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Federica Brandizzi

Researcher at Michigan State University

Publications -  201
Citations -  10477

Federica Brandizzi is an academic researcher from Michigan State University. The author has contributed to research in topics: Endoplasmic reticulum & Golgi apparatus. The author has an hindex of 53, co-authored 188 publications receiving 9135 citations. Previous affiliations of Federica Brandizzi include Oxford Brookes University & Great Lakes Bioenergy Research Center.

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Mapping the Arabidopsis organelle proteome

Tom Dunkley, +12 more
- 25 Apr 2006 - 
TL;DR: The localization of organelle proteins by the isotope tagging technique in conjunction with isotope tags for relative and absolute quantitation and 2D liquid chromatography for the simultaneous assignment of proteins to multiple subcellular compartments has enabled protein steady-state distributions to be determined.
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Organization of the ER–Golgi interface for membrane traffic control

Federica Brandizzi, +1 more
- 01 Jun 2013 - 
TL;DR: Comparison of the ER–Golgi interface across different systems, particularly mammalian and plant cells, reveals fundamental elements and distinct organization of this interface that should provide key insights into the mechanisms that control efficient trafficking of proteins and lipids through the secretory pathway.
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IRE1: ER stress sensor and cell fate executor

Yani Chen, +1 more
- 01 Nov 2013 - 
TL;DR: An updated scenario of the IRE1 signaling model is provided, a discussion of emerging IRE 1 sensing mechanisms is discussed, features among species are compared, and exciting future directions in UPR research are outlined.
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Membrane Protein Transport between the Endoplasmic Reticulum and the Golgi in Tobacco Leaves Is Energy Dependent but Cytoskeleton Independent: Evidence from Selective Photobleaching

Federica Brandizzi, +4 more
- 01 Jun 2002 - 
TL;DR: The results indicate that in plant cells, the Golgi apparatus is a dynamic membrane system whose components continuously traffic via membrane trafficking pathways regulated by brefeldin A- and N-ethylmaleimide-sensitive machinery.
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Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells.

Luis L. P. daSilva, +5 more
- 01 Jul 2004 - 
TL;DR: It is proposed that punctate accumulation of Sar1p represents ER export sites (ERES), and this work could demonstrate using the drug brefeldin A that formation of ERES is strictly dependent on a functional retrograde transport route from the Golgi apparatus.