Julia Ast

Publications : 21
Aldex : 20
H-index : 8
Citations : 338

Two Pex5 Proteins With Different Cargo Specificity Are Critical for Peroxisome Function in Ustilago maydis.

Julia Ast et 7 al.

May 12, 2022 in Frontiers in cell and developmental biology
Peroxisomes are dynamic multipurpose organelles with a major function in fatty acid oxidation and breakdown of hydrogen peroxide. Many proteins destined for the peroxisomal matrix contain a C-terminal peroxisomal targeting signal type 1 (PTS1), which is recognized by tetratricopeptide repeat (TPR) proteins of the Pex5 family. Various species express at least two different Pex5 proteins, but how th...

chemistry

Expanded LUXendin Color Palette for GLP1R Detection and Visualization In Vitro and In Vivo

Julia Ast et 14 al.

Apr 4, 2022 in JACS Au
JACS AuDOI: 10.1021/jacsau.2c00130

biology

14-3-3ζ constrains insulin secretion by regulating mitochondrial function in pancreatic β-cells.

Yves Mugabo, Gareth E Lim et 14 al.

Mar 17, 2022 in JCI insight
While critical for neurotransmitter synthesis, 14-3-3 proteins are often assumed to have redundant functions due to their ubiquitous expression, but despite this assumption, various 14-3-3 isoforms have been implicated in regulating metabolism. We previously reported contributions of 14-3-3ζ in β-cell function, but these studies were performed in tumor-derived MIN6 cells and systemic knockout mice...

science

Journal Club

Andreas Peschel, Daniela Kruck et 13 al.

Feb 13, 2022 in Biospektrum

Sulfonated red and far-red rhodamines to visualize SNAP- and Halo-tagged cell surface proteins.

Ramona Birke et 16 al.

Feb 21, 2022 in Organic & biomolecular chemistry
The (in)ability to permeate membranes is a key feature of chemical biology probes that defines their suitability for specific applications. Here we report sulfonated rhodamines that endow xanthene dyes with cellular impermeability for analysis of surface proteins. We fuse charged sulfonates to red and far-red dyes to obtain Sulfo549 and Sulfo646, respectively, and further link these to benzylguani...

cardiology

GLP1R Attenuates Sympathetic Response to High Glucose via Carotid Body Inhibition

Audrys G. Pauza, David Murphy et 14 al.

Feb 1, 2022 in Circulation Research

Reagents and models for detecting endogenous GLP1R and GIPR.

Julia Ast et 3 al.

Dec 12, 2021 in EBioMedicine
Glucagon-like peptide-1 receptor (GLP1R) agonists target the GLP1R, whereas dual GLP1R/ gastric inhibitory polypeptide receptor (GIPR) agonists target both the GLP1R and GIPR. Despite the importance of these drug classes for the treatment of diabetes and obesity, still very little is known about the localization of GLP1R and GIPR themselves. Complicating matters is the low abundance of GLP1R and G...

chemistry

LUXendins reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics

Julia Ast et 20 al.

Jan 1, 2019 in bioRxiv
The glucagon-like peptide-1 receptor (GLP1R) is a class B G protein-coupled receptor (GPCR) involved in metabolism. Presently, its visualization is limited to genetic manipulation, antibody detection or the use of probes that stimulate receptor activation. Herein, we present LUXendin645, a far-red fluorescent GLP1R antagonistic peptide label. LUXendin645 produces intense and specific membrane labe...

chemistry

Interrogating surface versus intracellular transmembrane receptor populations using cell-impermeable SNAP-tag substrates

Pascal Poc et 11 al.

Jan 1, 2020 in Chemical Science
Employing self-labelling protein tags for the attachment of fluorescent dyes has become a routine and powerful technique in optical microscopy to visualize and track fused proteins. However, membrane permeability of the dyes and the associated background signals can interfere with the analysis of extracellular labelling sites. Here we describe a novel approach to improve extracellular labelling by...

chemistry

Interrogating surface versus intracellular transmembrane receptor populations using cell-impermeable SNAP-tag substrates

Pascal Poc et 10 al.

Jan 1, 2020 in bioRxiv
Employing self-labelling protein tags for the attachment of fluorescent dyes has become a routine and powerful technique in optical microscopy to visualize and track fused proteins. However, membrane permeability of the dyes and the associated background signals can interfere with the analysis of extracellular labeling sites. Here we describe a novel approach to improve extracellular labeling by f...

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