, Lyndsay Olson
Publikováno v:
Mitochondrion. 46:51-58
Duchenne muscular dystrophy (DMD) is a recessive, fatal X-linked disease that is characterized by progressive skeletal muscle wasting due to the absence of dystrophin, which is an a essential protein that bridges the inner cytoskeleton and extra-cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c48a8f8c9081cb3f6797bc8e3393b4c
https://doi.org/10.1016/j.mito.2018.02.006
https://doi.org/10.1016/j.mito.2018.02.006
Autor:
Bharat Lagu, Eric L. Bell, Effie Tozzo, Nirbhay Kumar Tiwari, Andrew Basinski, Arthur F. Kluge, Matthew M. Goddeeris, Ramesh S. Senaiar, Narasimha Rao Krishnamurthy, Ross Fredenburg, Sunil Kumar Panigrahi, Michael A. Patane, Mahaboobi Jaleel, Taisuke Takahashi, Peter Dwyer
Publikováno v:
ACS Medicinal Chemistry Letters. 9:935-940
The X-ray structure of the previously reported PPARδ modulator 1 bound to the ligand binding domain (LBD) revealed that the amide moiety in 1 exists in the thermodynamically disfavored cis-amide orientation. Isosteric replacement of the cis-amide wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0663921ac4e0f062d40544f2aece30db
https://doi.org/10.1021/acsmedchemlett.8b00287
https://doi.org/10.1021/acsmedchemlett.8b00287
Autor:
Mahaboobi Jaleel, Matthew M. Goddeeris, Ramesh S. Senaiar, Peter Dwyer, Eric L. Bell, Sunil Kumar Panigrahi, Ross Fredenburg, Bharat Lagu, Narasimha Rao Krishnamurthy, Andrew Basinski, Michael A. Patane, Nirbhay Kumar Tiwari, Taisuke Takahashi, Effie Tozzo, Arthur F. Kluge
[Image: see text] The X-ray structure of the previously reported PPARδ modulator 1 bound to the ligand binding domain (LBD) revealed that the amide moiety in 1 exists in the thermodynamically disfavored cis-amide orientation. Isosteric replacement o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6579f783424d3bdf0cdce8fc284c2809
https://europepmc.org/articles/PMC6580794/
https://europepmc.org/articles/PMC6580794/
Autor:
Jacob Lloyd, Fuad Abdulla, Eric L. Bell, Gregory M. Vercellotti, Domi Stickens, Zachary Monroe Kiser, Chunsheng Chen, Margaret Biddle, John D. Belcher, Lyndsay Olson, Julia Nguyen
Publikováno v:
Blood. 134:983-983
In sickle cell disease (SCD) excessive release of Hb and heme into the vasculature can activate innate immune toll-like receptor 4 (TLR4) signaling in the vasculature leading to inflammation and vaso-occlusion. Heme-mediated TLR4 signaling can be int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::191a2d07dab43d9400e51ffab7ff54bf
https://doi.org/10.1182/blood-2019-127300
https://doi.org/10.1182/blood-2019-127300
Autor:
James P. White, Rafael de Cabo, Magdalene K. Montgomery, David A. Sinclair, Ana P. Gomes, Eric L. Bell, Evi M. Mercken, Christiane D. Wrann, Javid Moslehi, Basil P. Hubbard, Luis A. Rajman, Carlos M. Palmeira, Nathan L. Price, Anabela P. Rolo, João S. Teodoro, Alvin J. Y. Ling, Nigel Turner
Publikováno v:
Cell. 155(7):1624-1638
SUMMARY Ever since eukaryotes subsumed the bacterial ancestor of mitochondria, the nuclear and mitochondrial genomes have had to closely coordinate their activities, as each encode different subunits of the oxidative phosphorylation (OXPHOS) system.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d0dc8ff52c52f0dba0cf92d225324eb
Autor:
Dena E. Cohen, Kenneth S. Kendler, Eric L. Bell, Kelli B. Pointer, Sven Bergmann, Takeshi Otowa, Abhirup Das, John M. Asara, Justin P. Rubio, Leonard Guarente, Sergiy Libert, Xiangning Chen, John M. Hettema, Edwin J. C. G. van den Oord, Martin Preisig, Karen Kapur
Publikováno v:
Cell. 147(7):1459-1472
SummarySIRT1 is a NAD+-dependent deacetylase that governs a number of genetic programs to cope with changes in the nutritional status of cells and organisms. Behavioral responses to food abundance are important for the survival of higher animals. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd8e1b7f5a291516248c4ff8e1b22c30