Maria F. Presti

ORCID: 0000-0003-1541-5770
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About
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Research Areas
  • Monoclonal and Polyclonal Antibodies Research
  • Ubiquitin and proteasome pathways
  • Molecular Junctions and Nanostructures
  • Nanopore and Nanochannel Transport Studies
  • Microfluidic and Bio-sensing Technologies
  • Advanced Biosensing Techniques and Applications
  • RNA modifications and cancer
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Coagulation, Bradykinin, Polyphosphates, and Angioedema
  • Renal Diseases and Glomerulopathies
  • Microfluidic and Capillary Electrophoresis Applications
  • RNA Research and Splicing
  • Molecular Communication and Nanonetworks
  • Transgenic Plants and Applications
  • Gene Regulatory Network Analysis
  • Advanced Fluorescence Microscopy Techniques
  • Biochemical and Structural Characterization
  • Biotin and Related Studies
  • Click Chemistry and Applications

SUNY Upstate Medical University
2019-2023

Abstract Protein detection has wide-ranging implications in molecular diagnostics. Substantial progress been made protein analytics using nanopores and the resistive-pulse technique. Yet, a long-standing challenge is implementing specific interfaces for detecting proteins without steric hindrance of pore interior. Here, we formulate class sensing elements programmable antibody-mimetic binder fused to monomeric nanopore. This way, such modular design significantly expands utility nanopore...

10.1038/s41467-023-36944-9 article EN cc-by Nature Communications 2023-03-20

Ubiquitin‐binding shuttle UBQLN2 mediates crosstalk between proteasomal degradation and autophagy, likely via interactions with K48‐ K63‐linked polyubiquitin chains, respectively. comprises self‐associating regions that drive its homotypic liquid–liquid phase separation (LLPS). Specific one of these ubiquitin inhibit LLPS. Here, we show that, unlike ubiquitin, the effects multivalent chains on LLPS are highly dependent chain types. Specifically, K11‐Ub4 K48‐Ub4 generally LLPS, whereas...

10.15252/embr.202255056 article EN cc-by-nc-nd EMBO Reports 2022-06-28

Myo1e is a nonmuscle motor protein enriched in podocytes. Mutations MYO1E are associated with steroid-resistant nephrotic syndrome (SRNS). Most of the variants identified by genomic sequencing have not been functionally characterized. Here, we set out to analyze two mutations domain, T119I and D388H, which were selected on basis sequence conservation.EGFP-tagged human constructs delivered into Myo1e-KO mouse podocyte-derived cells via adenoviral infection stability, localization,...

10.1681/asn.2021111505 article EN Journal of the American Society of Nephrology 2022-09-09

Summary Ubiquitin-binding shuttle UBQLN2 mediates crosstalk between proteasomal degradation and autophagy, likely via interactions with K48- K63-linked polyubiquitin chains, respectively. is recruited to stress granules in cells undergoes liquid-liquid phase separation (LLPS) vitro . However, ubiquitin or multivalent K48-linked chains eliminate LLPS. Here, we found that, although some chain types (K11-Ub4 K48-Ub4) did generally inhibit LLPS, others (K63-Ub4, M1-Ub4 a designed tetrameric...

10.1101/2021.11.12.467822 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-11-13

Designing proteins that can switch between active (ON) and inactive (OFF) conformations in response to signals such as ligand binding incident light has been a tantalizing endeavor protein engineering for over decade. While designs have yielded novel biosensors, therapeutic agents, smart biomaterials, the times (times switching ON OFF) of many switches too slow be practical use. Among defining properties switches, kinetics most challenging optimize. This is largely due difficulty...

10.1021/acs.jpcb.1c04082 article EN The Journal of Physical Chemistry B 2021-07-29

A grand challenge in biosensor design is to develop a single molecule, fluorescent protein-based platform that can be easily adapted recognize targets of choice. Conceptually, this achieved by fusing small, antibody-like binding domain protein such way target activates fluorescence. Although simple envision, its execution not obvious. Here, we created family adaptable, turn-on monobody (ATOM) biosensors consisting monobody, circularly permuted at one two positions, inserted into three...

10.1101/2023.03.28.534597 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2023-03-28

ABSTRACT Protein-based fluorescent biosensors are powerful tools for analyte recognition in vitro and cells. Numerous proteinaceous binding scaffolds have been developed that recognize ligands with affinity specificity comparable to those of conventional antibodies, but smaller, readily overexpressed, more amenable engineering. Like these domains useful as modules protein switches biosensors, they not capable reporting on the event by themselves. Here, we engineer a small scaffold—a...

10.1101/2022.08.26.505460 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-08-26

Abstract Protein detection and biomarker profiling have wide-ranging implications in many areas of basic research molecular diagnostics. Substantial progress has been made protein analytics using nanopores the resistive-pulse technique. Yet, a long-standing challenge is implementing specific binding interfaces for detecting proteins without steric hindrance pore interior. To overcome this technological difficulty, we formulate new class sensing elements programmable antibody-mimetic binder...

10.1101/2022.10.12.511930 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-10-14

Abstract Myo1e is a non-muscle motor protein enriched in the podocyte foot processes. Mutations MYO1E are associated with steroid-resistant nephrotic syndrome (SRNS). Here, we set out to differentiate between pathogenic and neutral variants identified SRNS patients by exome sequencing. Based on sequence conservation structural predictions, two mutations domain, T119I D388H, were selected for this study. EGFP-tagged constructs delivered into Myo1e-KO podocytes via adenoviral infection analyze...

10.1101/2021.11.11.468158 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-11-12
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