(Q42832101)

8 November 2017

title

Evidence for a high affinity, saturable, prenylation-dependent p21Ha-ras binding site in plasma membranes (English)

1 reference

8 November 2017

Siddiqui AA

1

1 reference

8 November 2017

Garland JR

series ordinal

2

1 reference

8 November 2017

Dalton MB

series ordinal

3

1 reference

8 November 2017

Sinensky M

series ordinal

4

1 reference

8 November 2017

language of work or name

English

0 references

publication date

1 February 1998

1 reference

Journal of Biological Chemistry

8 November 2017

published in

1 reference

8 November 2017

volume

273

1 reference

8 November 2017

issue

6

1 reference

8 November 2017

page(s)

3712-3717

1 reference

Protein prenylation: molecular mechanisms and functional consequences

8 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

All ras proteins are polyisoprenylated but only some are palmitoylated

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Inhibition of DNA synthesis in cultures of 3T3 cells by isolated surface membranes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Lamin B constitutes an intermediate filament attachment site at the nuclear envelope

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Purification of baculovirus-expressed recombinant Ras and Rap proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Function and regulation of ras.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Protein prenylation: a mediator of protein-protein interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

In vitro assay and characterization of the farnesylation-dependent prelamin A endoprotease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

5'-Nucleotidase activity and substrate affinity in digenetic trematodes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Analysis of serum insulin-like growth factor binding proteins using western blotting: use of the method for titration of the binding proteins and competitive binding studies

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Unexpectedly strong binding of a large metal ion (Bi3+) to human serum transferrin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchange

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3712

21 January 2018

Identifiers

DOI

10.1074/JBC.273.6.3712

1 reference

8 November 2017

1 reference