Results 101 to 110 of about 793,543 (339)

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Frizzled Proteins are bona fide G Protein-Coupled Receptors [PDF]

, 2009
Receptors of the Frizzled family initiate Wnt ligand-dependent signaling controlling multiple steps in organism development and highly conserved in evolution. Misactivation of the Wnt/Frizzled signaling is cancerogenic.
Silke Buestorf, Vladimir L. Katanaev
core   +1 more source

On the role of G protein-coupled receptors oligomerization [PDF]

, 2013
The existence of a supramolecular organization of the G protein-coupled receptor (GPCR) is now being widely accepted by the scientific community.
Ahern, Siobhán, Ciruela Alférez, Francisco, Fernández Dueñas, Víctor, Gómer Soler, Maricel   +3 more
core   +2 more sources

Genetic Polymorphisms of Prokineticins and Prokineticin Receptors Associated with Human Disease

Life
Prokineticins (PKs) are low molecular weight proteins that exert their effects by binding to two seven-transmembrane G-protein-coupled receptors (prokineticin receptors, PKRs).
Roberta Lattanzi, Rossella Miele
doaj   +1 more source

GPCRdb: an information system for G protein-coupled receptors

Nucleic Acids Res., 2015
Recent developments in G protein-coupled receptor (GPCR) structural biology and pharmacology have greatly enhanced our knowledge of receptor structure-function relations, and have helped improve the scientific foundation for drug design studies. The GPCR
Vignir Ísberg, Stefan Mordalski, Christian Munk, Krzysztof Rataj, K. Harpsøe, A. Hauser, B. Vroling, A. Bojarski, G. Vriend, David E. Gloriam   +9 more
semanticscholar   +1 more source

Molecular bases of circadian magnesium rhythms across eukaryotes

FEBS Letters, EarlyView.
Circadian rhythms in intracellular [Mg2+] exist across eukaryotic kingdoms. Central roles for Mg2+ in metabolism suggest that Mg2+ rhythms could regulate daily cellular energy and metabolism. In this Perspective paper, we propose that ancestral prokaryotic transport proteins could be responsible for mediating Mg2+ rhythms and posit a feedback model ...
Helen K. Feord, Gerben van Ooijen
wiley   +1 more source

Flavonoid allosteric modulation of mutated visual rhodopsin associated with retinitis pigmentosa [PDF]

, 2017
Dietary flavonoids exhibit many biologically-relevant functions and can potentially have beneficial effects in the treatment of pathological conditions. In spite of its well known antioxidant properties, scarce structural information is available on the ...
Garriga Solé, Pere, Herrera Hernández, María Guadalupe, Lupala, Cecylia Severin, Pérez González, Juan Jesús, Ramon Portés, Eva, Tena Campos, Mercè   +5 more
core   +3 more sources

RINGdb: An integrated database for G protein-coupled receptors and regulators of G protein signaling

BMC Genomics, 2006
Background Many marketed therapeutic agents have been developed to modulate the function of G protein-coupled receptors (GPCRs). The regulators of G-protein signaling (RGS proteins) are also being examined as potential drug targets.
Huang Hsien-Da, Wu Li-Cheng, Sun Wei-Hsin, Fang Yu-Ching, Juan Hsueh-Fen, Horng Jorng-Tzong   +5 more
doaj   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

FEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang, Grace Du, Charity Yongo‐Luwawa, Angelina Lu, Brett Kinrade, Kim Munro, Karl E. Klose, William D. Lubell, Peter Davies, Shuaiqi Guo   +9 more
wiley   +1 more source

Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. [PDF]

, 2015
G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways.
Barty, Anton, Basu, Shibom, Boutet, Sébastien, Caffrey, Martin, Caro, Lydia N, Carragher, Bridget, Chapman, Henry N, Cherezov, Vadim, Coe, Jesse, Conrad, Chelsie E, de Waal, Parker W, Diederichs, Kay, Dong, Yuhui, Ernst, Oliver P, Fromme, Petra, Fromme, Raimund, Gao, Xiang, Gati, Cornelius, Griffin, Patrick R, Grotjohann, Ingo, Gu, Xin, Gurevich, Vsevolod V, Han, Gye Won, He, Yuanzheng, Howe, Nicole, Hubbell, Wayne L, Ishchenko, Andrii, James, Daniel, Jiang, Hualiang, Jiang, Yi, Kang, Yanyong, Katritch, Vsevolod, Ke, Jiyuan, Kupitz, Christopher, Lee, Regina J, Li, Dianfan, Li, Jun, Lisova, Stella, Liu, Haiguang, Liu, Wei, Ma, Jinming, Melcher, Karsten, Messerschmidt, Marc, Moeller, Arne, Pal, Kuntal, Pascal, Bruce D, Potter, Clinton S, Roy-Chowdhury, Shatabdi, Spence, John CH, Standfuss, Jörg, Stevens, Raymond C, Suino-Powell, Kelly M, Tan, MH Eileen, Tan, Minjia, Van Eps, Ned, Vishnivetskiy, Sergey A, Wang, Dingjie, Wang, Meitian, Weierstall, Uwe, West, Graham M, White, Thomas A, Williams, Garth J, Xu, H Eric, Xu, Qingping, Yang, Huaiyu, Yefanov, Oleksandr, Zatsepin, Nadia A, Zhang, Chenghai, Zhao, Yingming, Zheng, Zhong, Zhi, Xiaoyong, Zhou, X Edward   +71 more
core   +1 more source