scholarly journals A genetically encoded cyclobutene probe for labelling of live cells

2017 ◽  
Vol 53 (76) ◽  
pp. 10604-10607 ◽  
Author(s):  
K. Liu ◽  
B. Enns ◽  
B. Evans ◽  
N. Wang ◽  
X. Shang ◽  
...  
Keyword(s):  
Live Cells ◽  
Efficient Synthesis ◽  
Protein Labelling

Efficient synthesis of and protein labelling with a genetically encoded cyclobutene probe.

A Ni-NTA-based red fluorescence probe for protein labelling in live cells

2017 ◽  
Vol 5 (6) ◽  
pp. 1166-1173 ◽  
Author(s):  
Ailun Chao ◽  
Nan Jiang ◽  
Ya Yang ◽  
Hongyan Li ◽  
Hongzhe Sun
Keyword(s):  
Protein Purification ◽  
Fluorescence Probe ◽  
Live Cells ◽  
Great Success ◽  
Protein Labelling ◽  
Red Fluorescence

The great success of a His6-Ni-nitrilotriaceate (Ni-NTA) system in protein purification has inspired scientists to develop novel Ni-NTA based fluoresent probes for imaging of proteins in live cells.

The development of a nucleus staining fluorescent probe for dynamic mitosis imaging in live cells

2015 ◽  
Vol 51 (45) ◽  
pp. 9336-9338 ◽  
Author(s):  
Krishna Kanta Ghosh ◽  
Yun-Mi Jeong ◽  
Nam-Young Kang ◽  
JungYeol Lee ◽  
Wan Si Yan Diana ◽  
...  
Keyword(s):  
Real Time ◽  
Fluorescent Probe ◽  
Live Cells ◽  
Efficient Synthesis ◽  
Nucleus Staining

The rapid and efficient synthesis of a novel fluorescent xanthone library (AX) and its application for the development of a new nucleus staining fluorescent probe (CDb12) for monitoring real-time mitosis progression in live cells is presented.

In cellulo protein labelling with Ru-conjugate for luminescence imaging and bioorthogonal photocatalysis

2015 ◽  
Vol 51 (93) ◽  
pp. 16664-16666 ◽  
Author(s):  
Kalyan K. Sadhu ◽  
E. Lindberg ◽  
N. Winssinger
Keyword(s):  
Ruthenium Complex ◽  
Photocatalytic Reduction ◽  
Live Cells ◽  
Direct Visualization ◽  
Protein Labelling ◽  
Aryl Azide ◽  
Luminescence Imaging

Labelling of proteins with a luminescent ruthenium complex enables the direct visualization and photocatalytic reduction of aryl azide in live cells.

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.

Multi-mode light microscopy of microtubule assembly dynamics and chromosome movement in vivo and In vitro

1996 ◽  
Vol 54 ◽  
pp. 730-731
Author(s):  
E. D. Salmon ◽  
J. C. Waters ◽  
C. Waterman-Storer
Keyword(s):  
Imaging System ◽  
Ccd Camera ◽  
Transmitted Light ◽  
Microtubule Assembly ◽  
Live Cells ◽  
Optical Efficiency ◽  
Multiple Band ◽  
Multi Mode

We have developed a multi-mode digital imaging system which acquires images with a cooled CCD camera (Figure 1). A multiple band pass dichromatic mirror and robotically controlled filter wheels provide wavelength selection for epi-fluorescence. Shutters select illumination either by epi-fluorescence or by transmitted light for phase contrast or DIC. Many of our experiments involve investigations of spindle assembly dynamics and chromosome movements in live cells or unfixed reconstituted preparations in vitro in which photodamage and phototoxicity are major concerns. As a consequence, a major factor in the design was optical efficiency: achieving the highest image quality with the least number of illumination photons. This principle applies to both epi-fluorescence and transmitted light imaging modes. In living cells and extracts, microtubules are visualized using X-rhodamine labeled tubulin. Photoactivation of C2CF-fluorescein labeled tubulin is used to locally mark microtubules in studies of microtubule dynamics and translocation. Chromosomes are labeled with DAPI or Hoechst DNA intercalating dyes.

