(Q44456115)

English

A mutation in the catalytic domain of pp60v-src is responsible for the host- and temperature-dependent phenotype of the Rous sarcoma virus mutant tsLA33-1

scientific article published on March 1, 1992

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scholarly article

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Europe PubMed Central

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3 December 2017

A mutation in the catalytic domain of pp60v-src is responsible for the host- and temperature-dependent phenotype of the Rous sarcoma virus mutant tsLA33-1 (English)

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310553

11 September 2022

Rous sarcoma virus

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Rous sarcoma virus

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based on heuristic

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author name string

R. Foster

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310553

11 September 2022

G. S. Martin

2

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310553

11 September 2022

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publication date

1 March 1992

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3 December 2017

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https://api.elsevier.com/content/article/PII:0042682292903037?httpAccept=text/xml

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10.1016/0042-6822(92)90303-7

https://api.crossref.org/works/10.1016/0042-6822(92)90303-7

1 December 2023

https://api.elsevier.com/content/article/PII:0042682292903037?httpAccept=text/plain

1 reference

10.1016/0042-6822(92)90303-7

https://api.crossref.org/works/10.1016/0042-6822(92)90303-7

1 December 2023

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

187

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Europe PubMed Central

PubMed publication ID

3 December 2017

1

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Europe PubMed Central

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3 December 2017

145-155

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Europe PubMed Central

PubMed publication ID

3 December 2017

Amino Acid Alterations Within a Highly Conserved Region of the Rous Sarcoma Virus src Gene Product pp60src Inactivate Tyrosine Protein Kinase Activity

2

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Oncogenes and signal transduction

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Phosphotyrosine-containing proteins and expression of transformation parameters in cells infected with partial transformation mutants of Rous sarcoma virus

4

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Three glycolytic enzymes are phosphorylated at tyrosine in cells transformed by Rous sarcoma virus

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Phosphorylation of talin at tyrosine in Rous sarcoma virus-transformed cells

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Linker insertion-deletion mutagenesis of the v-src gene: isolation of host- and temperature-dependent mutants

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Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases

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Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus-transforming gene product

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Mapping of nonconditional and conditional mutants in the src gene of Prague strain Rous sarcoma virus

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The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein

13

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The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

14

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Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells

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Adaptor plasmids simplify the insertion of foreign DNA into helper-independent retroviral vectors

16

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Hormonal regulation of the Rous sarcoma virus src gene via a heterologous promoter defines a threshold dose for cellular transformation

17

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Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation

19

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Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src

20

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New Procedure for DNA Transfection with Polycation and Dimethyl Sulfoxide

22

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SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

23

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The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function

24

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Mutants of rous sarcoma virus with extensive deletions of the viral genome

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A novel viral oncogene with structural similarity to phospholipase C

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ras GTPase activating protein: signal transmitter and signal terminator

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2 New M13 vectors for cloning

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Src homology region 2 domains direct protein-protein interactions in signal transduction

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Transformation by Rous sarcoma virus: A cellular substrate for transformation-specific protein phosphorylation contains phosphotyrosine

31

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Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene

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A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps

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DNA sequencing with chain-terminating inhibitors

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Nucleotide sequence of Rous sarcoma virus

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Vinculin: A cytoskeletal target of the transforming protein of rous sarcoma virus

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Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus

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Measurement of protein using bicinchoninic acid

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A mutation at the ATP-binding site of pp60v-src abolishes kinase activity, transformation, and tumorigenicity

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Sequence similarity of phospholipase C with the non-catalytic region of src.

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Functional Domains of the pp60v-src Protein as Revealed by Analysis of Temperature-Sensitive Rous Sarcoma Virus Mutants

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Normal rat cell lines deficient in nuclear thymidine kinase

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Molecular cloning of two types of GAP complementary DNA from human placenta

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Revertants of an ASV-transformed rat cell line have lost the complete provirus or sustained mutations insrc

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A mutation in v-src that removes a single conserved residue in the SH-2 domain of pp60v-src restricts transformation in a host-dependent manner

48

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Cloning of bovine GAP and its interaction with oncogenic ras p21.

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The selective isolation of temperature-sensitive mutants of Rous sarcoma virus

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A host-dependent temperature-sensitive mutant of Rous sarcoma virus: evidence for host factors affecting transformation

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10.1016/0042-6822(92)90303-7

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

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