Profiling and Validation of Live‐Cell Protein Methylation with Engineered Enzymes and Methionine Analogues

2021 ◽  
Vol 1 (8) ◽  
Author(s):  
Nicole Weiss ◽  
Chamara Seneviranthe ◽  
Ming Jiang ◽  
Ke Wang ◽  
Minkui Luo
Keyword(s):  
Live Cell ◽  
Cell Protein ◽  
Protein Methylation

scholarly journals Red-Shifted Aminated Derivatives of GFP Chromophore for Live-Cell Protein Labeling with Lipocalins

2018 ◽  
Vol 19 (12) ◽  
pp. 3778 ◽  
Author(s):  
Nina Bozhanova ◽  
Mikhail Baranov ◽  
Nadezhda Baleeva ◽  
Alexey Gavrikov ◽  
Alexander Mishin
Keyword(s):  
Green Fluorescent Protein ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Fluorescent Protein ◽  
Live Cell ◽  
Protein Labeling ◽  
Cell Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent ◽  
Derivatives Of

Fluorogens are an attractive type of dye for imaging applications, eliminating time-consuming washout steps from staining protocols. With just a handful of reported fluorogen-protein pairs, mostly in the green region of spectra, there is a need for the expansion of their spectral range. Still, the origins of solvatochromic and fluorogenic properties of the chromophores suitable for live-cell imaging are poorly understood. Here we report on the synthesis and labeling applications of novel red-shifted fluorogenic cell-permeable green fluorescent protein (GFP) chromophore analogs.

Live‐Cell Protein Sulfonylation Based on Proximity‐driven N ‐Sulfonyl Pyridone Chemistry

2018 ◽  
Vol 57 (3) ◽  
pp. 659-662 ◽  
Author(s):  
Kazuya Matsuo ◽  
Yuki Nishikawa ◽  
Marie Masuda ◽  
Itaru Hamachi
Keyword(s):  
Live Cell ◽  
Cell Protein

Live‐Cell Protein Sulfonylation Based on Proximity‐driven N ‐Sulfonyl Pyridone Chemistry

2017 ◽  
Vol 130 (3) ◽  
pp. 667-670 ◽  
Author(s):  
Kazuya Matsuo ◽  
Yuki Nishikawa ◽  
Marie Masuda ◽  
Itaru Hamachi
Keyword(s):  
Live Cell ◽  
Cell Protein

Live-Cell Protein Modification by Boronate-Assisted Hydroxamic Acid Catalysis

2021 ◽  
Vol 143 (37) ◽  
pp. 14976-14980
Author(s):  
Christopher Adamson ◽  
Hidetoshi Kajino ◽  
Shigehiro A. Kawashima ◽  
Kenzo Yamatsugu ◽  
Motomu Kanai
Keyword(s):  
Hydroxamic Acid ◽  
Protein Modification ◽  
Acid Catalysis ◽  
Live Cell ◽  
Cell Protein

Abstract LB-062: A live-cell, protein-protein interaction assay identified inhibitors of KRAS4b-G12D interaction with full-length RAF1

2020 ◽  
Author(s):  
John Columbus ◽  
Thomas J. Turbyville ◽  
Vanessa Wall ◽  
Dominic Esposito ◽  
David A. Barda ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Live Cell ◽  
Full Length ◽  
Cell Protein ◽  
Protein Protein Interaction

scholarly journals Live-cell protein labelling with nanometre precision by cell squeezing

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Alina Kollmannsperger ◽  
Armon Sharei ◽  
Anika Raulf ◽  
Mike Heilemann ◽  
Robert Langer ◽  
...  
Keyword(s):  
Live Cell ◽  
Cell Protein ◽  
Protein Labelling

scholarly journals Distance-Matched Tagging Sequence Optimizes Live-Cell Protein Labeling by a Biarsenical Fluorescent Reagent AsCy3_E

ACS Omega ◽  
2018 ◽  
Vol 3 (2) ◽  
pp. 2104-2110 ◽  
Author(s):  
Karen A. Hecht ◽  
Yijia Xiong ◽  
Daniel A. Barrack ◽  
Nicole R. Ford ◽  
Guritno Roesijadi ◽  
...  
Keyword(s):  
Live Cell ◽  
Protein Labeling ◽  
Cell Protein

scholarly journals A genetically encoded fluorescent tRNA is active in live-cell protein synthesis

2016 ◽  
Vol 45 (7) ◽  
pp. 4081-4093 ◽  
Author(s):  
Isao Masuda ◽  
Takao Igarashi ◽  
Reiko Sakaguchi ◽  
Ram G. Nitharwal ◽  
Ryuichi Takase ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Live Cell ◽  
Cell Protein

Immunogold labeling of CMP-KDO synthetase produced by recombinant E. Coli cells

1987 ◽  
Vol 45 ◽  
pp. 924-925
Author(s):  
F. A. Durum ◽  
R. G. Goldman ◽  
T. J. Bolling ◽  
M. F. Miller
Keyword(s):  
Inclusion Bodies ◽  
Large Scale ◽  
Recombinant Dna ◽  
Test System ◽  
Cell Protein ◽  
Gram Negative Bacteria ◽  
Cytoplasmic Inclusions ◽  
Isolation And Purification ◽  
E Coli ◽  
Low Concentrations

CMP-KDO synthetase (CKS) is an enzyme which plays a key role in the synthesis of LPS, an outer membrane component unique to gram negative bacteria. CKS activates KDO to CMP-KDO for incorporation into LPS. The enzyme is normally present in low concentrations (0.02% of total cell protein) which makes it difficult to perform large scale isolation and purification. Recently, the gene for CKS from E. coli was cloned and various recombinant DNA constructs overproducing CKS several thousandfold (unpublished data) were derived. Interestingly, no cytoplasmic inclusions of overproduced CKS were observed by EM (Fig. 1) which is in contrast to other reports of large proteinaceous inclusion bodies in various overproducing recombinant strains. The present immunocytochemical study was undertaken to localize CKS in these cells.Immune labeling conditions were first optimized using a previously described cell-free test system. Briefly, this involves soaking small blocks of polymerized bovine serum albumin in purified CKS antigen and subjecting them to various fixation, embedding and immunochemical conditions.

Sign in / Sign up

Export Citation Format

Share Document