Results 51 to 60 of about 17,003 (187)

The role of EBNA binding proteins in cell transformation [PDF]

, 2013
Epstein - Barr virus (EBV) infects m ajority of the human population and maintains sub - cl inical infection . However , under certain conditions it is associated with several B - cell malignancies , such as Burkitt lymphoma ...
Darekar, Suhas
core   +1 more source

Calcium Channel Blocker Lacidipine Promotes Antitumor Immunity by Reprogramming Tryptophan Metabolism

Advanced Science, Volume 12, Issue 3, January 20, 2025.
The antihypertensive drug lacidipine, as a bifunctional modulator of the enzymatic activity and expression of indoleamine 2,3‐dioxygenase 1 (IDO1), targets calcium channels to inhibit (Protein Tyrosine 2 (Pyk2)‐Janus Kinase 1 (JAK1)‐calmodulin complex‐mediated IDO1 immunosuppression.
Yuwen Sheng, Chong Qiao, Zhonghui Zhang, Xiaoke Shi, Linhan Yang, Ruiying Xi, Jialing Yu, Wanli Liu, Guolin Zhang, Fei Wang   +9 more
wiley   +1 more source

Resetting of the Human Circadian Melatonin Rhythm by Ambient Hypoxia

Journal of Pineal Research, Volume 77, Issue 1, January 2025.
ABSTRACT Circadian clocks in the body drive daily cycles in physiology and behavior. A master clock in the brain maintains synchrony with the environmental day–night cycle and uses internal signals to keep clocks in other tissues aligned. Work in cell cultures uncovered cyclic changes in tissue oxygenation that may serve to reset and synchronize ...
Titiaan E. Post, Riccardo De Gioannis, Jan Schmitz, Martin Wittkowski, Tina Martin Schäper, Anna Wrobeln, Joachim Fandrey, Marie‐Therese Schmitz, Joseph S. Takahashi, Jens Jordan, Eva‐Maria Elmenhorst, Daniel Aeschbach   +11 more
wiley   +1 more source

The PAS-domain kinase PASKIN: a new sensor in energy homeostasis [PDF]

, 2018
.: The PAS domain kinase PASKIN, also termed PAS kinase or PASK, is an evolutionarily conserved potential sensor kinase related to the heme-based oxygen sensors of nitrogen-fixing bacteria.
Borter, E., Schläfli, P., Spielmann, P., Wenger, R.   +3 more
core  

Phytochemical Profiling, Acute Toxicity, and Hepatoprotective Effects of Anchusa Limbata in Thioacetamide‐Induced Liver Cirrhosis in Rats

Food Science &Nutrition, Volume 12, Issue 12, Page 10628-10645, December 2024.
The phytochemical profiling showed increased polyphenolic (129.2 mg GAE/g) and flavonoid (105.3 mg EQ/g extract) contents in methanolic extract of Anchusa limbata. The present of MEAL supplementation ameliorated TAA‐mediated hepatoxicity in rats by modulating several molecular mechanisms.
Khaled Abdul‐Aziz Ahmed, Ahmed A. J. Jabbar, Mohammed M. Hussein M. Raouf, Ayman M. Al‐Qaaneh, Rawaz Rizgar Hassan, Musher Ismael Salih, Ramzi A. Mothana, Gadah Abdulaziz Al‐Hamoud, Mahmood Ameen Abdulla, Sidgi Hasson, Parween Abdul‐samad Ismail   +10 more
wiley   +1 more source

Therapeutic potential of Parabacteroides distasonis in gastrointestinal and hepatic disease

MedComm, Volume 5, Issue 12, December 2024.
This review illustrate the metabolic network medicated by Parabacteroides distasonis and its role and action mechanism in gastrointestinal and hepatic disease. The natural components affecting Parabacteroides distasonis was summarized, which show the therapeutic potential for gastrointestinal and hepatic diseases. Abstract Increasing evidences indicate
Jingyi Duan, Qinmei Li, Yan Cheng, Weifeng Zhu, Hongning Liu, Fei Li   +5 more
wiley   +1 more source

Enzymatic functionalization of carbon-hydrogen bonds [PDF]

, 2011
The development of new catalytic methods to functionalize carbon–hydrogen (C–H) bonds continues to progress at a rapid pace due to the significant economic and environmental benefits of these transformations over traditional synthetic methods.
Arnold, Frances H., Coelho, Pedro S., Lewis, Jared C.   +2 more
core   +1 more source

Fundulus as the premier teleost model in environmental biology : opportunities for new insights using genomics [PDF]

