Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects. - Wikidata - wikimedia - TriplyDB

Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

http://www.wikidata.org/entity/Q35590255

about

Mechanism of activation of the Caenorhabditis elegans ras homologue let-60 by a novel, temperature-sensitive, gain-of-function mutation p190 RhoGAP, the major RasGAP-associated protein, binds GTP directly Protein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptor The centaurin gamma-1 GTPase-like domain functions as an NTPase Mutations in human dynamin block an intermediate stage in coated vesicle formation Biochemical and X-ray crystallographic studies on shikimate kinase: The important structural role of the P-loop lysine Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway.CHL1 is a nuclear protein with an essential ATP binding site that exhibits a size-dependent effect on chromosome segregation.Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activation Biochemical properties of the ras-related YPT protein in yeast: a mutational analysis.Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p.Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins Molecular determinants for cyclic nucleotide binding to the regulatory domains of phosphodiesterase 2A Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii KATP channel subunits in rat dorsal root ganglia: alterations by painful axotomy Identification of genomic regions that interact with a viable allele of the Drosophila protein tyrosine phosphatase corkscrew Systematic structure-function analysis of the small GTPase Arf1 in yeast.Effects of site-directed mutagenesis of mglA on motility and swarming of Myxococcus xanthus.Chimeric proteins define variable and essential regions of Ha-ras-encoded protein.Mutational analysis of SEC4 suggests a cyclical mechanism for the regulation of vesicular traffic.Serum screening for oncogene proteins in workers exposed to PCBs.Mutants of H-ras that interfere with RAS effector function in Saccharomyces cerevisiae.Genetic analysis of the Kirsten-ras-revertant 1 gene: potentiation of its tumor suppressor activity by specific point mutations.Proposed active site domain in estrogen sulfotransferase as determined by mutational analysis.Caenorhabditis elegans SUR-5, a novel but conserved protein, negatively regulates LET-60 Ras activity during vulval induction.Reprogramming the purine nucleotide cofactor requirement of Drosophila P element transposase in vivo.Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator.A screen for genes that function downstream of Ras1 during Drosophila eye development.Regulation of sugar and ethanol metabolism in Saccharomyces cerevisiae.Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant.Complex formation between RAS and RAF and other protein kinases Conformational effects of substituting amino acids for glutamine-61 on the central transforming region of the P21 proteins Novel Rap1 dominant-negative mutants interfere selectively with C3G and Epac.Raf-1 interferes with Ras and Rap1A effector functions in yeast Properties of a genetically engineered G domain of elongation factor Tu.The human c-Kirsten ras gene is activated by a novel mutation in codon 13 in the breast carcinoma cell line MDA-MB231.

P2860

Q24308974-E9F04029-0790-471E-BC4C-3AFE121C1000 Q24608990-33FAF9A5-C225-4684-AD06-E260E423EDDD Q24643469-38623CD0-A4AF-4942-B2E3-03779E4763B1 Q24672233-E11A7E46-FAA8-459A-A647-2E4AAF4EDE22 Q24674406-FA932C60-183D-4A99-869B-6DC5CA63A50C Q27631871-4BB2D8E3-CD96-42F1-BAB2-513A3EB126A2 Q27674619-9E323111-20B4-489E-9B41-81D40BD04769 Q27929791-B7F808D9-433D-4CD7-A4D1-E4EAF8E60A86 Q27932069-0D5BA2FA-2F0B-4196-8DA1-D9F1DA489B98 Q27932199-C8F234D2-7BBC-4712-95DB-8DAE8CC23777 Q27935130-C80AF275-95AC-4680-8292-0BF4D0281AD0 Q27936486-0C208D44-473F-4DDA-B81B-D9B98C17BC68 Q27940327-CBEFBB00-3CC6-4C85-B023-B9806FEAFC58 Q28137760-B7B926F2-238E-4AD5-97A6-0A5E31335541 Q28268016-31FAC439-4039-4AAA-90C5-98AB2A528477 Q28506496-6377FAAE-F119-4662-8482-0E39DC5C6C7C Q28577176-608D31E5-25F9-436F-829E-8043E71BD00D Q28769070-D20B9700-6FA1-471B-B46B-9EDC9220EAE0 Q30475857-A8E206AF-8883-4160-9C04-D03874D51CBD Q30497633-2DE5CDD1-351A-4DFD-BF0F-A03AE4804A60 Q33552267-41404002-2C0C-4EDE-ADE5-4A8340FF2D6D Q33566253-9DD39FAB-DFC3-4F2C-A854-171E6DBA83E3 Q33577301-536BC988-1FA6-40B0-ABE1-AEA814C55402 Q33581406-BE054482-6848-45BA-998B-B331E5452874 Q33615357-05F4218F-8E31-4BEC-A5AE-21327F43E7FB Q33668846-69206134-449A-4BD2-8B58-68A60564563C Q33775151-7DEB9E1B-82B6-4F85-BA68-C772C7D326D0 Q33887134-56088E9D-34B2-46D4-8A49-DD0FF150DC38 Q33937838-91209CE3-D251-4FAE-BB8A-A5BBD3BC1549 Q33967357-78DE21D6-2736-4631-BACE-1C53E33A6458 Q34027490-36A43A97-E5C8-4FAB-BD83-D14F2D2C4007 Q34047787-CAEA2558-1152-442C-96CC-48A4374E6218 Q34300458-B13D7E42-4558-424A-B21A-55F417BF8E0C Q34300969-9C4790A8-0D3A-4A69-BB33-C981EE9896EB Q34351032-FDEFC1A5-D1CB-4AB5-938B-244750F413D1 Q34370360-350CF3D8-F03A-4940-86FD-429B84F97AFB Q34414134-FC53A9CA-4BB8-4B77-8575-C35B87C83D3D Q34440446-A79F8AAC-F77F-43BE-BC52-0A331ADB787C Q34622043-BCDA7C03-DBCF-4543-83E5-CE7499F8AE53 Q34696613-5B828D1D-51D8-4B96-8089-814E79796CC6

