A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity. - Wikidata - wikimedia - TriplyDB

A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity.

A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity.

http://www.wikidata.org/entity/Q37532652

about

Prenylation of a Rab1B mutant with altered GTPase activity is impaired in cell-free systems but not in intact mammalian cells Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases A tagging-via-substrate technology for detection and proteomics of farnesylated proteins Structure of mammalian protein geranylgeranyltransferase type-I The putative "switch 2" domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein The farnesyl transferase inhibitor RPR-130401 does not alter radiation susceptibility in human tumor cells with a K-Ras mutation in spite of large changes in ploidy and lamin B distribution Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart.Substrate specificity determinants in the farnesyltransferase beta-subunit.RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins.Evidence for prenylation-dependent targeting of a Ykt6 SNARE in Plasmodium falciparum Protein farnesyltransferase and protein prenylation in Plasmodium falciparum CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells TrkB-mediated activation of geranylgeranyltransferase I promotes dendritic morphogenesis G protein gamma subunits with altered prenylation sequences are properly modified when expressed in Sf9 cells.TcRho1, a farnesylated Rho family homologue from Trypanosoma cruzi: cloning, trans-splicing, and prenylation studies.Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities.Therapeutic intervention based on protein prenylation and associated modifications Geranylgeranyltransferase I is essential for dendritic development of cerebellar Purkinje cells.Porcine Liver Carboxylesterase Requires Polyisoprenylation for High Affinity Binding to Cysteinyl Substrates.Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma brucei Blocking oncogenic Ras signaling for cancer therapy.Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases.Mutant farnesyltransferase beta subunit of Saccharomyces cerevisiae that can substitute for geranylgeranyltransferase type I beta subunit.Lipid posttranslational modifications. Farnesyl transferase inhibitors.Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein Consequences of altered isoprenylation targets on a-factor export and bioactivity.Ajoene, a garlic compound, inhibits protein prenylation and arterial smooth muscle cell proliferation.RhoB prenylation is driven by the three carboxyl-terminal amino acids of the protein: evidenced in vivo by an anti-farnesyl cysteine antibody.GGTase-I deficiency reduces tumor formation and improves survival in mice with K-RAS-induced lung cancer.Clinical activity of farnesyl transferase inhibitors in hematologic malignancies: possible mechanisms of action.Identification of Ras farnesyltransferase inhibitors by microbial screening.Lipid-modified proteins as biomarkers for cardiovascular disease: a review.Single prenyl-binding site on protein prenyl transferases.Regulation of intracellular actin polymerization by prenylated cellular proteins.Fungal lipopeptide mating pheromones: a model system for the study of protein prenylation Genetic evidence for in vivo cross-specificity of the CaaX-box protein prenyltransferases farnesyltransferase and geranylgeranyltransferase-I in Saccharomyces cerevisiae Ras as a therapeutic target in hematologic malignancies.Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity

P2860

Q24529934-63E602CD-9DD6-4CAE-9195-278831FF6651 Q24530008-BA72F24D-3CBA-4D4C-AF57-92C4CD46ADAC Q24531139-5DBA4CF7-0B0D-442D-B124-4C2B725657A0 Q24562961-61F71E4E-6158-492B-A0A3-2F8C3993A6C3 Q24644688-C1269077-DF82-4B9F-8860-E3C568AFBD91 Q24657695-F8F11A3E-958F-4F23-AA55-60FBBE40E56D Q24805139-9D136FA6-1214-47D3-B1D0-50FDE38A8D4A Q27929835-D1D5A0DC-50C1-4C0B-B792-40B2CABA3507 Q27930129-8BD71986-340D-4AC4-A835-448D5CAF8E15 Q27936473-B0B84E79-F7CF-4CAA-9187-2764068ABCFA Q27973698-196A6A7E-FD52-4792-AC0F-AD4F56A79DB1 Q27973925-E997BEA3-A0E8-408A-A6F5-CFAE9D789B44 Q28299793-08D967E6-B1E6-43E9-9468-ED2920F08547 Q28567838-7107FE9D-1E8F-4D2A-A866-50FED36866DB Q28583900-9BF042F4-8530-4F84-A17E-83BC47CCEA74 Q30468687-76A96984-9A93-45C7-B400-1231CF55F86C Q30669934-64EB665C-F5DE-47C4-93A6-A3F2A4F2290C Q33514156-1DD31C1B-F65A-42A6-ADC8-6D3DA2ED3F93 Q33943379-0837ED11-8A9B-4F20-8076-6B105BE9930F Q33986654-53E224B6-1926-4C1B-8C7A-E3363658A834 Q34006187-E4096165-8BE5-4B13-ACC3-0B1194D6EE72 Q34034992-AA06C58D-0145-40B6-A636-22877DD9CC15 Q34311585-4404A434-FFEF-43EF-A79E-8BCA3C71843B Q34328046-E3F0785E-4B12-4788-9AB6-4D48A6AEB60B Q34649429-359CD163-4BBC-454C-A3AB-442CD530F694 Q34651253-38B6CE65-E85E-49EB-A04F-245682B1CC56 Q34728624-B77BAAA7-7986-42EB-99CA-151BD4D714C4 Q35038534-BD6F4C15-8F41-4C05-AA4B-25B255BD900D Q35045068-950947DD-E4B1-48CA-BA19-A01F39E19DB0 Q35331913-FE5B5943-5876-444B-923F-F8806D46C013 Q35762090-B3443779-F697-4AB1-AA5A-6A1349E67F0F Q35932017-B2F839ED-F2D2-4359-8E48-893C70263935 Q36165226-F3A153F9-E911-4939-9DCF-C36952F5D60F Q36271227-0ABA130A-090E-4159-8571-E1AB49E7F64F Q36522608-0A04AF7B-AB76-4890-80B9-C06FEE937F90 Q36531238-8AD501E7-89E6-4DFF-8219-43DE194C98AB Q36669959-AAA5EB29-4F2D-4C2F-930F-C937889F670A Q36690625-F62B7127-8258-4A5E-B5F0-927ACC375525 Q36866611-65CA68EB-082E-4DA9-BC5D-C9F209D8B465 Q37108753-FE48F524-5F58-4A9D-8B5E-E709FC3E3267

