Multiplexed patterning of hybrid lipid membrane and protein arrays for cell signaling study

Lab on a Chip ◽  
2021 ◽  
Author(s):  
Yu-Ting Ti ◽  
Hsiao-Chi Cheng ◽  
Ying Li ◽  
Hsiung-Lin Tu
Keyword(s):  
Cell Signaling ◽  
Lipid Membrane ◽  
Protein Arrays

A chip-based strategy for multiplexed patterning of hybrid lipid membrane and protein arrays for cell signaling study.

761 Reverse-phase protein arrays as a tool to discover mutation-associated alterations in cell signaling pathways

2010 ◽  
Vol 8 (5) ◽  
pp. 192
Author(s):  
J. Starmann ◽  
S. Blaich ◽  
C. Bender ◽  
H. Armbruster ◽  
H. Mannsperger ◽  
...  
Keyword(s):  
Cell Signaling ◽  
Signaling Pathways ◽  
Reverse Phase ◽  
Protein Arrays ◽  
Phase Protein ◽  
Cell Signaling Pathways

Comparison of Conventional and Electron Spectroscopic Imaging in the Fixed Beam Electron Microscope of Ordered Protein Arrays

1985 ◽  
Vol 43 ◽  
pp. 74-75
Author(s):  
E. L. Buhle ◽  
U. Aebi
Keyword(s):  
Image Processing ◽  
Electron Microscope ◽  
High Resolution ◽  
Image Plane ◽  
Electron Spectroscopic Imaging ◽  
Protein Arrays ◽  
Beam Electron ◽  
Average Unit ◽  
Fixed Beam ◽  
Energy Components

CTEM brightfield images are formed by a combination of relatively high resolution elastically scattered electrons and unscattered and inelastically scattered electrons. In the case of electron spectroscopic images (ESI), the inelastically scattered electrons cause a loss of both contrast and spatial resolution in the image. In the case of ESI imaging on the Zeiss EM902, the transmited electrons are dispersed into their various energy components by passing them through a magnetic prism spectrometer; a slit is then placed in the image plane of the prism to select the electrons of a given energy loss for image formation. The purpose of this study was to compare CTEM with ESI images recorded on a Zeiss EM902 of ordered protein arrays. Digital image processing was employed to analyze the average unit cell morphologies of the two types of images.

Chapter 2b: The molecular antigenic structure of the TBEV

2020 ◽  
Keyword(s):  
Conformational Changes ◽  
Neutralizing Antibodies ◽  
Lipid Membrane ◽  
Cell Entry ◽  
Antigenic Structure ◽  
E Proteins ◽  
Amino Acid Sequence Level ◽  
Endosomal Membrane ◽  
E Protein ◽  
Golgi Network

TBEV-particles are assembled in an immature, noninfectious form in the endoplasmic reticulum by the envelopment of the viral core (containing the viral RNA) by a lipid membrane associated with two viral proteins, prM and E. Immature particles are transported through the cellular exocytic pathway and conformational changes induced by acidic pH in the trans-Golgi network allow the proteolytic cleavage of prM by furin, a cellular protease, resulting in the release of mature and infectious TBE-virions. The E protein controls cell entry by mediating attachment to as yet ill-defined receptors as well as by low-pH-triggered fusion of the viral and endosomal membrane after uptake by receptor-mediated endocytosis. Because of its key functions in cell entry, the E protein is the primary target of virus neutralizing antibodies, which inhibit these functions by different mechanisms. Although all flavivirus E proteins have a similar overall structure, divergence at the amino acid sequence level is up to 60 percent (e.g. between TBE and dengue viruses), and therefore cross-neutralization as well as (some degree of) cross-protection are limited to relatively closely related flaviviruses, such as those constituting the tick-borne encephalitis serocomplex.

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