Results 61 to 70 of about 476,931 (298)
FEBS Letters, EarlyView.Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes +4 more
wiley +1 more source
Energies, 2018 The continuous increase in energy consumption has made the potential of wind-power generation tremendous. However, the obvious intermittency and randomness of wind speed results in the fluctuation of the output power in a wind farm, seriously affecting ...
Dongxiao Niu, Di Pu, Shuyu Dai
doaj +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source
Structural insights into an engineered feruloyl esterase with improved MHET degrading properties
FEBS Letters, EarlyView.A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa +5 more
wiley +1 more source
FEBS Letters, EarlyView.Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura +2 more
wiley +1 more source
Partnership: The Canadian Journal of Library and Information Practice and Research, 2008 As the number of electronic serials available to libraries continues to increase while library budgets remain either stagnant or on the decrease, it becomes necessary to evaluate the use of a library’s electronic collection.
Alain Raymond Lamothe
doaj +1 more source
Diversity and complexity in neural organoids
FEBS Letters, EarlyView.Neural organoid research aims to expand genetic diversity on one side and increase tissue complexity on the other. Chimeroids integrate multiple donor genomes within single organoids. Self‐organising multi‐identity organoids, exogenous cell seeding, or enforced assembly of region‐specific organoids contribute to tissue complexity.
Ilaria Chiaradia, Madeline A. Lancaster
wiley +1 more source
An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane
FEBS Letters, EarlyView.Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa +3 more
wiley +1 more source
期刊線上資訊交換標準ONIX for Serials初探 A Study on ONIX for Serials [PDF]
Jiàoyù zīliào yǔ túshūguǎn xué, 2008 網際網路（World-Wide Web）的興起促成了電子商務的發展。為紓解出版商、代理商及圖書館間龐大期刊資料傳輸的重擔，期刊標準在未來的地位將會越來越重要。期刊標準種類繁多，其中EDItEUR及NISO合作發展的期刊線上資訊交換標準 ONIX of Serials是專為期刊資源而發展的結構化、全面性及可擴展性詮釋資料標準，設計於支援期刊界特定商業需要。ONIX for Serials標準若欲充分發揮效能，必須使用定義精確的識別碼。而發展於60年代末、70年代初，一向被用來辨識紙本期刊的國際標準期刊號碼（
Ho-Chin Chen, Hsiao-Hui Chang
doaj
FEBS Letters, EarlyView.Ascidian Ciona larvae initially show strong clockwise tail twisting, which is largely corrected during development. However, a small residual twist remains. This study shows that organized helical myofibrils in tail muscles mechanically stabilize this residual asymmetry, preventing complete restoration of bilateral symmetry and revealing how embryos ...
Yuki S. Kogure +3 more
wiley +1 more source