Environment-Responsive Fluorescent Nucleoside Analogue Probe for Studying Oligonucleotide Dynamics in a Model Cell-like Compartment

2013 ◽  
Vol 117 (46) ◽  
pp. 14273-14282 ◽  
Author(s):  
Maroti G. Pawar ◽  
Seergazhi G. Srivatsan
Keyword(s):  
Nucleoside Analogue ◽  
Model Cell ◽  
Fluorescent Nucleoside

Structural and Dynamical Impact of a Universal Fluorescent Nucleoside Analogue Inserted Into a DNA Duplex

2017 ◽  
Vol 121 (50) ◽  
pp. 11249-11261 ◽  
Author(s):  
Loussiné Zargarian ◽  
Akli Ben Imeddourene ◽  
Krishna Gavvala ◽  
Nicolas P. F. Barthes ◽  
Benoit Y. Michel ◽  
...  
Keyword(s):  
Nucleoside Analogue ◽  
Dna Duplex ◽  
Fluorescent Nucleoside

scholarly journals Spontaneous Nanoparticle Formation From a Fluorescent Nucleoside Analogue

2011 ◽  
Vol 32 (spc8) ◽  
pp. 2906-2910 ◽  
Author(s):  
Eun-Kyoung Bang ◽  
Do-Hyun Moon ◽  
Byeang-Hyean Kim
Keyword(s):  
Nucleoside Analogue ◽  
Nanoparticle Formation ◽  
Fluorescent Nucleoside

ChemInform Abstract: Expanded Fluorescent Nucleoside Analogue as Hybridization Probe.

ChemInform ◽  
2008 ◽  
Vol 39 (12) ◽  
Author(s):  
Young Jun Seo ◽  
Sankarprasad Bhuniya ◽  
Subhasish Tapadar ◽  
Jeong Wu Yi ◽  
Byeang Hyean Kim
Keyword(s):  
Nucleoside Analogue ◽  
Hybridization Probe ◽  
Fluorescent Nucleoside

Membrane–cytoskeleton interactions in cholesterol-dependent domain formation

2015 ◽  
Vol 57 ◽  
pp. 177-187 ◽  
Author(s):  
Jennifer N. Byrum ◽  
William Rodgers
Keyword(s):  
Biological Properties ◽  
Membrane Rafts ◽  
Membrane Domains ◽  
Biological Functions ◽  
Membrane Cytoskeleton ◽  
Heterogeneous Structures ◽  
Integral Role ◽  
Model Cell ◽  
Actomyosin Cytoskeleton ◽  
Dependent Domain

Since the inception of the fluid mosaic model, cell membranes have come to be recognized as heterogeneous structures composed of discrete protein and lipid domains of various dimensions and biological functions. The structural and biological properties of membrane domains are represented by CDM (cholesterol-dependent membrane) domains, frequently referred to as membrane ‘rafts’. Biological functions attributed to CDMs include signal transduction. In T-cells, CDMs function in the regulation of the Src family kinase Lck (p56lck) by sequestering Lck from its activator CD45. Despite evidence of discrete CDM domains with specific functions, the mechanism by which they form and are maintained within a fluid and dynamic lipid bilayer is not completely understood. In the present chapter, we discuss recent advances showing that the actomyosin cytoskeleton has an integral role in the formation of CDM domains. Using Lck as a model, we also discuss recent findings regarding cytoskeleton-dependent CDM domain functions in protein regulation.

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