Results 51 to 60 of about 114,843,840 (203)

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

FEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai, Mohyeddine Omrane, Nassima Benzoubir, Didier Samuel, Ama Gassama‐Diagne   +4 more
wiley   +1 more source

Lipid Droplets, Phospholipase A₂, Arachidonic Acid, and Atherosclerosis

Biomedicines, 2021
Lipid droplets, classically regarded as static storage organelles, are currently considered as dynamic structures involved in key processes of lipid metabolism, cellular homeostasis and signaling.
Miguel A. Bermúdez, María A. Balboa, Jesús Balsinde   +2 more
doaj   +1 more source

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

FEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

Micromachined glass apertures for artificial lipid bilayer formation in a microfluidic system [PDF]

, 1998
The use of spark assisted chemical engraving (SACE) to produce glass apertures that are suitable for the formation of artificial bilayer lipid membranes is described.
Uttamchandani, D.G., Syms, R., Aljada, Muhsen, Yan Xing, Zhu, YH, Shi, XM, Ashok, A, Xing, Yan, Hida, Hirotaka, Shikida, M, Li, Yongyao, Pirri C, F., Ballestra, A., Lee, TMH, Pirri, Candido, Cai, H, Xing, Y, Blue, Robert, Gautam, A K, Weng, C, Brown, J.G., Zhang, Xin, Zhang, P., Xu, Y, DEZEST, D, Wong, Man, Kwan, FY, Sucher, Nikolaus J., Zeng, Fan, Pal, Prem, Agrawal, A, Svetovoy, Vitaly, Soma', Aurelio, Xiao, G, Qu, Xiaopeng, Sharma, V, Dong, Shu Rong, Yan, X, To, S, Dutta, A, Wai, PKA, Chu, HK, Y Xing, Song, Y. J., Chan, CY, Yue, TM, Ferrando, N, NICU, L, Gu, Changdong, Goslvez, M A, V Svetovoy, Karyn Mutkins, De Pasquale, Giorgio, Amit Agrawal, Shiv G Singh, Luo, Yuan, Wang, K, Duryodhan, V S, Fukuzawa, K, MATHIEU, Fabrice, Agrawal, Amit, Flockhart, Gordon M H, Chen, Xuyuan, Lo, GQ, Veijola, T., Jiang, Linan, THOMAS, Olivier, Tam, KF, Hida, H., Ehmann, KF, Gadea Gironés, Rafael, JASINEVICIUS, R. G., Zhang, Y, Song, Liyan, Zhang, X, Liu, H, Zagnoni, Michele, Kang, C, Canavese, Giancarlo, Cocuzza, Matteo, Liu, B, Cui, Jingzhi, Ko, SM, Krijnen, G.J.M.; id_orcid, Zhou, Jianying, Wong, Kam Sing, Mei, SM, Chen, R., Polido Gomes, J.F., Stagg, J., Marasso, Simone Luigi, VALES, L. F., Zhang, Tong Yi, Farinelli, P, de Bree, H.E., Zhu, Z, REMIENS, D, Hau, Winky L.W., Singh, Shiv Govind, Zhu, W, COSTECALDE, J, Yick Chuen Chan, Li, Li, Svetovoy, V.B., G J M Krijnen, Yang, W. W., Xu, Hui, Sandison, Mairi E., Hida, H, Zhang, SJ, B Tang, Cheng, Zaijun, Pan, W., Ferrando, Néstor, Chan, Mansun, Yung, KC, Xiao, K., M C Elwenspoek, CUNHA, L. S., N Ferrando, Lee, Yi Kuen, Yung, KL, BALLESTRA A., Chan, Yick Chuen, NICU, Liviu, Sharma, A K, COSTECALDE, Jean, Lee, Sylvanus Yuk Kwan, Lijie Li, M Shikida, Bhide, R R, J Cerdá, Giuri, E., Gosalvez Ayuso, Miguel Angel, Zagnoni, M., Trau, Dieter W., Tan, Q, Singh, S S, Wu, Zhangming, Shu, Yi, Prem Pal, Pandey, A K, Morgan, Hywel, H-e De Bree, Burn, Paul, Sridharan, A, H Hida, Singh, S G, Li, Y, Ricciardi, Carlo, SOYER, C, Sato, Kazuo, Zhao, T. S., Qiu, H. H., Zhangming Wu, Wright, Mike T., R Gadea, Sandison, M.E., Abu-Hantash, Mustafa, ANDREETA, M. R. B., Meredith, Paul, Pal, P, Bai, G, Zhang, XM, 伞海生, Liu, AQ, Jin, Baidong, Li, Lijie, Yu, MB, CARASCHI, L. C., Wang, Wentao, Samuel Cheng, George Vamvounis, Tagliaferro, Alberto, Vamvounis, George, Li, Juntao, Deladi, S., Haldar, S, Cheng, CH, Bhide, Rohit R, J W Van Honschoten, Krijnen, G.J.M., Robert Blue, Jin, Hao, Duttagupta, S P, Gosalvez, M A, Liu, Bo, van Honschoten, J.W., Wu, Zhang Ming, Ma, Wei, Miguel A Gosálvez, Kwong, DL, SINGH, SG, Pandey, Ashok Kumar, DEÜ, Jean-François, Li Li, A Sridharan, Abu-Hantash, M., Lowrie, C., Ma, Xianghong, E. GIURI, Elwenspoek, M.C., Xianghong Ma, Lina Stankovic, Morgan, H., Chi, Guanxin, Desmulliez, M.P.Y., Cerda, J, Sharma, Vandana, Begbie, M., Stankovic, Lina, Rohit R Bhide, Mutkins, Karyn, DEZEST, Denis, V B Svetovoy, Liang, Bing, Lee, WB, Li, L., M A Gosalvez, Gordon M H Flockhart, Shin, Dong Youn, Zheng, YP, Feng, Zhihong, Sato, K, Yuan Li, Demarchi, Danilo, Ren, Tian Ling, Wentao Wang, Stankovic, Vladimir, Qiu, Huihe, Wang, Zhenlong, Yao, J., MATHIEU, F, Deepak Uttamchandani, DEÜ, J F, Kazuo Sato, Liu, Yikun, Vladimir Stankovic, Cerdá Boluda, Joaquín, San, Haisheng, Yi-Kuen Lee, Elwenspoek, Michael Curt, BHIDE, RR, Muhsen Aljada, Perrone, Denis, MAZENQ, L, Giorcelli, Mauro, Shin, Dong-Youn, Paul Burn, Sato, K., Mike T Wright, Yobas, Levent, Gosálvez, M. A., Wu, Q. X., Cheng, S., Li, Gang, Tang, B, Wang, Yuelin, Gadea, R, Krijnen, Gijsbertus J.M., Xiaopeng Qu, Uttamchandani, Deepak, Sandison, M E, Weiland, D., Cheung, CF, Zhou, Changjian, Huihe Qiu, MAZENQ, Laurent, S Deladi, Veerla, S, Grassia, Paul, Sun, D, Ferrando Jódar, Néstor, Zohar, Yitshak, Wang, Rong Xin, Svetovoy, V., Singh, Shiv G, Amakawa, H, REMIENS, Denis, Quaglio, Marzia, Li, Yuan, SOYER, Caroline, Morgan, H, Zou, H., Sanginario, Alessandro, VEIJOLA T., Paul Meredith, K Sato, Yang, Yi   +288 more
core   +2 more sources

