Results 21 to 30 of about 1,283,777 (223)

Structure-function relations in phosphorylcholine-binding mouse myeloma proteins [PDF]

open access: yes, 1977
The binding site interactions between the phosphorylcholine (phosphocholine)-binding mouse myeloma proteins TEPC 15, W3207, McPC 603, MOPC 167, and MOPC 511 and the isotopically substituted hapten phosphoryl-[methyl-13C]choline have been investigated ...
Goetze, Andrew M., Richards, John H.
core   +2 more sources

Phosphatidylinositol (4,5)-bisphosphate turnover by INP51 regulates the cell wall integrity pathway in "Saccharomyces cerevisiae" [PDF]

open access: yes, 2004
Signal transduction pathways are important for the cell to transduce external or internal stimuli where second messengers play an important role as mediators of the stimuli. One important group of second messengers are the phosphoinositide family present
Morales-Johansson, Helena
core   +1 more source

Stimulation of a glycosyl-phosphatidylinositol-specific phospholipase by insulin and the sulfonylurea, glimepiride, in rat adipocytes depends on increased glucose transport [PDF]

open access: yes, 1994
. Lipoprotein lipase (LPL) and glycolipidanchored cAMP-binding ectoprotein (Gcel) are modified by glycosyl-phosphatidylinositol (GPI) in rat adipocytes, however, the linkage is potentially unstable. Incubation of the cells with either insulin (0.1-30 nM)
Bandlow, Wolfhard   +3 more
core   +3 more sources

Human-Phosphate-Binding-Protein inhibits HIV-1 gene transcription and replication [PDF]

open access: yesVirology Journal, 2011
Abstract The Human Phosphate-Binding protein (HPBP) is a serendipitously discovered lipoprotein that binds phosphate with high affinity. HPBP belongs to the DING protein family, involved in various biological processes like cell cycle regulation.
Cherrier, Thomas   +11 more
openaire   +5 more sources

Phosphatase Protection Assay: 14-3-3 Binding Protects the Phosphate group of RSG from λ Protein Phosphatase

open access: yesBio-Protocol, 2015
14-3-3 proteins regulate diverse cellular processes in eukaryotes by binding to phospho-serine or threonine of target proteins. One of the physiological functions of 14-3-3 is to bind and protect phosphate groups of the target proteins against ...
Takeshi Ito, Yohsuke Takahashi
doaj   +1 more source

Mucins and calcium phosphate precipitates additively stimulate cholesterol crystallization

open access: yesJournal of Lipid Research, 1998
Human biliary mucin and calcium binding protein (CBP) influence formation of both calcium salt precipitates and cholesterol crystals and colocalize in the center of cholesterol gallstones.
A.A. van den Berg   +4 more
doaj   +1 more source

Esculetin Inhibits Cancer Cell Glycolysis by Binding Tumor PGK2, GPD2, and GPI

open access: yesFrontiers in Pharmacology, 2020
Glycolysis can improve the tolerance of tissue cells to hypoxia, and its intermediates provide raw materials for the synthesis and metabolism of the tumor cells.
Song-Tao Wu   +16 more
doaj   +1 more source

Expansive evolution of the TREHALOSE-6-PHOSPHATE PHOSPHATASE gene family in Arabidopsis [PDF]

open access: yes, 2012
Trehalose is a nonreducing sugar used as a reserve carbohydrate and stress protectant in a variety of organisms. While higher plants typically do not accumulate high levels of trehalose, they encode large families of putative trehalose biosynthesis genes.
Avonce, Nelson   +10 more
core   +2 more sources

Crystal Structures of the Global Regulator DasR from Streptomyces coelicolor: Implications for the Allosteric Regulation of GntR/HutC Repressors. [PDF]

open access: yesPLoS ONE, 2016
Small molecule effectors regulate gene transcription in bacteria by altering the DNA-binding affinities of specific repressor proteins. Although the GntR proteins represent a large family of bacterial repressors, only little is known about the allosteric
Simon B Fillenberg   +4 more
doaj   +1 more source

Investigation of Structural Mimetics of Natural Phosphate Ion Binding Motifs

open access: yesMolecules, 2015
Phosphates are ubiquitous in biology and nearly half of all proteins interact with their partners by means of recognition of phosphate residues. Therefore, a better understanding of the phosphate ion binding by peptidic structures is highly desirable ...
Evgeny A. Kataev, Tatiana A. Shumilova
doaj   +1 more source

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