scholarly journals Sterically Shielded, Stabilized Nitrile Imine for Rapid Bioorthogonal Protein Labeling in Live Cells

2018 ◽  
Vol 140 (14) ◽  
pp. 4860-4868 ◽  
Author(s):  
Peng An ◽  
Tracey M. Lewandowski ◽  
Tuğçe G. Erbay ◽  
Peng Liu ◽  
Qing Lin
Keyword(s):  
Protein Labeling ◽  
Live Cells ◽  
Nitrile Imine

Superfast Tetrazole–BCN Cycloaddition Reaction for Bioorthogonal Protein Labeling on Live Cells

2021 ◽  
Author(s):  
Gangam Srikanth Kumar ◽  
Stefano Racioppi ◽  
Eva Zurek ◽  
Qing Lin
Keyword(s):  
Cycloaddition Reaction ◽  
Protein Labeling ◽  
Live Cells

Recognition-driven chemical labeling of endogenous proteins in multi-molecular crowding in live cells

2017 ◽  
Vol 53 (88) ◽  
pp. 11972-11983 ◽  
Author(s):  
Kazuma Amaike ◽  
Tomonori Tamura ◽  
Itaru Hamachi
Keyword(s):  
Protein Labeling ◽  
Live Cells ◽  
Molecular Crowding ◽  
Chemical Labeling ◽  
Endogenous Protein ◽  
Bona Fide ◽  
Endogenous Proteins

Endogenous protein labeling is one of the most invaluable methods for studying the bona fide functions of proteins in live cells.

Photoisomerization-enhanced 1,3-dipolar cycloaddition of carbon-bridged octocyclic azobenzene with photo-released nitrile imine for peptide stapling and imaging in live cells

2020 ◽  
Vol 18 (29) ◽  
pp. 5602-5607
Author(s):  
Jiajie Deng ◽  
Xueting Wu ◽  
Guiling Guo ◽  
Xiaohu Zhao ◽  
Zhipeng Yu
Keyword(s):  
Cell Apoptosis ◽  
Live Cells ◽  
Dipolar Cycloaddition ◽  
Ligation Reaction ◽  
Nitrile Imine ◽  
Nitrile Imines ◽  
Peptide Stapling

A novel photo-click ligation reaction between nitrile imines and photo-switchable octocyclic azobenzenes was established to both tune the conformation of the NoxaB peptide and conjugate probes with enhanced efficacy in cell apoptosis.

Protein Labeling in Live Cells for Immunological Applications

2018 ◽  
Vol 29 (3) ◽  
pp. 680-685 ◽  
Author(s):  
Parisa Moghaddam-Taaheri ◽  
Amy J. Karlsson
Keyword(s):  
Protein Labeling ◽  
Live Cells

scholarly journals Rational Development of Caged-Biotin Protein-Labeling Agents and Some Applications in Live Cells

2011 ◽  
Vol 18 (10) ◽  
pp. 1261-1272 ◽  
Author(s):  
Takuya Terai ◽  
Eri Maki ◽  
Shigeru Sugiyama ◽  
Yoshinori Takahashi ◽  
Hiroyoshi Matsumura ◽  
...  
Keyword(s):  
Protein Labeling ◽  
Live Cells ◽  
Rational Development

A novel reactive turn-on probe capable of selective profiling and no-wash imaging of Bruton's tyrosine kinase in live cells

2019 ◽  
Vol 55 (24) ◽  
pp. 3473-3476 ◽  
Author(s):  
Xin Wang ◽  
Nan Ma ◽  
Rui Wu ◽  
Ke Ding ◽  
Zhengqiu Li
Keyword(s):  
Tyrosine Kinase ◽  
Mammalian Cells ◽  
High Sensitivity ◽  
Protein Labeling ◽  
Live Cells ◽  
Bruton’S Tyrosine Kinase ◽  
Bruton's Tyrosine Kinase ◽  
Turn On ◽  
Sensitivity And Selectivity

A series of reaction-based probes have been developed by conjugation of maleimide–coumarin into ibrutinib. The resulting probes display high sensitivity and selectivity toward BTK, and were proven to be suitable for simultaneous protein labeling and no-wash imaging of BTK inside live mammalian cells.

scholarly journals Selective Mitochondrial Protein Labeling Enabled by Biocompatible Photocatalytic Reactions inside Live Cells

JACS Au ◽  
2021 ◽  
Author(s):  
Haoyan Wang ◽  
Yixin Zhang ◽  
Kaixing Zeng ◽  
Jiali Qiang ◽  
Ye Cao ◽  
...  
Keyword(s):  
Mitochondrial Protein ◽  
Protein Labeling ◽  
Live Cells ◽  
Photocatalytic Reactions

4-dimensional, high-resolution imaging of living cells

1992 ◽  
Vol 50 (1) ◽  
pp. 416-417
Author(s):  
Shinya Inoué
Keyword(s):  
Light Microscope ◽  
Living Cells ◽  
Live Cells ◽  
Video Tape ◽  
Active Living ◽  
High Resolution Imaging ◽  
3 Dimensional ◽  
Dynamic Architecture ◽  
Resolution Imaging ◽  
Disk Memory

This paper reports progress of our effort to rapidly capture, and display in time-lapsed mode, the 3-dimensional dynamic architecture of active living cells and developing embryos at the highest resolution of the light microscope. Our approach entails: (A) real-time video tape recording of through-focal, ultrathin optical sections of live cells at the highest resolution of the light microscope; (B) repeat of A at time-lapsed intervals; (C) once each time-lapsed interval, an image at home focus is recorded onto Optical Disk Memory Recorder (OMDR); (D) periods of interest are selected using the OMDR and video tape records; (E) selected stacks of optical sections are converted into plane projections representing different view angles (±4 degrees for stereo view, additional angles when revolving stereos are desired); (F) analysis using A - D.

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