, 2007
Author Posting. © Elsevier B.V., 2007. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution.
Able, Able, Adams, Allen, Andrew Whitehead, Armknecht, Armstrong, Arzuaga, Arzuaga, Arzuaga, Atz, Bacanskas, Baier-Anderson, Barron, Belknap, Bello, Bello, Bergey, Bernard B. Rees, Bernardi, Berra, Bieri, Bigelow, Billiard, Binder, Bjerkas, Black, Black, Bochdanovits, Boleza, Bonin, Bosworth, Boudreau, Boudreau, Bradford, Brown, Burgess, Burkhart, Bush, Campbell, Carletta, Cashon, Cerda, Choe, Cindi A. Hoover, Cliff, Cochran, Cohen, Cohen, Cooper, Cooper, Couillard, Cousteau, Coward, Crawford, Crawford, Crawford, Crawford, Crawford, Crawford, Crisp, Daborn, Davanzo, David H. Evans, David W. Towle, Dawley, De Montellano, Deborah L. MacLatchy, Degnan, Delamere, Delpire, Diane E. Nacci, Diaz, Diaz, DiMichele, DiMichele, DiMichele, DiMichele, DiMichele, DiMichele, DiMichele, Douglas L. Crawford, Dubé, Dubé, Dubé, Edwards, Edwards, Eisler, Elskus, Elskus, Enard, Endler, Engle, Epstein, Eriksson, Evans, Evans, Eveloff, Faisal, Fangue, Fernandez-Salguero, Fisher, Flamarique, Flemmer, Fournie, Fournier, Fries, Fritz, Fuller, Fuller, Fumi Katoh, Gagnon, Gaworecki, Gibson, Gloria V. Callard, Godard, Goldstone, Gonzalez, Gorr, Gracey, Greaney, Greaney, Greaney, Greeley, Greytak, Greytak, Greytak, Griffith, Guengerich, Gutjahr-Gobell, Haasch, Hahn, Hahn, Hahn, Hahn, Hahn, Hahn, Hahn, Harris, Hegelund, Hewitt, Hewitt, Hicks, Hinegardner, Hinegardner, Hirota, Hsiao, Hsiao, Hsiao, Janovy, Janovy, Joel N. Meyer, John J. Stegeman, Kajimura, Karchner, Karchner, Karen G. Burnett, Karnaky, Karnaky, Kashiwada, Katoh, Kayser, Kelly-Reay, Keys, Khan, Khan, Kimball, Kingsolver, Kloepper-Sams, Kloepper-Sams, Kohler, Kraemer, Krause, Krause, Krause, Kültz, Lafferty, Lai, Lake, Landry, Lauerman, Laurent, Law, LeBlanc, LeBlanc, Lee, Lemos, Lima, Lin, Lin, Lisa J. Bain, Lotrich, Love, MacLatchy, Maglich, Malvin, Mancera, Maples, Marcogliese, Marcogliese, Marcogliese, Marcogliese, Marjorie F. Oleksiak, Mark E. Hahn, Marshall, Marshall, Marshall, Marshall, Marshall, Marshall, Marshall, Marta Gómez-Chiarri, Martinez, Martinez, Matta, McArdle, McKenzie, McMillan, Meyer, Meyer, Meyer, Meyer, Meyer, Meyer, Monteverdi, Moore, Moseley, Mulvey, Mulvey, Nacci, Nacci, Nacci, Nacci, Nacci, Nacci, Nacci, Nebert, Nelson, Nelson, Nevid, Nikinmaa, Oleksiak, Oleksiak, Oleksiak, Oleksiak, Omura, Ownby, Padma, Pait, Palumbi, Paschall, Patel, Patrick, Patrick, Paynter, Payseur, Perry, Peter A. Van Veld, Peterson, Petrino, Petrino, Phillips, Philpott, Pierce, Pierce, Pierce, Pierce, Place, Place, Place, Podrabsky, Powell, Powell, Powell, Powell, Powers, Powers, Powers, Powers, Prasch, Prasch, Preston, Prince, Prince, Pruell, Quattro, Rees, Rice, Richard N. Winn, Richard T. Di Giulio, Rifkin, Roark, Roest Crollius, Roling, Roling, Roling, Roling, Ropson, Ropson, Roszell, Roszell, Roszell, Safe, Sarah Cohen, Schlichting, Schofield, Schulte, Schulte, Schulte, Schulte, Scott, Scott, Scott, Scott, Scott, Segal, Segal, Segal, Selman, Selman, Semple, Shang, Shang, Sharp, Sharpe, Shaughnessy, Shaw, Shimizu, Sibel I. Karchner, Silva, Singer, Skinner, Smith, Smith, Spalding, Stamatoyannopoulos, Stegeman, Stegeman, Stierhoff, Storz, Sumpter, Swartz, Taniguchi, Tarrant, Taylor, Taylor, Taylor, Taylor, Taylor, Taylor, Teal, Thomas D. Singer, Timme-Laragy, Timmerman, Tirindelli, Ton, Toomey, Toppin, Towle, Tremblay, Trinkaus, Trinkaus, Urushitani, Urushitani, Van Beneden, Van Beneden, Van der Meer, Van Praag, Van Veld, Van Veld, Van Veld, Van Veld, Vigouroux, Virani, Vogelbein, Vogelbein, Vogelbein, Vogelbein, Vogelbein, Vogelbein, Voight, Voyer, Wang, Wannamaker, Ward, Wassenberg, Wassenberg, Wassenberg, Weaver, Weis, Weis, Weis, Weis, Weis, Weis, Weis, Weis, Weis, Wenger, Whitehead, Whitehead, Whitehead, Wienholds, Wienholds, Willett, William S. Baldwin, William S. Marshall, Winn, Winn, Wolfgang K. Vogelbein, Wood, Wu, Yang, Zhao, Zhou, Zhou   +415 more
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A role for von Hippel-Lindau protein in pancreatic beta-cell function. [PDF]

, 2009
ObjectiveThe Vhlh gene codes for the von Hippel-Lindau protein (VHL), a tumor suppressor that is a key player in the cellular response to oxygen sensing.
Cano, David A, Hebrok, Matthias, Puri, Sapna   +2 more
core  

Sequence and functional characterization of hypoxia inducible factors, HIF1α, HIF2αa, and HIF3α, from the estuarine fish, Fundulus heteroclitus [PDF]

, 2016
Author Posting. © The Author(s), 2016. This is the author's version of the work. It is posted here under a nonexclusive, irrevocable, paid-up, worldwide license granted to WHOI. It is made available for personal use, not for redistribution.
Hahn, Mark E., Karchner, Sibel I., Rees, Bernard B., Skripnikova, Elena, Townley, Ian K., Wiese, Thomas E.   +5 more
core   +1 more source