aspartic acid has been researched along with lactoferrin in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (20.00) | 18.2507 |
| 2000's | 1 (20.00) | 29.6817 |
| 2010's | 3 (60.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Baker, EN; Bland, T; Day, CL; Faber, HR; Norris, GE; Tweedie, JW | 1 |
| Anderson, BF; Baker, EN; Breyer, WA; Day, CL; Jameson, GB; Tweedie, JW | 1 |
| Benaïssa, M; Hardivillé, S; Hoedt, E; Mariller, C; Pierce, A | 1 |
| Buszewski, B; Liu, JJ; Milanowski, M; Pomastowski, P; Rafińska, K; Sprynskyy, M; Yi, M; Žuvela, P | 1 |
| Bertamino, A; Campiglia, P; Carotenuto, A; Gomez-Monterrey, IM; Grieco, P; Novellino, E; Pepe, G; Sala, M; Scala, MC; Spensiero, A | 1 |
5 other study(ies) available for aspartic acid and lactoferrin
| Article | Year |
|---|---|
Altered domain closure and iron binding in transferrins: the crystal structure of the Asp60Ser mutant of the amino-terminal half-molecule of human lactoferrin.
Topics: Animals; Anions; Aspartic Acid; Binding Sites; Cell Line; Cricetinae; Crystallography, X-Ray; Humans; Iron; Lactoferrin; Metals; Mutagenesis, Site-Directed; Protein Conformation; Serine; Structure-Activity Relationship; Transferrin | 1996 |
Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form.
Topics: Amino Acid Substitution; Arginine; Aspartic Acid; Crystallization; Crystallography, X-Ray; Humans; Lactoferrin; Models, Molecular; Mutation; Protein Conformation; Protein Structure, Tertiary; Transferrin | 2002 |
O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin.
Topics: Acetylglucosamine; Aspartic Acid; Carbohydrates; Cell Line; DNA; Genes, Reporter; Humans; Lactoferrin; Microscopy, Fluorescence; Mutagenesis, Site-Directed; Phosphorylation; Promoter Regions, Genetic; Serine; Transcription, Genetic; Transcriptional Activation | 2010 |
Silver-Lactoferrin Nanocomplexes as a Potent Antimicrobial Agent.
Topics: Animals; Anti-Infective Agents; Aspartic Acid; Bacteria; Binding Sites; Cattle; Drug Design; Glutamic Acid; Ions; Lactoferrin; Metal Nanoparticles; Microbial Sensitivity Tests; Molecular Dynamics Simulation; Nanotechnology; Protein Binding; Pseudomonas aeruginosa; Quantum Theory; Silver; Software; Surface Properties | 2016 |
Investigation on side-product formation during the synthesis of a lactoferrin-derived lactam-bridged cyclic peptide.
Topics: Animals; Aspartic Acid; Cattle; Cyclization; Cysteine; Lactams; Lactoferrin; Peptides, Cyclic | 2018 |