User:Alexander Berchansky
From Proteopedia
(Difference between revisions)
| Line 17: | Line 17: | ||
*[[Journal:Acta Cryst D:S2059798318000050|A DNA structural alphabet provides new insight into DNA flexibility]] | *[[Journal:Acta Cryst D:S2059798318000050|A DNA structural alphabet provides new insight into DNA flexibility]] | ||
*[[Journal:Acta Cryst F:S1744309112050270|Crystal structure of ADL1, a plant-specific homologue of the universal diaminopimelate amino transferase enzyme of lysine biosynthesis]] | *[[Journal:Acta Cryst F:S1744309112050270|Crystal structure of ADL1, a plant-specific homologue of the universal diaminopimelate amino transferase enzyme of lysine biosynthesis]] | ||
| + | *[[Journal:Acta Cryst F:S1744309112003326|Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae]] | ||
Revision as of 12:14, 4 June 2018
Dr. Alexander Berchansky, Ph.D., Israel Structural Proteomics Center, Weizmann Institute of Science
Interesting pages:
- Acetylcholinesterase
- AChE inhibitors and substrates
- Mutations in BRCA1/BARD1 RING-domain heterodimer
- Mutations in Brca1 BRCT Domains
- Missense Mutations in Phenylalanine Hydroxylase
- A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification
- Phosphofructokinase (PFK)
- Alcohol dehydrogenase
- Beta-glucosidase
- Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations
- A DNA structural alphabet provides new insight into DNA flexibility
- Crystal structure of ADL1, a plant-specific homologue of the universal diaminopimelate amino transferase enzyme of lysine biosynthesis
- Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae
