Page last updated: 2024-09-05

l 35 and bezafibrate

l 35 has been researched along with bezafibrate in 4 studies

Compound Research Comparison

Studies
(l 35)
Trials
(l 35)
Recent Studies (post-2010)
(l 35)
Studies
(bezafibrate)
Trials
(bezafibrate)
Recent Studies (post-2010) (bezafibrate)
16051,335267324

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19901 (25.00)18.7374
1990's2 (50.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Abraham, DJ; Mahran, MA; Mehanna, AS; Randad, RS1
Abraham, DJ; Kellogg, GE; Wireko, FC1
Lalezari, I; Lalezari, P1
Carelli Alinovi, C; De Rosa, MC; Giardina, B; Russo, A1

Other Studies

4 other study(ies) available for l 35 and bezafibrate

ArticleYear
Allosteric modifiers of hemoglobin. 1. Design, synthesis, testing, and structure-allosteric activity relationship of novel hemoglobin oxygen affinity decreasing agents.
    Journal of medicinal chemistry, 1991, Volume: 34, Issue:2

    Topics: Allosteric Regulation; Aniline Compounds; Antisickling Agents; Chemical Phenomena; Chemistry; Hemoglobin A; Humans; Oxygen; Propionates; Structure-Activity Relationship

1991
Allosteric modifiers of hemoglobin. 2. Crystallographically determined binding sites and hydrophobic binding/interaction analysis of novel hemoglobin oxygen effectors.
    Journal of medicinal chemistry, 1991, Volume: 34, Issue:2

    Topics: Allosteric Site; Bezafibrate; Chemical Phenomena; Chemistry; Computers; Drug Interactions; Hemoglobins; Humans; Oxygen; Stereoisomerism; Structure-Activity Relationship; Urea; X-Ray Diffraction

1991
Synthesis and investigation of effects of 2-[4- [[(arylamino)carbonyl]amino]phenoxy]-2-methylpropionic acids on the affinity of hemoglobin for oxygen: structure-activity relationships.
    Journal of medicinal chemistry, 1989, Volume: 32, Issue:10

    Topics: Erythrocytes; Glycolates; Hemoglobins; Humans; In Vitro Techniques; Molecular Structure; Oxyhemoglobins; Phenoxyacetates; Propionates; Structure-Activity Relationship

1989
Binding modes of L35 to alpha- and beta-semihemoglobins: structural insights into the inequivalence of alpha- and beta-subunits of hemoglobin.
    Biochemical and biophysical research communications, 2007, Mar-16, Volume: 354, Issue:3

    Topics: Apoproteins; Bezafibrate; Binding Sites; Dimerization; Hemoglobins; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Ligands; Models, Molecular; Oxygen; Peptide Fragments; Phenylurea Compounds; Protein Subunits

2007