P2860

Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

http://www.wikidata.org/entity/Q35590255

description

1986 nî lūn-bûn

@nan

1986年の論文

@ja

1986年論文

@yue

1986年論文

@zh-hant

1986年論文

@zh-hk

1986年論文

@zh-mo

1986年論文

@zh-tw

1986年论文

@wuu

1986年论文

@zh

1986年论文

@zh-cn

name

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@ast

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@en

type

label

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@ast

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@en

prefLabel

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@ast

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@en

P1433

Q35590255-179CD253-8576-40EF-8C55-73536C2D9A6A

P1476

Q35590255-5433E457-FEA9-4221-B63D-012126FE9236

P2093

Q35590255-3A8456B6-B1BB-4C3D-90D8-8307D1ED0FDA

Q35590255-B16DF2C3-0EF4-4719-8E21-ABB8EC693C07

Q35590255-B6A1E774-C8E8-405C-83D5-3885659F2B3D

Q35590255-C807AFC3-73B7-4F0C-BDFD-F77CC63EAD31

Q35590255-C9CC6347-8249-404C-84EB-172EC7C99731

Q35590255-CAF1D309-C7F6-4826-9938-EF8A56114EEC

Q35590255-DE4317B3-330A-4B27-9223-EEC1FE20D865

P2860

Q35590255-19B6AF52-50D2-4A81-BD84-20E7ED8DAD4E

Q35590255-1A1798AB-4E51-4352-9951-1B9960ECC431

Q35590255-2A6EA47C-926B-46F1-BE71-9C66359CF871

Q35590255-347E57C9-9F86-4E45-B7EF-FFC65A62A4ED

Q35590255-44189241-FA47-4846-940D-257EAC3C9CC9

Q35590255-4A5769FA-F767-407F-BA39-E35E89BDA2CA

Q35590255-62898F32-1DB5-498F-B7E5-07FFD9FA6C43

Q35590255-6947F900-9EFC-48A1-9D56-F73698F7D2E2

Q35590255-859FCE24-4A1E-4EE4-9BED-7D82AB363BC7

Q35590255-86D55B48-F1F4-4B0E-9984-C0633A6E01F2

P304

Q35590255-8371EC79-D360-4086-94CA-9F1E315B4070

P31

Q35590255-3B2EDB95-4A00-49BE-9A0A-34FFC0C22F1E

P356

Q35590255-FD8EFAF1-DDB2-4901-93C5-E5AB3E36DB2C

P407

Q35590255-476D1589-9BF4-49F3-91FC-8017AEA3D82D

P433

Q35590255-25B67EFF-C0DF-4C13-BA28-BB3B2430CDAF

P478

Q35590255-C9845E4E-933E-4719-A3CB-EB13625D514D

P577

Q35590255-BE5C38EF-096B-4CF0-BAB8-0733CB6A6A0C

P5875

Q35590255-C4D316F2-C8B4-4AA1-ACD5-6AD65AECABFA

P698

Q35590255-216E7F79-9605-42CD-AF9C-F0D2202F2B11

P932

Q35590255-824A8FE8-5499-4A18-B09C-065B369EEFF7

P356

P1433

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

P1476

Mutant ras-encoded proteins wi ...... t dominant biological effects.

@en

P2093

D'Alonzo JS

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

Gibbs JB

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

Scolnick EM

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

Sigal IS

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

Socher SH

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

Temeles GL

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

Wolanski BS

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

P2860

Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins

Differential activation of yeast adenylate cyclase by wild-type and mutant RAS proteins.

Genetic analysis of yeast RAS1 and RAS2 genes.

Substrate positions and induced-fit in crystalline adenylate kinase

Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae

Harvey murine sarcoma virus p21 ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus

Guanine nucleotide-binding activity as an assay for src protein of rat-derived murine sarcoma viruses

G proteins and dual control of adenylate cyclase.

Genes in S. cerevisiae encoding proteins with domains homologous to the mammalian ras proteins.

Functional homology of mammalian and yeast RAS genes.

P304

952-956

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

P31

scholarly article

P356

10.1073/PNAS.83.4.952

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

P407

P433

4

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

P478

83

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

P577

1986-02-01T00:00:00Z

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

P5875

19649089

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

P698

3513168

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

P932

322988

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