Polyproline Modulates Membrane Translocation of Arginine-Rich Cell-Penetrating Peptides: Insights from Molecular Dynamics Simulations [0.03%]
多脯氨酸调节精氨细胞穿透肽的膜转运：分子动力学模拟启示
Seungho Choe,Afira Mariam,Maheen Ejaz
Seungho Choe
Recent experiments have shown that incorporating polyproline segments into arginine (R)-rich cell-penetrating peptides (CPPs) enhances membrane penetration. Here, we employ molecular dynamics (MD) simulations combined with the weighted ense...
Peculiarities of Phosphatidylserine Externalization by Nano- and Microsecond Electric Pulses [0.03%]
纳秒和微秒电脉冲诱导的磷脂酰丝氨酸外翻的特殊性
Mantas Silkunas,Alayna Enos,Iurii Semenov et al.
Mantas Silkunas et al.
Phosphatidylserine (PS) externalization is a hallmark of apoptosis but can also be triggered within seconds by pulsed electric fields (PEFs). Whether PS reaches the outer leaflet by lateral migration through electropores or indirectly throu...
Protonation of Key Acidic Residues Reveals Binding Features of PCABs to Gastric H, K-ATPase [0.03%]
关键酸性残基的质子化揭示了PCAB与胃H,K-ATP酶的结合特征
Gerardo Zerbetto De Palma,Nicole T Cerf,Mónica R Montes
Gerardo Zerbetto De Palma
The group of inhibitors known as Potassium Competitive Acid Blockers (PCABs) has become one of the main topics of current research into reducing gastric H,K-ATPase activity. The design of novel PCABs relies on structure-based drug design st...
Electrostatic Interaction as a Key Modulator of Na+,K+-ATPase Function [0.03%]
静电作用作为Na+,K+-ATP酶功能的关键调节因素
Shadreen Fairuz,Zhitong Li,Amy Gorman et al.
Shadreen Fairuz et al.
The Na+,K+-ATPase is an integral membrane protein present in all animal plasma membranes. It uses the energy of ATP hydrolysis to pump 3 Na+ ions per ATP hydrolysed from the cell cytoplasm into the extracellular fluid in exchange for 2 K+ i...
Evolutionary Prevalence of the Electrostatic Switch Mechanism in P-type ATPases [0.03%]
P型ATP酶中静电开关机制的进化普适性
Nikita S Badve,Alyssa V Buda,Jonas A Káral et al.
Nikita S Badve et al.
P-type ATPases are active transporter enzymes that maintain ion electrochemical gradients for functions such as muscle contraction, kidney function, digestion, and nerve signalling. The dysfunction of these ATPases has been linked to severa...
Structure-Function Insights into Anionic and Cationic Undecapeptides: A Combined Modeling and Antibacterial Study [0.03%]
阳离子和阴离子十一肽的结构-功能关系的理论与实验研究
Thang Nguyen Quoc,Hai Bui Thi Phuong,Duc Nguyen Van et al.
Thang Nguyen Quoc et al.
Antimicrobial peptides (AMPs) represent a promising class of alternatives to conventional antibiotics. In this study, we compared the structural and functional properties of three synthetic undecapeptides: the anionic Cn-AMP2 and its N-term...
Fluorescence Lifetime Spectroscopy Reveals Distinct Allosteric Mechanisms of SERCA Inhibitors [0.03%]
荧光寿命谱学揭示出SERCA抑制剂的特异别构机制
Jaroslava Šeflová,Carlos Cruz-Cortés,Seth L Robia et al.
Jaroslava Šeflová et al.
We recently developed a time-correlated single photon counting (TCSPC) spectroscopy approach to investigate the activation mechanisms of the calcium pump SERCA (sarcoplasmic reticulum Ca2+-ATPase). Here, we apply this approach to characteri...
Deciphering Membrane Pore Formation Mechanisms of Plasmodium falciparum Perforin-Like Protein 1 (PfPLP1) [0.03%]
恶性疟原虫裂解素样穿孔蛋白1介导细胞膜裂解的机制研究
Sanket B Patil,Subrata Dasgupta,Prasenjit Bhaumik
Sanket B Patil
Membrane Attack Complex/Perforin (MACPF) domain proteins are β-pore forming toxins (β-PFTs) involved in the pathogenesis of various organisms. Among them, Perforin-like proteins (PLPs), produced by Plasmodium species, play essential roles...
Molecular Partners of Voltage-Gated Calcium Channel β and α2δ Auxiliary Subunits: Roles in Channel Complex Regulation and Beyond [0.03%]
电压门控钙通道β和α2δ辅助亚基的分子伙伴：在通道复合物调节及其他方面的功能
Alejandra Corzo-López,Margarita Leyva-Leyva,Ricardo González-Ramírez et al.
Alejandra Corzo-López et al.
Research on the auxiliary subunits β (CaVβ) and α2δ (CaVα2δ) of voltage-gated calcium channels has gained increasing interest as novel and unexpected functional interactions for these proteins are discovered. Beyond their classic role...