1,8-i-aedans has been researched along with cysteine in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (25.00) | 18.7374 |
| 1990's | 3 (37.50) | 18.2507 |
| 2000's | 3 (37.50) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Corino, GL; Gorman, JJ; Mitchell, SJ | 1 |
| Chiu, SS; Lewis, PN | 1 |
| Corbalan-Garcia, S; Gomez-Fernandez, JC; Teruel, JA | 1 |
| Biemann, K; Riordan, JF; Sturrock, ED; Wu, Z; Yu, XC | 1 |
| Fujiwara, K; Kojima, S; Onishi, H | 1 |
| Hemminga, MA; Meijer, AB; Spruijt, RB; Wolfs, CJ | 1 |
| Hemminga, MA; Spruijt, RB; Wolfs, CJ | 1 |
| Carag, C; Discher, DE; Johnson, CP; Speicher, DW; Tang, HY | 1 |
8 other study(ies) available for 1,8-i-aedans and cysteine
| Article | Year |
|---|---|
Fluorescent labeling of cysteinyl residues. Application to extensive primary structure analysis of proteins on a microscale.
Topics: Affinity Labels; Amino Acids; Animals; Chickens; Chromatography, High Pressure Liquid; Cysteine; Hydrolysis; Insulin; Microchemistry; Naphthalenesulfonates; Ovalbumin; Peptides; Proteins; Serum Albumin, Bovine; Spectrometry, Fluorescence | 1987 |
Effect of histone H3 sulfhydryl modifications on histone-histone interactions and nucleosome formation and structure.
Topics: Animals; Cattle; Chickens; Cysteine; Disulfides; Fluoresceins; Guanidines; Histones; Iodoacetamide; Iodoacetates; Macromolecular Substances; Naphthalenesulfonates; Nucleosomes; Protein Binding; Protein Denaturation; Sulfhydryl Compounds; Thymus Gland | 1980 |
Intramolecular distances within the Ca(2+)-ATPase from sarcoplasmic reticulum as estimated through fluorescence energy transfer between probes.
Topics: 4-Chloro-7-nitrobenzofurazan; Animals; Binding Sites; Calcium-Transporting ATPases; Cysteine; Energy Transfer; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Maleimides; Naphthalenesulfonates; Rabbits; Sarcoplasmic Reticulum; Spectrometry, Fluorescence | 1993 |
Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications.
Topics: Amino Acid Sequence; Chromatography, High Pressure Liquid; Cyanogen Bromide; Cysteine; Disulfides; Fluorescence; Humans; Male; Metalloendopeptidases; Molecular Sequence Data; Naphthalenesulfonates; Peptide Fragments; Peptidyl-Dipeptidase A; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfhydryl Reagents; Testis; Trypsin | 1996 |
SH1 (cysteine 717) of smooth muscle myosin: its role in motor function.
Topics: Amino Acid Sequence; Animals; Base Sequence; Chickens; Cysteine; DNA Primers; Molecular Sequence Data; Muscle, Smooth; Myosins; Naphthalenesulfonates; Recombinant Proteins | 1999 |
Membrane assembly of the bacteriophage Pf3 major coat protein.
Topics: Amino Acid Sequence; Bacteriophage M13; Capsid; Capsid Proteins; Cysteine; Inovirus; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Naphthalenesulfonates; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylglycerols; Phospholipids; Pseudomonas aeruginosa; Pseudomonas Phages; Spectrometry, Fluorescence; Virus Assembly | 2000 |
Membrane assembly of M13 major coat protein: evidence for a structural adaptation in the hinge region and a tilted transmembrane domain.
Topics: Amino Acid Sequence; Bacteriophage M13; Capsid Proteins; Circular Dichroism; Cysteine; Fluorescent Dyes; Lipid Bilayers; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Naphthalenesulfonates; Phospholipids; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Sulfhydryl Reagents; Virus Assembly | 2004 |
Forced unfolding of proteins within cells.
Topics: Chromatography, Liquid; Cysteine; Cytoskeletal Proteins; Erythrocytes; Fluorescence; Fluorescent Antibody Technique; Fluorescent Dyes; Heterocyclic Compounds, 4 or More Rings; Humans; Mesenchymal Stem Cells; Naphthalenesulfonates; Nonmuscle Myosin Type IIA; Protein Conformation; Protein Folding; Protein Structure, Quaternary; Protein Structure, Tertiary; Spectrin; Stress, Mechanical; Tandem Mass Spectrometry; Temperature; Vimentin | 2007 |