Results 41 to 50 of about 425,308 (294)

Development of an antibody fragment that stabilizes GPCR/G-protein complexes. [PDF]

, 2018
Single-particle cryo-electron microscopy (cryo-EM) has recently enabled high-resolution structure determination of numerous biological macromolecular complexes.
Dawson, Roger JP, Hilger, Daniel, Hu, Hongli, Kobilka, Brian K, Koehl, Antoine, Maeda, Shoji, Manglik, Aashish, Matile, Hugues, Schertler, Gebhard FX, Skiniotis, Georgios   +9 more
core   +2 more sources

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

TGF-β2 increases eHSP90α secretion via upregulating secretory autophagy pathway

Cell Communication and Signaling
Background Extracellular heat shock protein 90α (eHSP90α) regulates diverse cellular processes such as wound healing, tumor metastasis, angiogenesis and cell differentiation etc.
Jing Li, Junmin Li, Tong Xie, Shuxin Huang, Haijiao Tian, Mengyun Liu, Xiumei Kong, Dongzhe Zhang, Khan Iqbal Nawaz, Mingli Wang, Hui Li, Jing Zhang, Fengling Yuan, Weikai Guo, Xiukun Cui, Hongmei Mu, Yanzhong Hu   +16 more
doaj   +1 more source

Cattle-derived knob paratopes grafted onto peripheral loops of the IgG1 Fc region enable the generation of a novel symmetric bispecific antibody format

Frontiers in Immunology, 2023
In this work we present a novel symmetric bispecific antibody format based on engraftments of cattle-derived knob paratopes onto peripheral loops of the IgG1 Fc region.
Desislava Yanakieva, Lena Vollmer, Andreas Evers, Vanessa Siegmund, Paul Arras, Lukas Pekar, Achim Doerner, Bernhard Valldorf, Harald Kolmar, Stefan Zielonka, Stefan Zielonka, Simon Krah   +11 more
doaj   +1 more source

Augmenting adaptive immunity: progress and challenges in the quantitative engineering and analysis of adaptive immune receptor repertoires

