Imidazolium-based ionic liquids cause mammalian cell death due to modulated structures and dynamics of cellular membrane [0.03%]
咪唑类离子液体通过调节细胞膜结构和动力学诱导哺乳动物细胞死亡
Karishma Bakshi,Saheli Mitra,Veerendra Kumar Sharma et al.
Karishma Bakshi et al.
Here, we report the toxic effects of various imidazolium-based ionic liquids (ILs) with varying hydrocarbon chain lengths, on different human cell lines. Multiple biological assays have shown that the ILs with long hydrocarbon chains have s...
Dynamic interactions of CbiN and CbiM trigger activity of a cobalt energy-coupling-factor transporter [0.03%]
CbiN和CbiM的动态相互作用触发钴能量耦合因子转运蛋白的活性
Friedrich Finkenwirth,Michael Sippach,Sinah N Pecina et al.
Friedrich Finkenwirth et al.
Energy-coupling factor (ECF) transporters for uptake of vitamins and transition-metal ions into prokaryotic cells share a common architecture consisting of a substrate-specific integral membrane protein (S), a transmembrane coupling protein...
Effect of selected B-ring-substituted oxysterols on artificial model erythrocyte membrane and isolated red blood cells [0.03%]
几种B环取代的氧化固醇对红细胞模型膜和分离红细胞的影响
Marta Targosz-Korecka,Anita Wnętrzak,Anna Chachaj-Brekiesz et al.
Marta Targosz-Korecka et al.
In this paper, systematic studies concerning the influence of selected oxysterols on the structure and fluidity of human erythrocyte membrane modeled as Langmuir monolayers have been performed. Three oxidized cholesterol derivatives, namely...
The influence of the stereochemistry and C-end chemical modification of dermorphin derivatives on the peptide-phospholipid interactions [0.03%]
阿桔啡衍生物立体化学及C端修饰对肽-磷脂相互作用的影响
Katarzyna Trzeciak,Piotr Paluch,Tomasz Pawlak et al.
Katarzyna Trzeciak et al.
In this work the conformation of dermorphin, Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2, an opioid peptide and its analogues with different stereochemistry of alanine and different C-terminus is studied in aqueous and membrane environments. Using tw...
Katerina C Nastou,Georgios N Tsaousis,Vassiliki A Iconomidou
Katerina C Nastou
The majority of all proteins in cells interact with membranes either permanently or temporarily. Peripheral membrane proteins form transient complexes with membrane proteins and/or lipids, via non-covalent interactions and are of outmost im...
Extracellular lysine 38 plays a crucial role in pH-dependent transport via human monocarboxylate transporter 1 [0.03%]
门控机制依赖于外环境中赖氨酸38的参与调控单羧酸转运蛋白1的功能
Atsushi Yamaguchi,Yuya Futagi,Masaki Kobayashi et al.
Atsushi Yamaguchi et al.
Human monocarboxylate transporters (hMCTs) are expressed in many tissues and mediate the transport of various substrates across the plasma membrane. Among hMCTs, hMCT1-4 cotransport H+ with monocarboxylates such as pyruvate and l-lactate, i...
Hao Wang,Stefan Schoebel,Florian Schmitz et al.
Hao Wang et al.
Aquaporins are membrane-intrinsic proteins initially defined as water (H2O) channels in all organisms and subsequently found to have multiple substrate specificities, such as hydrogen peroxide (H2O2). H2O2 is a signaling molecule that parta...
Binding and intracellular transport of 25-hydroxycholesterol by Niemann-Pick C2 protein [0.03%]
Niemann-Pick C2蛋白对25-羟基胆固醇的结合及胞内转运作用
Daniel Petersen,Peter Reinholdt,Maria Szomek et al.
Daniel Petersen et al.
Side-chain oxidized cholesterol derivatives, like 25-hydroxycholesterol (25-OH-Chol) are important regulators of cellular cholesterol homeostasis. How transport of oxysterols through the endo-lysosomal pathway contributes to their biologica...
Tau-induced mitochondrial membrane perturbation is dependent upon cardiolipin [0.03%]
tau诱导的线粒体膜扰动依赖于心磷脂
Angelique Camilleri,Stephanie Ghio,Mario Caruana et al.
Angelique Camilleri et al.
Misfolding and aggregate formation by the tau protein has been closely related with neurotoxicity in a large group of human neurodegenerative disorders, which includes Alzheimer's disease. Here, we investigate the membrane-active properties...
Runrun Wu,Robert Stephenson,Abigail Gichaba et al.
Runrun Wu et al.
The β-barrel assembly machinery (BAM) is responsible for the biogenesis of outer membrane proteins (OMPs) into the outer membranes of Gram-negative bacteria. These OMPs have a membrane-embedded domain consisting of a β-barrel fold which c...