• Publications
  • Influence
Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly
TLDR
The reconstitution and characterization of subcomplexes formed by the cytoplasm-exposed synaptotagmin-like mitochondrial lipid-binding protein (SMP) domains present in three of the five ERMES subunits are reported, suggesting a structure-based mechanism for the facilitated transport of phospholipids between organelles.
Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design
TLDR
These structures represent the first step towards the characterization of these two malarial chaperones and the reconstitution of the entire PTEX to aid structure‐based design of novel anti‐malarial drugs.
Structure of a putative ClpS N‐end rule adaptor protein from the malaria pathogen Plasmodium falciparum
TLDR
The first crystal structure is reported of a eukaryotic homolog of bacterial ClpS from the malaria apicomplexan parasite Plasmodium falciparum (Pfal), and it is shown that, in solution, Pfal‐ClpS binds and discriminates peptides mimicking bona fide N‐end rule substrates.
Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes
TLDR
An enhanced chemoproteomic approach is presented to evaluate the activity and probe reactivity of deubiquitinase enzymes, using bioorthogonally tagged ABPs and a sequential on-bead digestion protocol to enhance the identification of probe-labeling sites.
Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies.
TLDR
A refined pseudo-atomic model of the Mdm12/Mmm1 ERMES complex that agrees with the crystallographic and small-angle X-ray scattering (SAXS) solution data is proposed and a monomeric form of MDM12 is revealed with a conformationally dynamic N-terminal β-strand.
An ancient mechanism of arginine-specific substrate cleavage: What's 'up' with NSP4?
TLDR
Although the substrates and physiological role of NSP4 remain to be determined, its remarkable evolutionary conservation, restricted tissue expression and homology to other neutrophil serine proteases anticipate a function in immune-related processes.
Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain.
TLDR
The observed quantitative binding of Ab6E2 to native PCSK9 from various cell lines suggests that the disorder-to-order transition is a true feature of PCSK 9 and not limited to peptides.
Neutrophil serine protease 4 is required for mast cell-dependent vascular leakage
TLDR
It is shown that expression of Neutrophil Serine Protease 4 during the early stages of mast cell development regulates the levels of histamine and serotonin in mast cell granules, which impacts mast cell-dependent vascular leakage in mouse models of immune complex-mediated diseases.
Determining the Lipid-Binding Specificity of SMP Domains: An ERMES Subunit as a Case Study.
TLDR
The methods for expression and purification of recombinant Mdm12, a bona fide SMP-containing protein, together with the subsequent identification of its bound phospholipids by high-performance thin-layer chromatography (HPTLC) and the characterization of its lipid exchange and transfer functions using lipid displacement and liposome flotation in vitro assays with liposomes as model biological membranes are described.