Author

L. F. S. Mendes

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 8 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:protein folding & dynamics· 7 Assay:proteomics· 4 Approach:biophysical modeling· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Organism:human· 2 Organism:yeast· 2

Frequent Co-Authors

A. J. Costa-Filho· 8 shared M. R. B. Batista· 4 shared E. Kava· 3 shared C. G. Oliveira· 2 shared M. C. Micheletto· 2 shared N. A. Fontana· 2 shared A. J. Costa Filho· 1 shared A. Watts· 1 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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8 shared papersBiophysics

A. J. Costa-Filho

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Author profile →

9 papers

Recent·Most cited

The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion

L. F. S. Mendes, C. G. Oliveira, M. D. Silva, S. K. Rout, R. Riek, A. J. Costa-Filho

This study investigates how liquid-liquid phase separation facilitates the formation of a vesicular-like compartment for unconventional protein secretion in yeast under starvation stress.

bioRxiv · Dec 19, 2023Biophysics

Exploring Liquid-Liquid Phase Separation in the Organization of Golgi Matrix Proteins

L. F. S. Mendes, C. G. Oliveira, A. J. Costa Filho, E. Kava

This study shows that Golgi Matrix Proteins (GMPs) tend to form biocondensates via Liquid-Liquid Phase Separation (LLPS) across eukaryotic lineages, suggesting a role for LLPS in Golgi organization.

bioRxiv · Jul 21, 2023 · PreprintBiochemistry

Biomolecular condensates of Chlorocatechol 1,2-Dioxygenase as enzymatic microreactors for the degradation of polycyclic aromatic hydrocarbons

N. N. Evangelista, M. C. Micheletto, L. F. S. Mendes, A. J. Costa-Filho

This study constructs a chimera protein that forms biomolecular condensates with enzymatic activity for degrading polycyclic aromatic hydrocarbons.

bioRxiv · May 29, 2023 · PreprintBiophysics

Resurrecting Golgi proteins to grasp Golgi ribbon formation and self-association under stress

l. f. s. mendes, M. R. B. Batista, E. Kava, L. Bleicher, M. C. Micheletto, A. J. Costa-Filho

This study reconstructs ancestor GRASP proteins to investigate their evolution and role in Golgi ribbon formation and stress-induced secretion.

bioRxiv · Jul 27, 2021Biophysics

Myristoylation and its effects on the human Golgi Reassembly and Stacking Protein 55

E. Kava, L. F. S. Mendes, M. R. B. Batista, A. J. Costa-Filho

This study investigates how myristoylation affects GRASP55's membrane anchoring and structural properties using biophysical and computational methods.

bioRxiv · Jun 22, 2021Biophysics

Structural and thermodynamic analyses of human TMED1 (p24γ1) Golgi dynamics

D. C. A. M. Mota, R. M. Mori, M. R. B. Batista, L. G. M. Basso, I. A. Cardoso, M. C. Nonato, A. J. Costa-Filho, L. F. S. Mendes

This study presents the first high-resolution structure of the GOLD domain of TMED1 and its biophysical properties, revealing dimer formation and insights into its membrane orientation.

bioRxiv · Feb 13, 2021Biophysics

Conformational flexibility of GRASP protein and its constituent PDZ subdomains reveals structural basis of its promiscuous interactome

L. F. S. Mendes, M. R. B. Batista, P. J. Judge, A. Watts, C. Redfield, A. J. Costa-Filho

This paper investigates the structural flexibility of GRASP PDZ domains and explains their promiscuous interactome through biophysical analysis.

bioRxiv · Jun 10, 2019Biophysics

Exploring Structural Aspects of the Human Golgi Matrix Protein GRASP55 in Solution

S. T. Reddy, L. F. S. Mendes, N. A. Fontana, A. J. Costa-Filho

This study investigates the structural properties of human GRASP55 in solution, revealing its disordered regions, monomeric state, and aggregation behavior during denaturation.

bioRxiv · Mar 31, 2019Biophysics

The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior

N. A. Fontana, R. Fonseca-Maldonado, L. F. S. Mendes, L. P. Meleiro, A. J. Costa-Filho

The paper shows that the yeast GRASP Grh1 is intrinsically disordered and can form amyloid fibrils, suggesting these properties may be common in the GRASP family.

bioRxiv · Jan 25, 2018Biophysics