lysyllysine has been researched along with transferrin in 5 studies
| Studies (lysyllysine) | Trials (lysyllysine) | Recent Studies (post-2010) (lysyllysine) | Studies (transferrin) | Trials (transferrin) | Recent Studies (post-2010) (transferrin) |
|---|---|---|---|---|---|
| 50 | 0 | 16 | 17,596 | 554 | 3,141 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 5 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Baker, EN; Bewley, MC; He, QY; MacGillivray, RT; Mason, AB; Smith, CA; Woodworth, RC | 1 |
| Baker, EN; Baker, HM; He, QY; MacGillivray, RT; Mason, AB; Nurizzo, D; Woodworth, RC | 1 |
| Alonso, MA; Ballesta, J; Batista, A; MartÃnez-Menárguez, JA; Puertollano, R | 1 |
| Anderson, BF; Arcus, VL; Baker, EN; Jameson, GB; Peterson, NA; Tweedie, JW | 1 |
| Baker, EN; Baker, HM; Mason, AB; Nurizzo, D | 1 |
5 other study(ies) available for lysyllysine and transferrin
| Article | Year |
|---|---|
Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "trigger" but does not significantly affect iron release.
Topics: Binding Sites; Crystallography, X-Ray; Dipeptides; Glutamic Acid; Histidine; Humans; Iron; Mutagenesis, Site-Directed; Protein Binding; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Transferrin | 2000 |
Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin.
Topics: Alanine; Amino Acid Substitution; Animals; Binding Sites; Carrier Proteins; Cations; Cell Line; Conserved Sequence; Cricetinae; Crystallography, X-Ray; Dipeptides; Humans; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Iron-Binding Proteins; Kinetics; Lysine; Mutagenesis, Site-Directed; Peptide Fragments; Recombinant Proteins; Transferrin; Transferrin-Binding Proteins | 2001 |
An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells.
Topics: Adaptor Protein Complex gamma Subunits; Amino Acid Motifs; Animals; Antibodies, Monoclonal; Biological Transport; Biotinylation; Caveolin 1; Caveolins; Cell Line; Cell Membrane; Detergents; Dipeptides; DNA; Dogs; Electrophoresis, Polyacrylamide Gel; Endocytosis; Endosomes; Epithelial Cells; Hemagglutinin Glycoproteins, Influenza Virus; Immunoblotting; Kidney; Membrane Proteins; Membrane Transport Proteins; Microscopy, Confocal; Microscopy, Immunoelectron; Mutation; Myelin and Lymphocyte-Associated Proteolipid Proteins; Myelin Proteins; Protein Structure, Tertiary; Proteolipids; Transfection; Transferrin | 2001 |
"Dilysine trigger" in transferrins probed by mutagenesis of lactoferrin: crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin.
Topics: Amino Acid Substitution; Animals; Arginine; Binding Sites; Cell Line; Cricetinae; Crystallization; Crystallography, X-Ray; Dipeptides; Glutamic Acid; Glycine; Humans; Iron; Lactoferrin; Leucine; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Recombinant Proteins; Transferrin | 2002 |
Structures of two mutants that probe the role in iron release of the dilysine pair in the N-lobe of human transferrin.
Topics: Crystallography, X-Ray; Dipeptides; Humans; Iron; Models, Molecular; Mutation; Transferrin | 2007 |