To be launched on Aug 2015
Sponsored by Biophysical Society of China and Institute of Biophysics, CAS, P.R. China.
Online published by SpringerLink.

  From Editor-in-Chief
I am delighted that submissions are now open for the brand new open access journal, Biophysics Reports. | I am pleased to be joined by this distinguished Editorial Board..
I am proud to be launching this journal together with SpringerOpen, the most active open access publisher in the physical sciences. I am equally proud to be working with the Biophysical Society of China, and Biophysics Reports is the society’s official journal.
With Biophysics Reports, we will provide a resource on novel theories, methods, protocols and improvements on basic research techniques in the biological and biomedical sciences.
Reasons to publish with us

        ●  Rigorous peer review
        ●  Free of charge for submission/publication
        ●  Rapid publication upon acceptance
        ●  Compliance with all open access mandates.
And you can download all the details and instructions for publishing in Biophysics Reports here.
Tao Xu
Institute of Biophysics, CAS
  Online First More>>
Comparison of immune profiles between hepatocellular carcinoma subtypes
DOI: 10.1007/s41048-019-00102-w
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    Biophysics Reports. 2019, 5 (5-6): 0-0.  
    Abstract   HTML   PDF (2217KB) ( 3 )
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    Towards understanding the mechanisms of proton pumps in Complex-I of the respiratory chain
    Xuejun C. Zhang, Bin Li
    Biophysics Reports. 2019, 5 (5-6): 219-234.   DOI: 10.1007/s41048-019-00094-7
    Abstract   HTML   PDF (1184KB) ( 27 )
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    Super-resolution microscopy: successful applications in centrosome study and beyond
    Jingyan Fu, Chuanmao Zhang
    Biophysics Reports. 2019, 5 (5-6): 235-243.   DOI: 10.1007/s41048-019-00101-x
    Abstract   HTML   PDF (867KB) ( 11 )
    Centrosome is the main microtubule-organizing center in most animal cells. Its core structure, centriole, also assembles cilia and flagella that have important sensing and motility functions. Centrosome has long been recognized as a highly conserved organelle in eukaryotic species. Through electron microscopy, its ultrastructure was revealed to contain a beautiful nine-symmetrical core 60 years ago, yet its molecular basis has only been unraveled in the past two decades. The emergence of super-resolution microscopy allows us to explore the insides of a centrosome, which is smaller than the diffraction limit of light. Super-resolution microscopy also enables the compartmentation of centrosome proteins into different zones and the identification of their molecular interactions and functions. This paper compiles the centrosome architecture knowledge that has been revealed in recent years and highlights the power of several super-resolution techniques.
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    Refining RNA solution structures with the integrative use of label-free paramagnetic relaxation enhancement NMR
    Zhou Gong, Shuai Yang, Qing-Fen Yang, Yue-Ling Zhu, Jing Jiang, Chun Tang
    Biophysics Reports. 2019, 5 (5-6): 244-253.   DOI: 10.1007/s41048-019-00099-2
    Abstract   HTML   PDF (2482KB) ( 8 )
    NMR structure calculation is inherently integrative, and can incorporate new experimental data as restraints. As RNAs have lower proton densities and are more conformational heterogenous than proteins, the refinement of RNA structures can benefit from additional types of restraints. Paramagnetic relaxation enhancement (PRE) provides distance information between a paramagnetic probe and protein or RNA nuclei. However, covalent conjugation of a paramagnetic probe is difficult for RNAs, thus limiting the use of PRE NMR for RNA structure characterization. Here, we show that the solvent PRE can be accurately measured for RNA labile imino protons, simply with the addition of an inert paramagnetic cosolute. Demonstrated on three RNAs that have increasingly complex topologies, we show that the incorporation of the solvent PRE restraints can significantly improve the precision and accuracy of RNA structures. Importantly, the solvent PRE data can be collected for RNAs without isotope enrichment. Thus, the solvent PRE method can work integratively with other biophysical techniques for better characterization of RNA structures.
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    Regulation of intracellular Ca2+/CaMKII signaling by TRPV4 membrane translocation during osteoblastic differentiation
    Fen Hu, Yali Zhao, Zhenhai Hui, Fulin Xing, Jianyu Yang, Imshik Lee, Xinzheng Zhang, Leiting Pan, Jingjun Xu
    Biophysics Reports. 2019, 5 (5-6): 254-263.   DOI: 10.1007/s41048-019-00100-y
    Abstract   HTML   PDF (1324KB) ( 22 )
    Bone constantly remodels between resorption by osteoclasts and formation by osteoblasts; therefore the functions of osteoblasts are pivotal for maintaining homeostasis of bone mass. Transient receptor potential vanilloid 4 (TRPV4), a type of mechanosensitive channel, has been reported to be a key regulator in bone remodeling. However, the relationship between TRPV4 and osteoblast function remains largely elusive. Only little is known about the spatial distribution change of TRPV4 during osteoblastic differentiation and related signal events. Based on three-dimensional super-resolution microscopy, our results clearly showed a different distribution of TRPV4 in undifferentiated and differentiated osteoblasts, which reflected the plasma membrane translocation of TRPV4 along with prolonged differentiation. GSK1016790A (GSK101), the most potent agonist of TRPV4, triggered rapid calcium entry and calmodulin-dependent protein kinase II (CaMKII) phosphorylation via TRPV4 activation in a differentiation-dependent manner, indicating that the abundance of TRPV4 at the cell surface resulting from differentiation may be related to the modulation of Ca2+ response and CaMKII activity. These data provide compelling evidences for the plasma membrane translocation of TRPV4 during osteoblastic differentiation as well as demonstrate the regulation of downstream Ca2+/CaMKII signaling.
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CN 10-1302/Q
ISSN 2364-3439
eISSN 2364-3420
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