Salmonella lipopolysaccharide‐containing supported lipid bilayers as platforms to study bacteriophage interactions

FEBS Letters, EarlyView.
We present robust protocols for the preparation of supported lipid bilayers (SLBs) incorporating either Salmonella smooth LPS or outer membrane vesicles (OMVs). We use a combination of quartz crystal microbalance with dissipation (QCM‐D) and fluorescence microscopy to both characterize the SLBs of various compositions and to probe their interactions ...
Hudson P. Pace, Alyssa Borges, Charles Arnaud, Tove Karlsson, Nina K. Bröker, Stefanie Barbirz, Marta Bally   +6 more
wiley   +1 more source

DHA modifies lipid raft structure and function of cancer cells

, 2014
In vivo and in vitro studies suggest that ω-3 PUFA can be cancer chemopreventive, chemosuppressive and auxiliary agents for cancer therapy. Ω-3 PUFA could alter cancer growth influencing cell replication, cell cycle, and cell death.
G. Montorfano, P.A. Corsetto, A. Cremona, A.M. Rizzo, P. Roderi   +4 more
core   +1 more source

The antidepressant drug sertraline is a novel inhibitor of yeast Pah1 and human lipin 1 phosphatidic acid phosphatases

Journal of Lipid Research
Phosphatidic acid phosphatase (PAP) is an evolutionarily conserved eukaryotic enzyme that catalyzes the Mg2+-dependent dephosphorylation of phosphatidic acid to produce diacylglycerol.
Geordan J. Stukey, Matthew R. Breuer, Natalie Burchat, Ruta Jog, Kollin Schultz, Gil-Soo Han, Matthew S. Sachs, Harini Sampath, Ronen Marmorstein, George M. Carman   +9 more
doaj   +1 more source

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

FEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Microbiome‐blood–brain barrier interactions in aging — mechanisms and therapeutic potential

FEBS Letters, EarlyView.
Aging reshapes the gut microbiome (↓SCFA‐producing commensals; ↑pro‐inflammatory outputs), shifting circulating metabolites (↓SCFAs; ↑LPS, ↑TMAO, ↑PAA) that act at the BBB to increase nonspecific transcytosis, alter transport, and promote astrocyte reactivity, heightening brain vulnerability.
Daniel Cuervo‐Zanatta, Hari Baskar Balasubramanian, Amir Pasokh, Marietta Zille   +3 more
wiley   +1 more source

Structure‐forward targeting of claudins with synthetic binders

FEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source