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

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.

scholarly journals Actin-binding Verprolin Is a Polarity Development Protein Required for the Morphogenesis and Function of the Yeast Actin Cytoskeleton

1997 ◽  
Vol 139 (7) ◽  
pp. 1821-1833 ◽  
Author(s):  
Gabriela Vaduva ◽  
Nancy C. Martin ◽  
Anita K. Hopper
Keyword(s):  
Actin Cytoskeleton ◽  
Binding Proteins ◽  
Mitochondrial Protein ◽  
Binding Activity ◽  
Actin Binding ◽  
Live Cells ◽  
Growth Defect ◽  
Protein Distribution ◽  
Cycle Dependent ◽  
And Function

Yeast verprolin, encoded by VRP1, is implicated in cell growth, cytoskeletal organization, endocytosis and mitochondrial protein distribution and function. We show that verprolin is also required for bipolar bud-site selection. Previously we reported that additional actin suppresses the temperature-dependent growth defect caused by a mutation in VRP1. Here we show that additional actin suppresses all known defects caused by vrp1-1 and conclude that the defects relate to an abnormal cytoskeleton. Using the two-hybrid system, we show that verprolin binds actin. An actin-binding domain maps to the LKKAET hexapeptide located in the first 70 amino acids. A similar hexapeptide in other acting-binding proteins was previously shown to be necessary for actin-binding activity. The entire 70– amino acid motif is conserved in novel higher eukaryotic proteins that we predict to be actin-binding, and also in the actin-binding proteins, WASP and N-WASP. Verprolin-GFP in live cells has a cell cycle-dependent distribution similar to the actin cortical cytoskeleton. In fixed cells hemagglutinin-tagged Vrp1p often co-localizes with actin in cortical patches. However, disassembly of the actin cytoskeleton using Latrunculin-A does not alter verprolin's location, indicating that verprolin establishes and maintains its location independent of the actin cytoskeleton. Verprolin is a new member of the actin-binding protein family that serves as a polarity development protein, perhaps by anchoring actin. We speculate that the effects of verprolin upon the actin cytoskeleton might influence mitochondrial protein sorting/function via mRNA distribution.

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

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.

Sign in / Sign up

Export Citation Format

Share Document