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User:Alexander Berchansky

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CRISPR type VI (Cas13a (previously known as C2c2), Cas13b, Cas13c, Cas13d) - see [[CRISPR type VI]]
CRISPR type VI (Cas13a (previously known as C2c2), Cas13b, Cas13c, Cas13d) - see [[CRISPR type VI]]
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*[[Journal:Acta Cryst D:S0907444911047251|Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations]]
 
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*[[Journal:Acta Cryst D:S2059798318000050|A DNA structural alphabet provides new insight into DNA flexibility]]
 
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*[[Journal:Acta Cryst D:S2059798319000676|Crystal structures of pyrrolidone-carboxylate peptidase I from ''Deinococcus radiodurans'' reveal the mechanism of L-pyroglutamate recognition]]
 
*[[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]]
*[[Journal:Acta Cryst F:S1744309112003326|Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae]]
Line 154: Line 151:
*[[Journal:JBSD:41|Molecular Mechanism of HIV-1 gp120 Mutations That Reduce CD4 Binding Affinity]]
*[[Journal:JBSD:41|Molecular Mechanism of HIV-1 gp120 Mutations That Reduce CD4 Binding Affinity]]
*[[Book:Structural Proteomics and its Impact on the Life Sciences:6]]‎
*[[Book:Structural Proteomics and its Impact on the Life Sciences:6]]‎
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*[[Journal:Acta Cryst D:S0907444911047251|Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations]]
 +
*[[Journal:Acta Cryst D:S2059798318000050|A DNA structural alphabet provides new insight into DNA flexibility]]
 +
*[[Journal:Acta Cryst D:S2059798319000676|Crystal structures of pyrrolidone-carboxylate peptidase I from ''Deinococcus radiodurans'' reveal the mechanism of L-pyroglutamate recognition]]
*[[Journal:Acta Cryst D:S2059798318014900|Structure of the AmyC GH13 alpha-amylase from Alicyclobacillus sp, reveals accommodation of starch branching points in the alpha-amylase family]]
*[[Journal:Acta Cryst D:S2059798318014900|Structure of the AmyC GH13 alpha-amylase from Alicyclobacillus sp, reveals accommodation of starch branching points in the alpha-amylase family]]
*[[Journal:Acta Cryst D:S2059798318017047|The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer]]
*[[Journal:Acta Cryst D:S2059798318017047|The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer]]

Revision as of 11:03, 3 July 2019

Dr. Alexander Berchansky, Ph.D., Israel Structural Proteomics Center, Weizmann Institute of Science

My interesting pages:

CRISPR-Cas (under development):

Classification according to the Wikipedia page CRISPR [1] with additions

CRISPR Class 1 uses a complex of multiple Cas proteins

CRISPR type I (Cas3)

CRISPR type I-A (Cascade) - see CRISPR subtype I-A

CRISPR type I-B (Cascade) - see CRISPR subtype I-B

CRISPR type I-C (Cascade) - see CRISPR subtype I-C

CRISPR type I-D (Cas10d)

CRISPR type I-E (Cascade) - see CRISPR subtype I-E

CRISPR type I-F (Csy1, Csy2, Csy3) - see CRISPR subtype I-F

CRISPR type I-U (GSU0054)

CRISPR type III (Cas10)

CRISPR type III-A (Csm complex) - see CRISPR subtype III-A (Csm complex)

CRISPR type III-B (Cmr complex)

CRISPR type III-C (Cas10 or Csx11)

CRISPR type III-D (Csx10)

CRISPR type Orphan

CRISPR type IV (Csf1)

CRISPR type IV-A

CRISPR type IV-B

CRISPR Class 2 uses a single large Cas protein

CRISPR type II-A - see CRISPR-Cas9

CRISPR type II-B (Cas4)

CRISPR type II-C

CRISPR type V (Cpf1, C2c1, C2c3) - see CRISPR type V

CRISPR type VI (Cas13a (previously known as C2c2), Cas13b, Cas13c, Cas13d) - see CRISPR type VI

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Eran Hodis

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