The chemical biology of Ras lipidation (Q34395767)

1 August 2017

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title

The chemical biology of Ras lipidation (English)

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1 August 2017

4

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1 August 2017

Völkert M

1

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1 August 2017

Wagner M

series ordinal

2

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1 August 2017

Peters C

series ordinal

3

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1 August 2017

publication date

1 August 2001

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1 August 2017

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1 August 2017

volume

382

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1 August 2017

issue

8

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1 August 2017

page(s)

1133-1145

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Bioorganic synthesis of lipid-modified proteins for the study of signal transduction.

1 August 2017

cites work

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https://api.crossref.org/works/10.1515%2FBC.2001.143

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Protein lipidation in cell signaling

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Analysis of macromolecular interactions using immobilized ligands.

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Synthesis of proteins by native chemical ligation

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Replacement of the H-Ras farnesyl group by lipid analogues: implications for downstream processing and effector activation in Xenopus oocytes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.143

GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Dislodgment and accelerated degradation of Ras.

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Acid-labile protecting groups for the synthesis of lipidated peptides

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Synthesis of functional Ras lipoproteins and fluorescent derivatives

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

The Farnesyl Group of H-Ras Facilitates the Activation of a Soluble Upstream Activator of Mitogen-activated Protein Kinase

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Cholesterol modification of hedgehog signaling proteins in animal development

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

S-Acylation and plasma membrane targeting of the farnesylated carboxyl-terminal peptide of N-ras in mammalian fibroblasts

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Expressed protein ligation, a novel method for studying protein-protein interactions in transcription

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

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

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers.

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Activation of c-Raf-1 by Ras and Src through different mechanisms: activation in vivo and in vitro

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Increasing complexity of the Ras signaling pathway

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Protein prenylation: molecular mechanisms and functional consequences

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Chemical Protein Synthesis by Solid Phase Ligation of Unprotected Peptide Segments

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

The Allyl Group as Mildly and Selectively Removable Carboxy-Protecting Group for the Synthesis of LabileO-Glycopeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.143

Chemoenzymatic Synthesis of N-RasLipopeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.143

Enzymes and protecting group chemistry

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Protecting Group Strategies in Organic Synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.143

Enzymatic Synthesis of Peptides andRas Lipopeptides Employing Choline Ester as a Solubilizing, Protecting, and Activating Group

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Synthesis of the palmitoylated and prenylated C-terminal lipopeptides of the human R- and N-Ras proteins

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Synthesis of characteristic lipopeptides of the human N-Ras protein and their evaluation as possible inhibitors of protein farnesyl transferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.143

Synthesis of the Palmitoylated and Farnesylated C-Terminal Lipohexapeptide of the Human N-Ras Protein by Employing an Enzymatically Removable Urethane Protecting Group

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2001.143

Enzymic Protecting Group Techniques

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

Chemoenzymatic Synthesis of Fluorescent N-Ras Lipopeptides and Their Use in Membrane Localization Studies in Vivo

21 January 2018

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https://api.crossref.org/works/10.1515%2FBC.2001.143

21 January 2018

Identifiers

DOI

10.1515/BC.2001.143

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1 August 2017

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