Proc. Cong Ding, Yage Chen, Haozheng Li, Bingyao Wang, Qi Wei, Huajun Tang, Shaokang Jia, Zhiyong He, Ping Wang, Xiang Zhou.

Here we describe a method, termed SILAC, for stable isotope labeling by amino acids in cell culture, for the in vivo incorporation of specific amino acids into all mammalian proteins. P. Berto, E.R. Spencer, K.A. Melanie D. White, Ziqing W. Zhao, Nicolas Plachta. Lechene Claude; Hillion Francois; McMahon Greg; Benson Douglas; Kleinfeld Alan M; Kampf J Patrick; Distel Daniel; Luyten Yvette; Bonventre Joseph; Hentschel Dirk; Park Kwon Moo; Ito Susumu; Schwartz Martin; Benichou Gilles; Slodzian Georges. Curr. Schipper-Krom, Sabine; Juenemann, Katrin; Jansen, Anne H.; Wiemhoefer, Anne; van den Nieuwendijk, Rianne; Smith, Donna L.; Hink, Mark A.; Bates, Gillian P.; Overkleeft, Hermen; Ovaa, Huib; Reits, Eric. Saar, Brian G.; Freudiger, Christian W.; Reichman, Jay; Stanley, C. Michael; Holtom, Gary R.; Xie, X. Sunney. (a) Spontaneous Raman spectrum of C–D peaks in HeLa cells incubated in optimized deuteration medium (red) displays a 50% increase when compared to that in the previously reported partial deuteration medium (blue) and is about 8 times higher than that using leucine-d10 (black) only. Zhilun Zhao, Yihui Shen, Fanghao Hu, Wei Min.

Raman scattering or the Raman effect / ˈ r ɑː m ən / is the inelastic scattering of photons by matter, meaning that there is an exchange of energy and a change in the light's direction. In this study, we use cephalochordate amphioxus (Branchiostroma belcheri, a living basal chordate) and zebrafish (Danio rerio), a vertebrate, as model animals and employ stimulated Raman microscopy (SRS), a newly developed label-free technique, to investigate notochord structure and chem. Advancing small ligands targeting RNA for better binding affinity and specificity: A study of structural influence through molecular design approach. Quant. Scale bar, 10 μm. The bright-field image shows the gross morphology of embryonic zebrafish at 24 hpf (dashed boxes). A review.

Pinkus, Jack L.; Charles, David; Chattoraj, Sati C. Deuterium-labeled 1,3,5(10)-estratriene-3,-17β-diol was used for the estn. You need an eReader or compatible software to experience the benefits of the ePub3 file format. lipids, cholesterol, and protein. Principle and experimental set‐up of stimulated Raman scattering (SRS) microscopy. anal.

Label-free live imaging allows us to obtain the whole animal's intact internal morphol., which is difficult to obtain through other mech. Chem. C.V. Raman, The molecular scattering of light.

Prescher, Jennifer A.; Bertozzi, Carolyn R. A review.

contrast is highly desirable in biomedical imaging. Herein, the authors report an imaging technique to visualize nascent proteins by harnessing the emerging stimulated Raman scattering (SRS) microscopy coupled with metabolic incorporation of deuterium-labeled amino acids.

the Altmetric Attention Score and how the score is calculated. Chem. Lett. A review.

Andresen, H. Rigneault, Background-free stimulated Raman spectroscopy and microscopy.

Octadeuterated all-trans-retinyl acetate dose of 1.5 mg was given to a volunteer and blood samples were collected over a 32-day period.

and sensitivity compared with magnetic resonance imaging.

In addn., the total quantity of certain ions present in the body can be detd. However, the selective visualization of a newly synthesized proteome in living systems with subcellular resoln. Tipping, Martin Lee, Alan Serrels, Valerie G. Brunton, Alison N. Hulme. Citations are the number of other articles citing this article, calculated by Crossref and updated daily.

Second, by tracking the methyl group (CH3) distribution attributed to pre-existing proteins, this platform also enables us to map protein degradation inside live cells. Chem.

Nat. J. Biomed. Biomed. Pages 8-1 to 8-10.

The hyperspectral stack of SRL images is further analyzed by a multivariate curve resoln.

Opt.

Toward this goal, we demonstrate hyperspectral stimulated Raman loss (SRL) imaging by intrapulse spectral scanning through a femtosecond pulse shaper.

H.J. Rev. 52, 2982d. Angew. Abstract. A 60× water objective (UPlanAPO/IR, 1.2 N.A., Olympus) is used for all cell imaging, and a 25× water objective (XLPlan N, 1.05 N.A., MP, Olympus) with both a high near-IR transmission and a large field of view is used for brain tissue and, For HeLa cells, cells were seeded on a coverslip in a Petri dish with 2 mL of regular medium for 20 h, which was then replaced with D-AA medium (or group I and group II D-AA media) for the designated amount of time. With one exception, this cleavage takes place regardless of the nature of the amino acid residue of βgal at the ubiquitin-βgal junction, thereby making it possible to expose different residues at the amino-termini of the otherwise identical βgal proteins. data were obtained by gas chromatog.-mass spectrometry. L. Wei et al., Imaging complex protein metabolism in live organisms by stimulated Raman scattering microscopy with isotope labeling.

Bennett, Eric J.; Shaler, Thomas A.; Woodman, Ben; Ryu, Kwon-Yul; Zaitseva, Tatiana S.; Becker, Christopher H.; Bates, Gillian P.; Schulman, Howard; Kopito, Ron R. Huntington's disease (HD) is a dominantly inherited neurodegenerative disorder caused by expansion of CAG triplet repeats in the huntingtin (HTT) gene (also called HD) and characterized by accumulation of aggregated fragments of polyglutamine-expanded HTT protein in affected neurons.

Stimulated Raman scattering (SRS) microscopy allows highly sensitive optical imaging based on vibrational spectroscopy without adding toxic or perturbative labels.
In our study, we focus on the hippocampus because it is the key region in brains that involves extensive protein synthesis.
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We thank J. Jackson and C. Dupre for assistance with the brain slices and J. C. Tapia, M. C. Wang, Z. Chen, D. Peterka, and R. Yuste for helpful discussions. This strategy should have broad applicability for imaging protein synthesis and for identifying proteins synthesized under various physiol. Cite as. Thus, this technique of nonlinear vibrational imaging of stable isotope incorporation will be a valuable tool to advance the authors' understanding of the complex spatial and temporal dynamics of newly synthesized proteome in vivo. Using these methods, we demonstrate quant.

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