n-(4-(2-benzimidazolyl)phenyl)maleimide and fluorescein-5-isothiocyanate

n-(4-(2-benzimidazolyl)phenyl)maleimide has been researched along with fluorescein-5-isothiocyanate in 2 studies

Compound Research Comparison

Studies (n-(4-(2-benzimidazolyl)phenyl)maleimide)	Trials (n-(4-(2-benzimidazolyl)phenyl)maleimide)	Recent Studies (post-2010) (n-(4-(2-benzimidazolyl)phenyl)maleimide)	Studies (fluorescein-5-isothiocyanate)	Trials (fluorescein-5-isothiocyanate)	Recent Studies (post-2010) (fluorescein-5-isothiocyanate)
22	0	0	8,493	33	2,090

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Adachi, Y; Kai, D; Kaya, S; Nakamura, Y; Taniguchi, K	1
Mårdh, S; Taniguchi, K	1

Other Studies

2 other study(ies) available for n-(4-(2-benzimidazolyl)phenyl)maleimide and fluorescein-5-isothiocyanate

Article	Year
Different susceptibility to phospholipase A2 treatment of the fluorescence intensity changes in the vicinity of Cys-964 and Lys-501 in the alpha-chain of probe-labeled Na+,K(+)-ATPase. Journal of biochemistry, 1994, Volume: 115, Issue:3 Topics: Acrylamides; Animals; Binding Sites; Cysteine; Fluorescein-5-isothiocyanate; Fluorescence Polarization; Fluorescent Dyes; Hydrogen Bonding; Kidney; Lysine; Maleimides; Models, Molecular; Phospholipases A; Phospholipases A2; Polyethylene Glycols; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Swine	1994
Reversible changes in the fluorescence energy transfer accompanying formation of reaction intermediates in probe-labeled (Na+,K+)-ATPase. The Journal of biological chemistry, 1993, Jul-25, Volume: 268, Issue:21 Topics: Acetates; Animals; Energy Transfer; Fluorescein-5-isothiocyanate; Fluorescence; Kidney; Maleimides; Oligomycins; Potassium; Protein Conformation; Sodium; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Sulfhydryl Reagents; Swine	1993

Article

Year

Different susceptibility to phospholipase A2 treatment of the fluorescence intensity changes in the vicinity of Cys-964 and Lys-501 in the alpha-chain of probe-labeled Na+,K(+)-ATPase.

Journal of biochemistry, 1994, Volume: 115, Issue:3

Topics: Acrylamides; Animals; Binding Sites; Cysteine; Fluorescein-5-isothiocyanate; Fluorescence Polarization; Fluorescent Dyes; Hydrogen Bonding; Kidney; Lysine; Maleimides; Models, Molecular; Phospholipases A; Phospholipases A2; Polyethylene Glycols; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Swine

1994

Reversible changes in the fluorescence energy transfer accompanying formation of reaction intermediates in probe-labeled (Na+,K+)-ATPase.

The Journal of biological chemistry, 1993, Jul-25, Volume: 268, Issue:21

Topics: Acetates; Animals; Energy Transfer; Fluorescein-5-isothiocyanate; Fluorescence; Kidney; Maleimides; Oligomycins; Potassium; Protein Conformation; Sodium; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Sulfhydryl Reagents; Swine

1993