AreTomo: An integrated software package for automated marker-free, motion-corrected cryo-electron tomographic alignment and reconstruction [0.03%]
AreTomo：一种集成软件包，用于自动无标记、运动校正的冷冻电子层析成像对准和重建
Shawn Zheng,Georg Wolff,Garrett Greenan et al.
Shawn Zheng et al.
AreTomo, an abbreviation for Alignment and Reconstruction for Electron Tomography, is a GPU accelerated software package that fully automates motion-corrected marker-free tomographic alignment and reconstruction in a single package. By corr...
Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes [0.03%]
巧躲一刀：RNaseRNA复合物结构研究中防止RNA被切割的技术
Seth P Jones,Christian Goossen,Sean D Lewis et al.
Seth P Jones et al.
RNases are varied in the RNA structures and sequences they target for cleavage and are an important type of enzyme in cells. Despite the numerous examples of RNases known, and of those with determined three-dimensional structures, relativel...
Benoît Zuber,Vladan Lučić
Benoît Zuber
Cryo-electron tomography (Cryo-ET) provides unique opportunities to image cellular components at high resolution in their native state and environment. While many different cell types were investigated by cryo-ET, here we review application...
How advances in cryo-electron tomography have contributed to our current view of bacterial cell biology [0.03%]
cryo电子层析成像技术的进步如何推动了我们对细菌细胞生物学的当前认知
Janine Liedtke,Jamie S Depelteau,Ariane Briegel
Janine Liedtke
Advancements in the field of cryo-electron tomography have greatly contributed to our current understanding of prokaryotic cell organization and revealed intracellular structures with remarkable architecture. In this review, we present some...
Recent advances in the structural biology of encapsulin bacterial nanocompartments [0.03%]
细菌纳米隔室encapsulin的结构生物学最新进展
Timothy Wiryaman,Navtej Toor
Timothy Wiryaman
Large capsid-like nanocompartments called encapsulins are common in bacteria and archaea and contain cargo proteins with diverse functions. Advances in cryo-electron microscopy have enabled structure determination of many encapsulins in rec...
Does dentine mineral change with anatomical location, microscopic site and patient age? [0.03%]
牙本质的矿化程度是否随解剖位置、显微结构及患者年龄而变化？
Arosha T Weerakoon,Crystal Cooper,Ian A Meyers et al.
Arosha T Weerakoon et al.
Objective: To determine the effect of patient age (young or mature), anatomical location (shallow/deep and central/peripheral) and microscopic site (intertubular/peritubular) on dentine mineral density, distribution and c...
Conformational switches that control the TEC kinase - PLCγ signaling axis [0.03%]
控制TEC激酶-PLCγ信号轴的构象开关
Jacques Lowe,Raji E Joseph,Amy H Andreotti
Jacques Lowe
Cell surface receptors such as the T-cell receptor (TCR) and B-cell receptor (BCR) engage with external stimuli to transmit information into the cell and initiate a cascade of signaling events that lead to gene expression that drives the im...
Daniel J Buss,Roland Kröger,Marc D McKee et al.
Daniel J Buss et al.
Structural hierarchy of bone - observed across multiple scales and in three dimensions (3D) - is essential to its mechanical performance. While the mineralized extracellular matrix of bone consists predominantly of carbonate-substituted hyd...
Colloid assembly and transformation (CAT): The relationship of PILP to biomineralization [0.03%]
胶体聚合和转化（CAT）：PILP与生物矿化的关系
Laurie Gower,Jeremy Elias
Laurie Gower
The field of biomineralization has undergone a revolution in the past 25 years, which paralleled the discovery by Gower of a polymer-induced liquid-precursor (PILP) mineralization process. She proposed this in vitro model system might be us...
Structural plasticity in the loop region of engineered lipocalins with novel ligand specificities, so-called Anticalins [0.03%]
工程化具有新型配体特异性的抗康林蛋白（Anticalin）的环区结构可塑性研究
S Achatz,A Jarasch,A Skerra
S Achatz
Anticalins are generated via combinatorial protein design on the basis of the lipocalin protein scaffold and constitute a novel class of small and robust engineered binding proteins that offer prospects for applications in medical therapy a...