Proteoliposomes reconstituted with human aquaporin-1 reveal novel single-ion-channel properties [0.03%]
用人aquaporin-1重组的蛋白脂质体揭示了新的单离子通道性质
Sam W Henderson,Yoshitaka Nakayama,Murray L Whitelaw et al.
Sam W Henderson et al.
Human aquaporin 1 (hAQP1) forms homotetrameric channels that facilitate fluxes of water and small solutes across cell membranes. In addition to water channel activity, hAQP1 displays non-selective monovalent cation-channel activity gated by...
Avraham Moriel,Haguy Wolfenson,Eran Bouchbinder
Avraham Moriel
Cell-matrix and cell-cell adhesion play important roles in a wide variety of physiological processes, from the single-cell level to the large scale, multicellular organization of tissues. Cells actively apply forces to their environment, ei...
Gennady Gorin,Lior Pachter
Gennady Gorin
Single-cell RNA sequencing data can be modeled using Markov chains to yield genome-wide insights into transcriptional physics. However, quantitative inference with such data requires careful assessment of noise sources. We find that long pr...
Pressure, motion, and conformational entropy in molecular recognition by proteins [0.03%]
蛋白质分子识别中的压力，运动和构象熵
José A Caro,Kathleen G Valentine,Taylor R Cole et al.
José A Caro et al.
The thermodynamics of molecular recognition by proteins is a central determinant of complex biochemistry. For over a half-century, detailed cryogenic structures have provided deep insight into the energetic contributions to ligand binding b...
Expansion microscopy of neutrophil nuclear structure and extracellular traps [0.03%]
中性粒细胞核结构和胞外陷阱的扩展显微镜检查
Jason Scott Holsapple,Lena Schnitzler,Louisa Rusch et al.
Jason Scott Holsapple et al.
Neutrophils are key players of the immune system and possess an arsenal of effector functions, including the ability to form and expel neutrophil extracellular traps (NETs) in a process termed NETosis. During NETosis, the nuclear DNA/chroma...
Optimization of cryo-electron microscopy for quantitative analysis of lipid bilayers [0.03%]
冷冻电子显微镜在脂质双层定量分析中的优化
Frederick A Heberle,Doug Welsch,Haden L Scott et al.
Frederick A Heberle et al.
Cryogenic electron microscopy (cryo-EM) is among the most powerful tools available for interrogating nanoscale structure of biological materials. We recently showed that cryo-EM can be used to measure the bilayer thickness of lipid vesicles...
Ayush Saurabh,Matthew Safar,Mohamadreza Fazel et al.
Ayush Saurabh et al.
Here we adapt the Bayesian nonparametrics (BNP) framework presented in the first companion article to analyze kinetics from single-photon, single-molecule Förster resonance energy transfer (smFRET) traces generated under continuous illumin...
Ayush Saurabh,Mohamadreza Fazel,Matthew Safar et al.
Ayush Saurabh et al.
We present a unified conceptual framework and the associated software package for single-molecule Förster resonance energy transfer (smFRET) analysis from single-photon arrivals leveraging Bayesian nonparametrics, BNP-FRET. This unified fr...
A dark intermediate in the fluorogenic reaction between tetrazine fluorophores and trans-cyclooctene [0.03%]
四嗪荧光团与反式环辛烯之间氟反应的一个暗中间体
Felix Hild,Philipp Werther,Klaus Yserentant et al.
Felix Hild et al.
Fluorogenic labeling via bioorthogonal tetrazine chemistry has proven to be highly successful in fluorescence microscopy of living cells. To date, trans-cyclooctene (TCO) and bicyclonyne have been found to be the most useful substrates for ...
Single-photon smFRET. III. Application to pulsed illumination [0.03%]
单光子smFRET（单分子荧光共振能量转移）第三部分：在脉冲照明中的应用
Matthew Safar,Ayush Saurabh,Bidyut Sarkar et al.
Matthew Safar et al.
Förster resonance energy transfer (FRET) using pulsed illumination has been pivotal in leveraging lifetime information in FRET analysis. However, there remain major challenges in quantitative single-photon, single-molecule FRET (smFRET) da...