phenylalanine and congo red

phenylalanine has been researched along with congo red in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's5 (83.33)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Azriel, R; Gazit, E1
Gordon, DJ; Meredith, SC1
Almeida, FC; Ferrão-Gonzales, AD; Ferreira, A; Foguel, D; Juliano, L; Moreau, VH; Robbs, BK; Silva, JL; Valente, AP1
Keasling, JD; Muller, SJ; Wang, K1
Bemporad, F; Chiti, F; Stefani, M; Taddei, N1
Kennan, RM; Pike, RN; Porter, CJ; Reboul, C; Reeve, SB; Rood, JI; Smith, AI; Steer, DL; Whisstock, JC; Wijeyewickrema, LC; Wong, W1

Other Studies

6 other study(ies) available for phenylalanine and congo red

ArticleYear
Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation.
    The Journal of biological chemistry, 2001, Sep-07, Volume: 276, Issue:36

    Topics: Alanine; Amino Acid Sequence; Amyloid; Asparagine; Coloring Agents; Congo Red; Glycine; Humans; Islet Amyloid Polypeptide; Kinetics; Light; Microscopy, Electron; Models, Chemical; Molecular Sequence Data; Peptides; Phenylalanine; Protein Binding; Scattering, Radiation; Sequence Homology, Amino Acid; Time Factors

2001
Probing the role of backbone hydrogen bonding in beta-amyloid fibrils with inhibitor peptides containing ester bonds at alternate positions.
    Biochemistry, 2003, Jan-21, Volume: 42, Issue:2

    Topics: Amino Acid Sequence; Amyloid beta-Peptides; Benzothiazoles; Congo Red; Cross-Linking Reagents; Diphenylhexatriene; Esters; Fluorescent Dyes; Humans; Hydrogen Bonding; Molecular Sequence Data; Peptide Fragments; Phenylalanine; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Thiazoles; Ultracentrifugation

2003
Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species.
    The Journal of biological chemistry, 2005, Oct-14, Volume: 280, Issue:41

    Topics: Amyloid; Amyloid beta-Peptides; Anilino Naphthalenesulfonates; Animals; Anions; Benzothiazoles; Biochemistry; Cell Line; Chromatography; Congo Red; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescent Dyes; Hydrogen-Ion Concentration; Kinetics; Light; Lysine; Magnetic Resonance Spectroscopy; Mice; Micelles; Models, Chemical; Models, Molecular; Molecular Conformation; Molecular Weight; Naphthalenesulfonates; Peptide Fragments; Peptides; Phenylalanine; Prions; Protein Structure, Secondary; Scattering, Radiation; Sodium Dodecyl Sulfate; Spectrophotometry; Static Electricity; Sulfonic Acids; Temperature; Tetrazolium Salts; Thiazoles; Time Factors

2005
Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides.
    International journal of biological macromolecules, 2005, Sep-15, Volume: 36, Issue:4

    Topics: Alanine; Amino Acid Motifs; Amyloid; Benzothiazoles; Circular Dichroism; Congo Red; Gene Library; Glycine; Hydrogel, Polyethylene Glycol Dimethacrylate; Isoleucine; Leucine; Macromolecular Substances; Microscopy, Electron, Scanning; Microscopy, Electron, Transmission; Models, Molecular; Peptides; Phenylalanine; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Temperature; Thiazoles; Ultraviolet Rays; Valine; X-Ray Diffraction

2005
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.
    Protein science : a publication of the Protein Society, 2006, Volume: 15, Issue:4

    Topics: Acid Anhydride Hydrolases; Acylphosphatase; Amino Acid Substitution; Amyloid; Benzothiazoles; Birefringence; Circular Dichroism; Congo Red; Data Interpretation, Statistical; Humans; Hydrophobic and Hydrophilic Interactions; Muscles; Phase Transition; Phenylalanine; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Thiazoles; Trifluoroethanol; Tyrosine

2006
S1 pocket of a bacterially derived subtilisin-like protease underpins effective tissue destruction.
    The Journal of biological chemistry, 2011, Dec-09, Volume: 286, Issue:49

    Topics: Amino Acids; Animals; Bacterial Proteins; Congo Red; Crystallization; Crystallography, X-Ray; Dichelobacter nodosus; Fibronectins; Foot Rot; Humans; Kinetics; Leucine; Models, Biological; Models, Molecular; Phenylalanine; Protein Structure, Tertiary; Serine Endopeptidases; Sheep; Subtilisin

2011