Results 1 to 10 of about 1,124,962 (295)

A single-domain green fluorescent protein catenane [PDF]

Nature Communications, 2023
Natural proteins exhibit rich structural diversity based on the folds of an invariably linear chain. Macromolecular catenanes that cooperatively fold into a single domain do not belong to the current protein universe, and their design and synthesis open ...
Zhiyu Qu, Jing Fang, Yu-Xiang Wang, Yibin Sun, Yajie Liu, Wen-Hao Wu, Wen-Bin Zhang   +6 more
doaj   +2 more sources

A highly photostable and bright green fluorescent protein. [PDF]

Nat Biotechnol, 2022
The low photostability of fluorescent proteins is a limiting factor in many applications of fluorescence microscopy. Here we present StayGold, a green fluorescent protein (GFP) derived from the jellyfish Cytaeis uchidae.
Hirano M, Ando R, Shimozono S, Sugiyama M, Takeda N, Kurokawa H, Deguchi R, Endo K, Haga K, Takai-Todaka R, Inaura S, Matsumura Y, Hama H, Okada Y, Fujiwara T, Morimoto T, Katayama K, Miyawaki A.   +17 more
europepmc   +2 more sources

Herpes Simplex Virus Thymidine Kinase-Green Fluorescent Protein Fusion Gene: New Tool for Gene Transfer Studies and Gene Therapy

BioTechniques, 1998
Green fluorescent protein (GFP) and herpes simplex virus type-1 thymidine kinase (TK) are commonly used markers in gene transfer studies. The latter gene has also proven to be an effective tool in cancer “suicide” gene therapy.
Sami Loimas, Jarmo Wahlfors, Juhani Jänne   +2 more
doaj   +2 more sources

Bright and stable monomeric green fluorescent protein derived from StayGold. [PDF]

Nat Methods
The high brightness and photostability of the green fluorescent protein StayGold make it a particularly attractive probe for long-term live-cell imaging; however, its dimeric nature precludes its application as a fluorescent tag for some proteins.
Zhang H, Lesnov GD, Subach OM, Zhang W, Kuzmicheva TP, Vlaskina AV, Samygina VR, Chen L, Ye X, Nikolaeva AY, Gabdulkhakov A, Papadaki S, Qin W, Borshchevskiy V, Perfilov MM, Gavrikov AS, Drobizhev M, Mishin AS, Piatkevich KD, Subach FV.   +19 more
europepmc   +2 more sources

Improved blue, green, and red fluorescent protein tagging vectors for S. cerevisiae. [PDF]

PLoS ONE, 2013
Fluorescent protein fusions are a powerful tool to monitor the localization and trafficking of proteins. Such studies are particularly easy to carry out in the budding yeast Saccharomyces cerevisiae due to the ease with which tags can be introduced into ...
Sidae Lee, Wendell A Lim, Kurt S Thorn
doaj   +2 more sources

RNA Mimics of Green Fluorescent Protein [PDF]

Science, 2011
Selection for RNAs that bind and activate derivatives of the green fluorescent protein fluorophore yields a wide range of useful spectral properties.
Jeremy S, Paige, Karen Y, Wu, Samie R, Jaffrey   +2 more
openaire   +3 more sources

Green Fluorescent Protein SELEX: Immobilization Chemistry and His-Tag Epitope Bias. [PDF]

Angew Chem Int Ed Engl
Stangherlin S, Malloch T, Clarke AJ, Liu J.   +3 more
europepmc   +3 more sources

Synthetic Control of Green Fluorescent Protein [PDF]

Journal of the American Chemical Society, 2009
Semisynthetic green fluorescent proteins (GFPs) can be prepared by producing truncated GFPs recombinantly and assembling them with synthetic beta-strands of GFP. The yield from expressing the truncated GFPs is low, and the chromophore is either partially formed or not formed. An alternative method is presented in which full-length proteins are produced
Kevin P. Kent, Luke M. Oltrogge, Steven G. Boxer   +2 more
openalex   +3 more sources

Production and purification of outer membrane vesicles encapsulating green fluorescent protein from Escherichia coli: a step towards scalable OMV technologies. [PDF]

Front Bioeng Biotechnol
Torres-Vanegas JD, Rincon-Tellez N, Guzmán-Sastoque P, Valderrama-Rincon JD, Cruz JC, Reyes LH.   +5 more
europepmc   +3 more sources

Red fluorescent proteins engineered from green fluorescent proteins

Proceedings of the National Academy of Sciences, 2023
Fluorescent proteins (FPs) form a fluorophore through autocatalysis from three consecutive amino acid residues within a polypeptide chain. The two major groups, green FPs (GFPs) and red FPs (RFPs), have distinct fluorophore structures; RFPs have an extended π-conjugation system with an additional double bond.
Hiromi Imamura, Shiho Otsubo, Mizuho Nishida, Norihiro Takekawa, Katsumi Imada   +4 more
openaire   +2 more sources