Buscar
Mostrando ítems 21-30 de 5162
The GRASP domain in golgi reassembly and stacking proteins: differences and similarities between lower and higher Eukaryotes
(Wiley-Blackwell, 2019-09-01)
The Golgi complex is part of the endomembrane system and is responsible for receiving transport cargos from the endoplasmic reticulum and for sorting and targeting them to their final destination. To perform its function ...
Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of single-chain chimeras
(Blackwell Publishing LtdOxfordInglaterra, 2005)
Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3(1)
(Elsevier Science BvAmsterdamHolanda, 2003)
Modulation of the Allosteric Communication between the Polo-Box Domain and the Catalytic Domain in Plk1 by Small Compounds
(American Chemical Society, 2018-08)
The Polo-like kinases (Plks) are an evolutionary conserved family of Ser/Thr protein kinases that possess, in addition to the classical kinase domain at the N-terminus, a C-terminal polo-box domain (PBD) that binds to ...
The leptospiral antigen Lp49 is a two-domain protein with putative protein binding function
(ACADEMIC PRESS INC ELSEVIER SCIENCE, 2008)
Pathogenic Leptospira is the etiological agent of leptospirosis, a life-threatening disease that affects populations worldwide. Currently available vaccines have limited effectiveness and therapeutic interventions are ...
Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris
(WILEY-BLACKWELLHOBOKEN, 2012)
RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris, RpfG together with the sensor kinase RpfC ...
The βγ-crystallin domain of Lysinibacillus sphaericus phosphatidylinositol phospholipase C plays a central role in protein stability
(Springer, 2018-08)
βγ-crystallin has emerged as a superfamily of structurally homologous proteins with representatives across all domains of life. A major portion of this superfamily is constituted by microbial members. This superfamily has ...
Mapping eIF5A binding sites for Dys1 and Lia1: In vivo evidence for regulation of eIF5A hypusination
(2003-12-18)
The evolutionarily conserved factor eIF5A is the only protein known to undergo hypusination, a unique posttranslational modification triggered by deoxyhypusine synthase (Dys1). Although eIF5A is essential for cell viability, ...