P2860

A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity.

http://www.wikidata.org/entity/Q37532652

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on June 1991

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A protein geranylgeranyltransf ...... otein prenylation specificity.

@en

A protein geranylgeranyltransf ...... otein prenylation specificity.

@nl

type

label

A protein geranylgeranyltransf ...... otein prenylation specificity.

@en

A protein geranylgeranyltransf ...... otein prenylation specificity.

@nl

prefLabel

A protein geranylgeranyltransf ...... otein prenylation specificity.

@en

A protein geranylgeranyltransf ...... otein prenylation specificity.

@nl

P1433

Q37532652-BBD78CB2-1D4D-445B-A7C1-0BD23C9F7AED

P1476

Q37532652-DA9EAFFF-25EF-43E8-B3A4-0F6CC6205362

P2093

Q37532652-36175029-89D9-4A32-B4A1-782D0DDB7307

Q37532652-57B88545-2106-4C33-B495-6767A2B184AA

Q37532652-B3919712-001D-4F12-8184-4028022685A9

Q37532652-BE24F86C-F364-40F8-B37D-9E6888EB5BB6

Q37532652-C568D479-1AE2-49A8-B055-F2236FE441D1

P2860

Q37532652-32F1B2B6-84AC-440E-8C66-92A645219390

Q37532652-37EF837D-03C6-4AA2-BCEF-97CE31C7249B

Q37532652-443FA1DB-7E03-4553-A552-7A046C2F686E

Q37532652-46EA44AF-3F2D-4D7A-B288-F175FA2628FC

Q37532652-4B6A9217-1D01-4001-9460-971E7A1039A0

Q37532652-518A0F07-1F32-4FF2-B92B-E7A29DC6DE20

Q37532652-57ABB644-BC64-49AC-B052-8F1B171F9518

Q37532652-628E24EC-7630-4B22-8DA1-376BB5A9A997

Q37532652-6DCDD8AA-097E-482F-86C6-9ED2ECD2C4BE

Q37532652-81540230-01DC-4765-A63E-1D5B6B8D1B6A

P304

Q37532652-7ADF3259-B884-468D-85A4-CB32069980D9

P31

Q37532652-6594127D-93AA-4D24-8441-09149E67F925

P356

Q37532652-764EBC5E-DA5C-494F-82D5-C6B616CA817D

P407

Q37532652-21C2715C-4F67-4F9A-9B43-C42D21242BC8

P433

Q37532652-C74C72AB-4DEE-4C6B-864B-96C9AFD497E9

P478

Q37532652-FF9F284D-AAB0-4FAE-A398-79D46C8944E6

P577

Q37532652-BE904C0D-3627-48F6-B88F-4D33D929B79E

P5875

Q37532652-DAB0C2E0-43EC-4758-90AB-57BB3EF3FB23

P698

Q37532652-34259333-CA09-437C-B99E-FFEAEEE069C7

P932

Q37532652-6675A4D3-7F5B-4B3C-945B-FBE0ABB77ECA

P356

PNAS.88.12.5302

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

A protein geranylgeranyltransf ...... otein prenylation specificity.

@en

P2093

F Ghomashchi

http://www.w3.org/2001/XMLSchema#string

G W Goodwin

http://www.w3.org/2001/XMLSchema#string

J A Glomset

http://www.w3.org/2001/XMLSchema#string

K Yokoyama

http://www.w3.org/2001/XMLSchema#string

M H Gelb

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular cloning of smg p21B and identification of smg p21 purified from bovine brain and human platelets as smg p21B

Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine

Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42

Identification and preliminary characterization of protein-cysteine farnesyltransferase

Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42

Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases

Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product

Saccharomyces cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone.

All ras proteins are polyisoprenylated but only some are palmitoylated

Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate

P304

5302-5306

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.88.12.5302

http://www.w3.org/2001/XMLSchema#string

P407

P433

12

http://www.w3.org/2001/XMLSchema#string

P478

88

http://www.w3.org/2001/XMLSchema#string

P577

1991-06-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

21102636

http://www.w3.org/2001/XMLSchema#string

P698

2052607

http://www.w3.org/2001/XMLSchema#string

P932

51860

http://www.w3.org/2001/XMLSchema#string