A novel bipartite phospholipid‐binding module in the neurofibromatosis type 1 protein-Reference-Cited by-同舟云学术

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A novel bipartite phospholipid‐binding module in the neurofibromatosis type 1 protein

Published:2006-02 Issue:2 Volume:7 Page:174-179
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

D'angelo Igor¹,Welti Stefan¹,Bonneau Fabien¹,Scheffzek Klaus¹

Affiliation:

1. European Molecular Biology Laboratory, Structural and Computational Biology Programme Meyerhofstrasse 1 69117 Heidelberg Germany

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1038/sj.embor.7400602

Reference33 articles.

1. Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling

2. The PH superfold: a structural scaffold for multiple functions

3. Differential regulation of rasGAP and neurofibromatosis gene product activities

4. Characterization of full-length neurofibromin: tubulin inhibits Ras GAP activity.

5. Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein

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1. An Atypical Mechanism of SUMOylation of Neurofibromin SecPH Domain Provides New Insights into SUMOylation Site Selection;Journal of Molecular Biology;2024-11

2. RAS Signaling Gone Awry in the Skin: The Complex Role of RAS in Cutaneous Neurofibroma Pathogenesis, Emerging Biological Insights;Journal of Investigative Dermatology;2023-08

3. Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics;Frontiers in Plant Science;2023-05-15

4. Evolving Diagnostic and Treatment Strategies for Pediatric CNS Tumors: The Impact of Lipid Metabolism;Biomedicines;2023-05-05

5. The therapeutic potential of neurofibromin signaling pathways and binding partners;Communications Biology;2023-04-20

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