Results 101 to 110 of about 3,161,922 (291)
ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains
FEBS Letters, EarlyView.CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif +8 morewiley +1 more sourceEvolution of stars and stellar populations /
, 2005 * presents stellar evolution as a tool for investigating the evolution of galaxies and of the universe in general.Includes bibliographical references (p.Cassisi, Santi,, Salaris, Maurizio,core Exploring stellar evolution with gravitational-wave observations
, 2018 International audienceRecent detections of gravitational waves from merging binary black holes opened new possibilities to study the evolution of massive stars and black hole formation.Dvorkin, I., Joseph Silk, Irina Dvorkin, Jean-Philippe Uzan, Silk, Joseph, Uzan, Jean-Philippe, Vangioni, Elisabeth, Dvorkin, Irina, Uzan, J., Vangioni, E., Silk, J., Elisabeth Vangioni +11 morecore +1 more sourceA ring system detected around the Centaur (10199) Chariklo [PDF]
, 2014 Hitherto, rings have been found exclusively around the four giant planets in the Solar System1. Rings are natural laboratories in which to study dynamical processes analogous to those that take place during the formation of planetary systems and galaxies.Vanzi, L., Frank, N.R., Spagnotto, Julio, H. Monteiro, Harpsøe, Kennet Bomann West, J. Lecacheux, M. Emilio, Braga-Ribas, Felipe, F. Roques, M. Gillon, E. Jehin, Vanzi, Leonardo, Machado, D. I., Roques, Françoise, Lellouch, Emmanuel, Vachier, Frédéric, R. Sfair, Almenares, L., Colazo, C., Colas, F., D. G. Lambas, Jørgensen, U., Jehin, E., Lemos, Pablo, J. L. Ortiz, J. B. Haislip, J. P. Moore, Gil Hutton, Ricardo Alfredo, Wang, X.-b., Gil-Hutton, Ricardo, Ivarsen, Kevin, Opitom, C., R. Melia, Ortiz, J. L., Moore, J., A. Ceretta, Harpsoe, K., Schneiter, E. M., Lambas, Diego García, Lacluyze, A.P., Braga-Ribas, F., Lorenzini, L., Schneiter, E.M., B. Sicardy, Gu, S.-h., L. Almenares, Melia, R., L. Maquet, Reichart, Daniel E., LaCluyze, A. P., Haislip, J. B., Ivarsen, K. M., L. Vanzi, Benedetti-Rossi, G., R. G. Sandness, Haislip, J.B., Garcia Lambas, Diego Rodolfo, G. Tancredi, Perez, V., J. Spagnotto, Sicardy, Bruno, Wang, Xiaobin, Martinez, N., Colas, François, P. Kervella, P. Lemos, Benedetti-Rossi, Gustavo, C. Colazo, Gil-Hutton, R., LaCluyze, A., Tancredi, G., Frank, N. R., Gu, S. -H., Snodgrass, Colin, Maury, A., Gillon, Michaël, Gomes, A. Ramos, Manfroid, Jean, MacHado, D.I., Gomes Jr., A., F. Char, Widemann, Thomas, Ceretta, Alberto, Maury, A. J., M. Dominik, Schneiter, E., Tancredi, Gonzalo, Char, F., Opitom, Cyrielle, Gillon, M., Brage-Ribas, F., Roland, S., Lacluyze, Aaron P., Moutamid, M. El, Lambas, D., Roques, F., Ceretta, A., Manfroid, J., Ligier, N., Lecacheux, J., V. Perez, Monteiro, H., Lambas, D. G., S. Roland, U. G. Jørgensen, El Moutamid, Maryame, Harpsøe, Kennet, Machado, D., J. Pollock, Leiva, R., R. Gil-Hutton, Colazo, Carlos, Benedetti Rossi, G., Mehret, Leandro Cesar, Braga Ribas, F., Frank, Nathan R., El Moutamid, M., Assafin, Marcelo, A. Ramos Gomes, Emilio, M., Gu, S., Jorgensen, U. G., Gu, Shenghong, N. Ligier, M. Rabus, Camargo, Julio, L. Lorenzini, Rabus, Markus, Skottfelt, Jesper Mirsa, Camargo, J. I. B., Sicardy, B., Skottfelt, J., Vieira-Martins, R., Lemos, P., Moore, Justin, Char, Farid, Moore, J.P., Rabus, M., Roig, F., Ivarsen, K., Vachier, F., Sandness, R. G., Wang, X. -B., Camargo, J., K. M. Ivarsen, Haislip, Joshua, Skottfelt, Jesper, Assafin, M., Lellouch, E., Vierira-Martins, R., Sandness, R.G., Vieira Martins, R., Ivarsen, K.M., Reichart, D.E., D. I. Machado, Gomes, A. R., J. Manfroid, Camargo, J., I B, Sfair, R. [UNESP], E. Lellouch, Frank, N., N. Morales, Reichart, D., F. Colas, Ortiz, J.L., X.-b. Wang, C. Opitom, S.-h. Gu, F. Braga-Ribas, Emilio, Marcelo, N. R. Frank, K. Harpsøe, Roland, Santiago, Vieira-Martins, Roberto, J. Skottfelt, Harpsøe, K., Jorgensen, U., N. Martinez, Moore, J. P., Ligier, Nicolas, J. I. B. Camargo, Pollock, J., Camargo, J.I.B., Reichart, D. E., Melia, Raul Roberto, Lecacheux, Jean, Jørgensen, Uffe Gråe, C. Snodgrass, Jørgensen, U.G., G. Benedetti-Rossi, Haislip, J., M. El Moutamid, Camargo, J.,, Sfair, R., Maquet, L., Sfair, Rafael, Mehret, L., Duffard, R., Jørgensen, U. G., Dominik, M., Duffard, R,, Kervella, Patrick, Dominik, Martin, R. Vieira-Martins, Snodgrass, C., Spagnotto, J., Widemann, T., Duffard, René, A. P. LaCluyze, Pollock, Joseph, E. M. Schneiter, Maquet, Lucie, Sandness, R., Morales, N., Kervella, P., Wang, X., L. Mehret, A. Maury, Ramos Gomes, A., F. Vachier, Jehin, Emmanuel, T. Widemann, R. Duffard, Schneiter, E. Matías, F. Roig, R. Leiva, M. Assafin, Ortiz, J., D. E. Reichart, Ortiz, José Luis, Morales, Nicolás, Duffard, René D., Gomes, A. Ramos, Jr., Dominik, M.; id_orcid +233 morecore +1 more sourceReconstructing enzyme evolution by protein engineering
FEBS Letters, EarlyView.Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...Lukas Drexler, Markus R. Busch, Reinhard Sterner +2 morewiley +1 more sourceInvestigating transcription factor dynamics in health and disease using FRAP
FEBS Letters, EarlyView.FRAP analysis of GFP‐tagged transcription factors reveals how molecular mobility and target engagement change in response to drug treatment. By combining live‐cell imaging, quantitative model fitting, and statistical analysis, this approach uncovers transcription factor dynamics linked to disease mechanisms, providing a powerful framework for ...Kannan Govindaraj, Carolina Vazquez Garzon, Jose Joaquin Velasco, Janine N. Post +3 morewiley +1 more sourceConserved binding mode but diverse interfaces of MreC‐PBP2 interactions
FEBS Letters, EarlyView.The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.Hyunseok Jang, Hyo Been Jin, Chang Min Kim, So Yeon Lee, Hyun Ho Park +4 morewiley +1 more sourceMicrobiome‐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 morewiley +1 more sourceStructure‐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. Vecchiowiley +1 more source