Characterization of a Motile Cellular Domain Arising During the Amoebo-Flagellate Transformation of Physarum Polycephalum

1980 ◽  
Vol 38 ◽  
pp. 552-553
Author(s):  
K.I. Pagh ◽  
M.R. Adelman
Keyword(s):  
Cell Shape ◽  
Physarum Polycephalum ◽  
Slime Mold ◽  
Live Cells ◽  
Cellular Domain

Unicellular amoebae of the slime mold Physarum polycephalum undergo marked changes in cell shape and motility during their conversion into flagellate swimming cells (l). To understand the processes underlying motile activities expressed during the amoebo-flagellate transformation, we have undertaken detailed investigations of the organization, formation and functions of subcellular structures or domains of the cell which are hypothesized to play a role in movement. One focus of our studies is on a structure, termed the “ridge” which appears as a flattened extension of the periphery along the length of transforming cells (Fig. 1). Observations of live cells using Nomarski optics reveal two types of movement in this region:propagation of undulations along the length of the ridge and formation and retraction of filopodial projections from its edge. The differing activities appear to be associated with two characteristic morphologies, illustrated in Fig. 1.

A new facile and efficient synthesis of trans-(+)-sobrerol by biotransformation of α-pinene using extremophiles microorganisms

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
LA Vilaseca ◽  
J Quillaguamán ◽  
L Fuentes ◽  
O Sterner
Keyword(s):  
Efficient Synthesis

A Photoactivable Formaldehyde Donor with Fluorescence Monitoring Reveals Threshold to Arrest Cell Migration

2019 ◽  
Author(s):  
Lukas P Smaga ◽  
Nicholas W Pino ◽  
Gabriela E Ibarra ◽  
Vishnu Krishnamurthy ◽  
Jefferson Chan
Keyword(s):  
Wound Healing ◽  
Cell Migration ◽  
Fluorescence Enhancement ◽  
Biological Effects ◽  
Cellular Systems ◽  
Live Cells ◽  
First Report ◽  
Cell Lysate ◽  
Intracellular Release ◽  
Biological Analytes

Controlled light-mediated delivery of biological analytes enables the investigation of highly reactivity molecules within cellular systems. As many biological effects are concentration dependent, it is critical to determine the location, time, and quantity of analyte donation. In this work, we have developed the first photoactivatable donor for formaldehyde (FA). Our optimized photoactivatable donor, photoFAD-3, is equipped with a fluorescence readout that enables monitoring of FA release with a concomitant 139-fold fluorescence enhancement. Tuning of photostability and cellular retention enabled quantification of intracellular FA release through cell lysate calibration. Application of photoFAD-3 uncovered the concentration range necessary for arresting wound healing in live cells. This marks the first report where a photoactivatable donor for any analyte has been used to quantify intracellular release.

α-Methylene-β-Lactone Probe for Measuring Live-Cell Reactions of Small Molecules

2020 ◽  
Author(s):  
Lei Wang ◽  
Louis Riel ◽  
Bekim Bajrami ◽  
Bin Deng ◽  
Amy Howell ◽  
...  
Keyword(s):  
Mass Spectra ◽  
Live Cell ◽  
Live Cells ◽  
The Novel ◽  
Proteomics Analysis ◽  
Chemical Proteomics ◽  
Tandem Mass Spectra ◽  
Modified Peptides ◽  
Covalent Probes ◽  
Ht 29

The novel use of the α-methylene-β-lactone (MeLac) moiety as a warhead of multiple electrophilic sites is reported. In this study, we demonstrate that a MeLac-alkyne is a competent covalent probe and reacts with diverse proteins in live cells. Proteomics analysis of affinity-enriched samples identifies probe-reacted proteins, resolves their modified peptides/residues, and thus characterizes probe-protein reactions. Unique methods are developed to evaluate confidence in the identification of the reacted proteins and modified peptides. Tandem mass spectra of the peptides reveal that MeLac reacts with nucleophilic cysteine, serine, lysine, threonine, and tyrosine residues, through either Michael addition or acyl addition. A peptide-centric proteomics platform, using MeLac-alkyne as the measurement probe, successfully analyzes the Orlistat selectivity in live HT-29 cells. MeLac is a versatile warhead demonstrating enormous potential to expedite the development of covalent probes and inhibitors in interrogating protein (re)activity. MeLac-empowered platforms in chemical proteomics are widely adaptable for measuring the live-cell action of reactive molecules.

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