, 2019
The adaptive immune system is a natural diagnostic and therapeutic. It recognizes threats earlier than clinical symptoms manifest and neutralizes antigen with exquisite specificity.
Abbas, Adams, Adli, Alipanahi, Alpert, AlQuraishi, Altan-Bonnet, Angeletti, Angermueller, Antunes, Arora, Arora, Arora, Azizi, Ba, Bachmann, Bandeira, Baran, Barlow, Bashford-Rogers, Bashor, Bassani-Sternberg, Bassani-Sternberg, Bassani-Sternberg, Bassing, Baumgarth, Ben-Hamo, Benjamin, Benjamin, Bentzen, Bentzen, Bepler, Bethune, Bhat, Birnbaum, Biswas, Blythe, Bolotin, Bongartz, Boyd, Bradbury, Bradley, Breden, Brenner, Briggs, Briney, Britanova, Broere, Brown, Buenrostro, Bulik-Sullivan, Burnett, Busse, Cao, Carey, Carmona, Carreno, Casadevall, Casini, Chaudhary, Chen, Cheow, Cheung, Chevalier, Ching, Christina Fan, Cinelli, Cobey, Cohen, Cohen, Cole, Corcoran, Correia, Corrie, Croote, Cybenko, Daberdaku, Dash, Davies, Davis, Davis, Davis, De Neuter, Deac, DeKosky, DeKosky, Devilder, Devulapally, DeWitt, DeWitt 3rd, DeWitt III, Dey, Ecker, Egorov, Egorov, EL-Manzalawy, EL-Manzalawy, EL-Manzalawy, Elgundi, Elhanati, Elhanati, Elhanati, Elhanati, Elton, Emerson, Emini, Esteva, Eyer, Farlik, Farmer, Farmer, Fellouse, Ferdous, Fine, Fink, Fischer, Fischman, Fishman, Flower, Fowler, Frank, Friedensohn, Galperin, Galson, Gee, Gee, Geering, Gentiluomo, Georgiev, Georgiou, Gidoni, Gielis, Glanville, Glanville, Goddard, Goldstein, Goodfellow, Goodfellow, Gowthaman, Graf, Greaves, Greenbaum, Greenspan, Greenspan, Greenspan, Greiff, Greiff, Greiff, Greiff, Greiff, Griffiths, Grigaityte, Guo, Guo, Hadrup, Halperin, Han, Han, Hartweger, Hashimshony, Hashimshony, Haynes, He, Heather, Heather, Hebditch, Heemskerk, Hellman, Hillman, Hochgerner, Hochreiter, Hochreiter, Hoehn, Hoehn, Holder, Holland, Holzinger, Hoogenboom, Hopp, Hornik, Hou, Howie, Hua, Huang, Imkeller, Irvine, Ishino, Islam, Islam, Jackson, Jackson, Jacobs, Jacobsen, Jacobsen, Jain, Jain, Jaitin, Janin, Jardine, Jardine, Jeanbart, Jerne, Jespersen, Joglekar, Jokinen, June, Jyothi, Kabat, Kanyavuz, Kaplon, Karplus, Keich, Keskin, Khosravi-Maharlooei, Kieke, Kingma, Kisielow, Klambauer, Klebanoff, Konishi, Korn, Kotzias, Kovaltsuk, Kramer, Krawczyk, Krawczyk, Krawczyk, Kringelum, Kunik, Kunik, Kuroda, Lanchantin, Lanzarotti, Lapidoth, Lapidoth, Laplane, Larsen, Lauer, Lavinder, Lavoie, LeCun, Lee, Lee, Legutki, Legutki, Levitt, Li, Li, Li, Li, Liberis, Lindeman, Linette, Liu, Liu, Liu, Liu, Lollier, Longo, Lu, Luo, Luo, Luo, López-Santibáñez-Jácome, Løset, MacBeath, Macosko, Madi, Madi, Mahajan, Manavalan, Manczinger, Mangul, Mangul, Marchalonis, Marcou, Margalit, Marrack, Marrack, Marrack, Martin, Martin, Mascola, Mason, Mason, Mayer, McDaniel, Meng, Merbl, Meysman, Mian, Migalska, Miho, Miho, Minhas, Moffett, Mohan, Mora, Mora, Murphy, Murugan, Muyldermans, Navalkar, Nemazee, Newell, Newell, Newell, Nimrod, North, Oakes, Ohlin, Olson, Ostmeyer, Ostmeyer, Ott, Ott, Padlan, Palme, Parker, Parola, Patterson, Pellequer, Perelson, Perelson, Persson, Peterson, Picelli, Pierce, Pittala, Pogorelyy, Pogorelyy, Pogson, Ponomarenko, Ponomarenko, Pou, Preuer, Priel, Purwada, Purwada, Quang, Radbruch, Ramos-López, Ramsköld, Raybould, Remington, Reshetova, Ribeiro, Richards, Richman, Riley, Rives, Rizzetto, Robert, Robins, Robins, Robinson, Rosati, Rosenberg, Rosenblatt, Rubelt, Rubinstein, Sahin, Saikia, Sandve, Sandve, Sblattero, Schmitt, Schneider, Schneider-Hohendorf, Schroeder, Schumacher, Schwab, Scott, Seet, Segler, Seimetz, Sela-Culang, Sela-Culang, Sela-Culang, Sethna, Sethna, Setliff, Sette, Sewell, Shah, Shalev-Shwartz, Sharon, Shaw, Shokri, Shugay, Shugay, Sidhom, Sidhom, Sikorski, Simonovsky, Simonyan, Sircar, Sircar, Slocombe, Smallwood, Soto, Spiess, Stoeckius, Stone, Strauli, Stubbington, Stubbington, Sundararajan, Swartz, Sylwester, Szegedy, Tague, Talmage, Tang, Taussig, Thakkar, Thomas, Thomas, Tickotsky, Tiller, Tirosh, Tompa, Tonegawa, Townsend, Trepel, Trolle, Turchaninova, Turner, Udyavar, Vamathevan, van der Schoot, Van Regenmortel, Venturi, Verkoczy, Vollmers, Voss, Vázquez Bernat, Wainberg, Walsh, Wang, Wang, Wang, Wang, Wang, Wang, Wang, Wardemann, Wardemann, Wardemann, Watson, Weinstein, Weitzner, Weitzner, Whitehead, Williams, Wine, Wine, Wirth, Woese, Wucherpfennig, Wurch, Xu, Xu, Xu, Yaari, Yaari, Yager, Yang, Younger, Zandian, Zarnitsyna, Zhang, Zhang, Zhao, Zhao, Zhao, Zheng, Zirlik, Zong   +478 more
core   +1 more source

