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Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution
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title
Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution
(English)
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main subject
crystal structure
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author
Johann Deisenhofer
series ordinal
3
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author name string
H Zhang
series ordinal
1
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M C Seabra
series ordinal
2
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publication date
15 March 2000
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published in
Structure
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volume
8
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issue
3
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page(s)
241-51
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cites work
Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes
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Protein prenylation: genes, enzymes, targets, and functions.
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Protein prenylation: a mediator of protein-protein interactions
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Membrane association and targeting of prenylated Ras-like GTPases
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Protein prenylation: molecular mechanisms and functional consequences
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Protein prenyltransferases
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Protein prenylation in eukaryotic microorganisms: genetics, biology and biochemistry
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Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit
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Tetrapeptide inhibitors of protein farnesyltransferase: amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation
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Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides
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Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
1 reference
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Protein farnesyltransferase: structure and implications for substrate binding
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Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
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Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue
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Mad Bet for Rab
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Rab GTPases: master regulators of membrane trafficking
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The diversity of Rab proteins in vesicle transport
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Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A
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Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex
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Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product
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Identifiers
DOI
10.1016/S0969-2126(00)00102-7
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Fatcat ID
release_g376chkpfjer3oyucotl47ufaa
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PubMed ID
10745007
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