Identification of Ras farnesyltransferase inhibitors by microbial screening. - Wikidata - awgldk - TriplyDB

Identification of Ras farnesyltransferase inhibitors by microbial screening.

Identification of Ras farnesyltransferase inhibitors by microbial screening.

http://www.wikidata.org/entity/Q36165226

about

Rational design of small molecule inhibitors targeting the Ras GEF, SOS1.Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype Thematic review series: lipid posttranslational modifications. Fighting parasitic disease by blocking protein farnesylation Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice Contribution of Src and Ras pathways in FGF-2 induced endothelial cell differentiation.Targeting protein prenylation for cancer therapy A genome-wide RNA interference screen reveals an essential CREB3L2-ATF5-MCL1 survival pathway in malignant glioma with therapeutic implications.Upregulation of nuclear factor-kappaB expression by SLURP-1 is mediated by alpha7-nicotinic acetylcholine receptor and involves both ionic events and activation of protein kinases.Ras farnesyltransferase inhibitors suppress the phenotype resulting from an activated ras mutation in Caenorhabditis elegans.Lipid posttranslational modifications. Farnesyl transferase inhibitors.Multimutated herpes simplex virus g207 is a potent inhibitor of angiogenesis.Consequences of altered isoprenylation targets on a-factor export and bioactivity.P2Y(2) receptor-mediated proliferation of C(6) glioma cells via activation of Ras/Raf/MEK/MAPK pathway.Biosynthesis of colabomycin E, a new manumycin-family metabolite, involves an unusual chain-length factor.The prenylation inhibitor manumycin A reduces the viability of Anaplasma phagocytophilum Combined rational design and a high throughput screening platform for identifying chemical inhibitors of a Ras-activating enzyme A dual-targeting approach to inhibit Brucella abortus replication in human cells.Manumycin A inhibits triple-negative breast cancer growth through LC3-mediated cytoplasmic vacuolation death.Inhibition of protein farnesylation enhances the chemotherapeutic efficacy of the novel geranylgeranyltransferase inhibitor BAL9611 in human colon cancer cells.Fungal lipopeptide mating pheromones: a model system for the study of protein prenylation Inhibition of farnesyltransferase: a rational approach to treat cancer?Fibroblast growth factor-2 promotes catabolism via FGFR1-Ras-Raf-MEK1/2-ERK1/2 axis that coordinates with the PKCδ pathway in human articular chondrocytes.Manumycin A corrects aberrant splicing of Clcn1 in myotonic dystrophy type 1 (DM1) mice.Inhibitors of cellular signalling are cytotoxic or block the budded-to-hyphal transition in the pathogenic yeast Candida albicans.Coupling of ionic events to protein kinase signaling cascades upon activation of alpha7 nicotinic receptor: cooperative regulation of alpha2-integrin expression and Rho kinase activity.Antitumor compounds from marine actinomycetes.Drug targeting of sphingolipid metabolism: sphingomyelinases and ceramidases.Allylic structures in cancer drugs and body metabolites that control cell life and death.Manumycin inhibits ras signal transduction pathway and induces apoptosis in COLO320-DM human colon tumour cells.Modulation of RhoA-Rho kinase-mediated Ca2+ sensitization of rabbit myometrium during pregnancy - role of Rnd3.Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB.Enhanced antiproliferative and apoptotic response of HT-29 adenocarcinoma cells to combination of photoactivated hypericin and farnesyltransferase inhibitor manumycin A Manumycin inhibits farnesyltransferase and induces apoptosis of drug-resistant interleukin 6-producing myeloma cells.Apoptosis of medulloblastoma cells in vitro follows inhibition of farnesylation using manumycin A.Suppression of human pancreatic cancer growth in BALB/c nude mice by manumycin, a farnesyl:protein transferase inhibitor.Farnesyltransferase as a target for anticancer drug design.Inhibitors of the Ras signal transduction pathway as potential antitumour agents.A mutant form of human protein farnesyltransferase exhibits increased resistance to farnesyltransferase inhibitors.Manumycin and gliotoxin derivative KT7595 block Ras farnesylation and cell growth but do not disturb lamin farnesylation and localization in human tumour cells.