Structural biology of ferritin nanocages

FEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

Organ‐specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides

FEBS Letters, EarlyView.
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley   +1 more source

Computational strategies for dissecting the high-dimensional complexity of adaptive immune repertoires

, 2017
The adaptive immune system recognizes antigens via an immense array of antigen-binding antibodies and T-cell receptors, the immune repertoire. The interrogation of immune repertoires is of high relevance for understanding the adaptive immune response in ...
Afzal, Ahmed, Albert, Amanna, Andrews, Angermueller, Apeltsin, Arden, Atchley, Avnir, Barabási, Barak, Bashford-Rogers, Bastian, Baum, Becattini, Ben-Hamo, Berger, Betz, Boc, Bolen, Bolkhovskaya, Bolotin, Bouckaert, Boyd, Boyd, Breden, Brown, Burnet, Bürckert, Calis, Castro, Chang, Chao, Chen, Ching, Cobey, Collins, Corcoran, Covacu, Csardi, Cui, Dash, de Bourcy, DeKosky, DeKosky, DeWitt, Dziubianau, Elhanati, Elhanati, Elhanati, Ellebedy, Emerson, Felsenstein, Friedensohn, Gadala-Maria, Galson, Galson, Geering, Georgiou, Ghraichy, Giribet, Giudicelli, Glanville, Glanville, Glanville, Good, Granato, Greiff, Greiff, Greiff, Greiff, Greiff, Grigaityte, Guindon, Gupta, Gupta, Hagberg, Halliley, Hammarlund, Heather, Hershberg, Hochreiter, Hoehn, Hoehn, Hoehn, Horns, Howie, Iversen, Jackson, Janeway, Jiang, Johnston, Jost, Jurtz, Kaplinsky, Kaplinsky, Kendall, Khavrutskii, Kidd, Kidd, Kidera, Kirik, Konishi, Kumar, Landsverk, Larkin, Lavinder, Laydon, Laydon, Lee, Lee, Lewitus, Li, Lindeman, Lindner, Liu, Love, Lozupone, Madi, Madi, Malissen, Mamoshina, Mangul, Manz, Martin, Meng, Miho, Mora, Morisita, Murugan, Nazarov, Nouri, Oakes, Ostmeyer, Paradis, Parameswaran, Parola, Pinheiro, Pollok, Ralph, Ravn, Reddy, Rempala, Rempala, Revell, Rizzetto, Robinson, Ronquist, Roybal, Rubelt, Rubelt, Safonova, Schliep, Schramm, Schwab, Shannon, Sheng, Sheng, Shlemov, Shugay, Shugay, Shugay, Snir, Snir, Stamatakis, Stern, Strauli, Stubbington, Stubbington, Sun, Sun Cinelli, Swofford, Thomas, Tickotsky, Tonegawa, Torkamani, Trepel, VanDuijn, Venturi, Venturi, Vieira, Vita, Wang, Wardemann, Warren, Watson, Watson, Watson, Weinstein, Wine, Wine, Wu, Yaari, Yaari, Yang, Yeap, Yermanos, Yokota, Yu, Zhu   +200 more
core   +1 more source

Interleukin-2 druggability is modulated by global conformational transitions controlled by a helical capping switch. [PDF]

, 2020
Interleukin-2 (IL-2) is a small α-helical cytokine that regulates immune cell homeostasis through its recruitment to a high-affinity heterotrimeric receptor complex (IL-2Rα/IL-2Rβ/γc).
De Paula, Viviane S, Garcia, K Christopher, Glassman, Caleb R, Jude, Kevin M, Nerli, Santrupti, Sgourakis, Nikolaos G   +5 more
core   +1 more source

Tau acetylation at K331 has limited impact on tau pathology in vivo

FEBS Letters, EarlyView.
We mapped tau post‐translational modifications in humanized MAPT knock‐in mice and in amyloid‐bearing double knock‐in mice. Acetylation within the repeat domain, particularly around K331, showed modest increases under amyloid pathology. To test functional relevance, we generated MAPTK331Q knock‐in mice.
Shoko Hashimoto, Yukio Matsuba, Mika Takahashi, Takaomi C. Saido   +3 more
wiley   +1 more source