Publication

SAS-1 Is a C2 Domain Protein Critical for Centriole Integrity in C. elegans

Related publications (48)

About
Privacy
Disclaimer

Graph Chatbot

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

SAS-1 Is a C2 Domain Protein Critical for Centriole Integrity in C. elegans

Graph Chatbot

Chat with Graph Search

Ultraviolet Superradiance from Mega-Networks of Tryptophan in Biological Architectures

Sperm-contributed centrioles segregate stochastically into blastomeres of 4-cell stage Caenorhabditis elegans embryos

Centriole elimination during Caenorhabditis elegans oogenesis initiates with loss of the central tube protein SAS-1

Tubulin engineering by semi-synthesis reveals that polyglutamylation directs detyrosination

Toxic Effects of Koumine on the Early-Life Development Stage of Zebrafish

Dissecting centriole fate in C. elegans development

Structures of SAS-6 coiled coil hold implications for the polarity of the centriolar cartwheel

TRIM37 prevents formation of centriolar protein assemblies by regulating Centrobin

Centriole foci persist in starfish oocytes despite Polo-like kinase 1 inactivation or loss of microtubule nucleation activity

A helical inner scaffold provides a structural basis for centriole cohesion