P2860

Q27318713-7345E098-79FB-4598-BF5E-DB616AB85D8A Q27671538-FBA7C507-50F6-4235-B443-BEA26BE331E9 Q28117127-1D59A3F3-2B4D-410A-B3DB-AAE6456CBD4A Q28285888-6D47D802-19CB-4D9A-992A-DCD70814702C Q28369454-FA14EFF0-5487-4100-B356-AE07B4A39F6F Q30711403-FFA6BB7C-B88F-42E3-953F-F56C8B85775B Q33679239-42FED719-8788-482E-92AC-53407292C97C Q33900952-9243C01A-1700-455A-A5BD-2200D779A461 Q34304838-437AB1A0-3B36-4408-8759-EE687E29A52A Q34434642-1ED62368-BF56-47BA-8656-444D6A969CB6 Q34651253-CE5A3191-4B8A-47E9-8A04-D4A844D8BEDB Q34928710-ED3FC896-39AB-435B-9D2E-8727DDFF4D36 Q35038534-2BF24329-441D-426F-944C-F8E76B55FD7C Q35042080-7E08DC68-35B7-430D-8F6F-415B6E0FEAB3 Q35170571-7A2470EB-FA40-40D0-B360-3F7EAD07399F Q35199212-E991EEF8-4AFE-4C15-AEA3-2543117499FC Q35590750-C00D91DD-5DDD-4875-93F6-AE6D77FD2D96 Q36170389-0B96FE11-31F5-4A6D-9B6A-9070ED3A55C2 Q36586495-596F76E4-C2BD-4157-BBD4-53B1D87676EA Q36622317-378605EA-4113-4601-AE86-AAA127F8C6C2 Q36669959-EA2DFE80-1272-478D-B9E8-1EA4D6C76716 Q36828655-F70AFF41-C21F-4CDE-A2D6-8BABFDCEC78C Q36934976-CEE7C339-4395-4E80-9929-52B496AFE7E1 Q36983716-5C72FAEE-E480-42AB-97E4-09F7E7212179 Q37343625-02084A36-A823-40E7-8506-A39B49F5E74F Q37372238-09D8685D-48BE-45C8-BE92-9058F7BFB17E Q37549963-AB8D0AEF-111D-4DE1-B0BE-C6F48C7B5967 Q37880161-7F4FF6B8-1212-4021-BE1F-C1018FF997F6 Q38089154-83CE629D-24DB-4D8E-804E-D03F6DEE1025 Q38274079-6AC63318-FF11-4078-B5BC-88B525521165 Q38349188-E6A8C1BF-CCE3-4A22-90BB-1084906B19EF Q39444763-10F9E1A8-57E5-4972-816D-0EB26CDAA1FC Q40360176-31F6629F-CA00-485D-A3BA-F492751F8BA5 Q40720447-5BC6A569-6FC1-42C1-959F-150841FA91FA Q40942828-43E1DEEE-614B-4A48-B438-D476C3377A40 Q41234843-E2D0E9DE-26C8-45D2-8DD7-ACA98D784310 Q41489707-757D76CD-5744-404B-B718-3D5E27BCD82F Q41515936-FECC6062-5448-4D79-B8CC-8106D68FA5DF Q41689650-EDE34A8B-295A-46AE-98B7-C053A2A1146C Q41931496-6E7F66D2-5989-46DA-B809-E358949AB15F

P2860

Identification of Ras farnesyltransferase inhibitors by microbial screening.

