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Plasmepsins
Colin Berry
,
Daniel E. Goldberg
Division of Infectious Diseases
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
Institute of Clinical and Translational Sciences (ICTS)
DBBS - Molecular Cell Biology
DBBS - Molecular Microbiology and Microbial Pathogenesis
DBBS - Biochemistry, Biophysics, and Structural Biology
Research output
:
Chapter in Book/Report/Conference proceeding
›
Chapter
›
peer-review
Overview
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Chemistry
Crystal Structure
100%
Ser-Gly
100%
Disulfide
100%
Structural Chemistry
100%
Thr-Asp
100%
Amino Acid
100%
Molecular Model
100%
Hemoglobins
100%
Pepstatin
100%
Globin
100%
Asp-Ser
100%
Biochemistry, Genetics and Molecular Biology
Active Site
100%
Crystal Structure
50%
Amino Acids
50%
Orthology
50%
Precursor
50%
Cathepsin D
50%
Molecular Model
50%
Hope
50%
Protease
50%
Disulfide Bond
50%
Hemoglobins
50%
Protease
50%
Pepstatin
50%
Globin
50%
Keyphrases
Plasmepsin I
100%
Plasmepsin
100%
Active Sites
40%
Aspartic Protease
40%
Orthologs
20%
Mature Form
20%
Selective Inhibitor
20%
Globin
20%
Optimum pH
20%
Cathepsin D
20%
Amino Acid Content
20%
Disulfide Bond
20%
Molecular Model
20%
Human Hemoglobin
20%
Microgram
20%
Biological Aspects
20%
Pepstatin A
20%
Modeled Structure
20%
Structural Chemistry
20%
CRISTAL
20%
Intraerythrocytic
20%
Conformational Differences
20%
Pharmacology, Toxicology and Pharmaceutical Science
Plasmepsin I
100%
Aspartic Proteinase
40%
Amino Acid
20%
Cathepsin D
20%
Disulfide Bond
20%
Pepstatin
20%
Hemoglobins
20%
Globin
20%
Plasmepsin II
20%