Results 41 to 50 of about 877,235 (257)

Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting

FEBS Open Bio, 2021
The Golgi‐localized, gamma‐ear containing, ADP‐ribosylation factor‐binding proteins (GGAs 1, 2, and 3) are multidomain proteins that bind mannose 6‐phosphate receptors (MPRs) at the Golgi and play a role, along with adaptor protein complex 1 (AP‐1), in ...
Balraj Doray, Lin Liu, Wang‐Sik Lee, Benjamin C. Jennings, Stuart Kornfeld   +4 more
doaj   +1 more source

The presence of phosphate-binding protein in inner mitochondrial membrane.

Acta medica Okayama, 1976
Phosphate-binding protein(s) was found in the inner mitochondrial membrane of calf heart by Sephadex G-200 and G-25 gel filtration. The binding activity was inhibited by N-ethylmaleimide and competed by a large amount of cold phosphate. The amount of phosphate bound to the fraction was 29 nmoles per mg of protein. Affinity chromatography with phosphate-
Hatase, Osamu, Tsutsui, Ken, Oda, Takuzo
openaire   +3 more sources

Reciprocal control of viral infection and phosphoinositide dynamics

FEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

Substrate specificity and ecological significance of PstS homologs in phosphorus uptake in marine Synechococcus sp. WH8102

Microbiology Spectrum
Phosphorus, a vital macronutrient, often limits primary productivity in marine environments. Marine Synechococcus strains, including WH8102, rely on high-affinity phosphate-binding proteins (PstS) to scavenge inorganic phosphate in oligotrophic oceans ...
Pramita Ranjit, Deepa Varkey, Bhumika S. Shah, Ian T. Paulsen   +3 more
doaj   +1 more source

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

FEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho, Shin Morioka, Junko Sasaki, Takehiko Sasaki   +3 more
wiley   +1 more source

Dimerization misalignment in human glutamate-oxaloacetate transaminase variants is the primary factor for PLP release. [PDF]

PLoS ONE, 2018
The active form of vitamin B6, pyridoxal 5'-phosphate (PLP), plays an essential role in the catalytic mechanism of various proteins, including human glutamate-oxaloacetate transaminase (hGOT1), an important enzyme in amino acid metabolism.
Jesi Lee, Trevor Gokey, Dylan Ting, Zheng-Hui He, Anton B Guliaev   +4 more
doaj   +1 more source

Structure Characterization of Escherichia coli Pseudouridine Kinase PsuK

Frontiers in Microbiology, 2022
Pseudouridine (Ψ) is one of the most abundant RNA modifications in cellular RNAs that post-transcriptionally impact many aspects of RNA. However, the metabolic fate of modified RNA nucleotides has long been a question. A pseudouridine kinase (PsuK) and a
Xiaojia Li, Xiaojia Li, Kangjie Li, Wenting Guo, Yan Wen, Yan Wen, Chunyan Meng, Baixing Wu   +7 more
doaj   +1 more source

Evaluation of Phosphate Removal from Water by Immobilized Phosphate-Binding Protein PstS. [PDF]

Journal of Bioscience and Bioengineering, 2000
The phosphate (P(i))-binding protein PstS is a member of a family of periplasmic proteins that act as high-affinity receptors for active transport systems in bacteria. PstS protein purified from Pseudomonas aeruginosa was immobilized to N-hydroxysuccinimide-activated Sepharose, packed into a plastic column (5 x 70 mm), and examined for its potential ...
A, Kuroda, H, Kunimoto, T, Morohoshi, T, Ikeda, J, Kato, N, Takiguchi, A, Miya, H, Ohtake   +7 more
openaire   +2 more sources

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

Crystallization and preliminary X-ray diffraction analysis of human phosphate-binding protein [PDF]

Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005
Human phosphate-binding protein (HPBP) was serendipitously discovered by crystallization and X-ray crystallography. HPBP belongs to a eukaryotic protein family named DING that is systematically absent from the genomic database. This apoprotein of 38 kDa copurifies with the HDL-associated apoprotein paraoxonase (PON1) and binds inorganic phosphate. HPBP
Contreras-Martel, Carlos, Carpentier, P., Morales, R., Renault, F., Chesne-Seck, M.L., Rochu, D., Masson, P., Fontecilla-Camps, J.C., Chabriere, E.   +8 more
openaire   +4 more sources