http://www.wikidata.org/entity/Q36165226

description

1993 nî lūn-bûn

@nan

1993年の論文

@ja

1993年学术文章

@wuu

1993年学术文章

@zh-cn

1993年学术文章

@zh-hans

1993年学术文章

@zh-my

1993年学术文章

@zh-sg

1993年學術文章

@yue

1993年學術文章

@zh

1993年學術文章

@zh-hant

name

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@ast

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@en

type

label

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@ast

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@en

prefLabel

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@ast

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@en

P1433

Q36165226-FC4712D6-6298-40F3-934B-119635A8DEF5

P1476

Q36165226-C2E299DD-5DF7-4333-A1C9-EE4F301F82B2

P2093

Q36165226-18120197-FF99-474A-91C6-0446D1232AC9

Q36165226-2A9598BC-4351-4F7F-A9F5-8F6BC42475E8

Q36165226-3F05AC4A-61BB-4A07-B202-C584C8B97E47

Q36165226-5841219F-D31C-4CD8-BB4E-698BDE9550F2

Q36165226-7F0A42F3-1E3C-429C-BDE9-3E19BA274AA5

Q36165226-AD35DB1F-B1A8-4334-BE37-F209F91E5EE0

Q36165226-BBB0B303-98DB-49EA-83D2-91A1406D3908

Q36165226-E4E231B7-5D35-4BC5-A5C6-07689BCB8D53

Q36165226-EFEB262F-2DF4-4E99-A8E3-7D4E48A7AA2A

P2860

Q36165226-1B7171FF-5CC1-496B-B2EA-4BA81844128D

Q36165226-23E5132E-0F54-46CF-96FD-FA722F263235

Q36165226-27C32DF1-958A-4F2E-9314-85352CC4B79A

Q36165226-373E50C8-6761-4808-9B84-BB5A3356F9E3

Q36165226-4E6FC874-9C7E-45F2-BDD4-7D9275AEC148

Q36165226-52CB6E4A-FB7D-488E-BA4F-AAC3B0FC63EE

Q36165226-55EA0F2C-3C06-4828-9C6D-6E5E08F454A0

Q36165226-5E89C4B5-BBE1-4C68-AE2F-205D73E2F4DB

Q36165226-6449BAF3-FF14-4893-92E9-15C1DD8E3035

Q36165226-670DEC7D-9458-44D3-9E91-BF38FE02706B

P304

Q36165226-9D4E685C-DDCE-4E29-A659-66A247431956

P31

Q36165226-FE4FBBC6-8634-44E9-B27D-3AD6CA68F7B1

P356

Q36165226-AF34DED3-B7EC-4E31-9B3D-2590C6661960

P407

Q36165226-C9804248-385E-48B1-AD36-7E10F8624E29

P433

Q36165226-5CCEA2DC-CF41-4CE7-A3DC-AE88CEA52C13

P478

Q36165226-5464A78D-F25A-489B-8DFF-13FA050E7C54

P577

Q36165226-8B26C12A-C6DA-423F-81D6-61BF35F292E2

P5875

Q36165226-54370B4C-04AA-4B4C-AC93-2DAAA35A0E82

P698

Q36165226-D7E8B467-2D0C-414A-865C-81E073C42988

P932

Q36165226-899D9842-828C-445F-9D47-94364F2F6D14

P356

P1433

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

P1476

Identification of Ras farnesyltransferase inhibitors by microbial screening.

@en

P2093

D Wood

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

F Tamanoi

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

H Nakano

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

K Akasaka

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

M Hara

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

M Okabe

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

M Uh

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

R Gomez

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

S Akinaga

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

P2860

Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit

Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart.

GPA1, a haploid-specific essential gene, encodes a yeast homolog of mammalian G protein which may be involved in mating factor signal transduction.

RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins.

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

cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1

Rab geranylgeranyl transferase. A multisubunit enzyme that prenylates GTP-binding proteins terminating in Cys-X-Cys or Cys-Cys

Mutants of H-ras that interfere with RAS effector function in Saccharomyces cerevisiae.

Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins.

P304

2281-2285

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

P31

scholarly article

P356

10.1073/PNAS.90.6.2281

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

P407

P433

6

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

P478

90

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

P577

1993-03-01T00:00:00Z

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

P5875

14739445

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

P698

8460134

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

P932

46070

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