Characterizing endogenous protein complexes with biological mass spectrometry

R Rogawski, M Sharon - Chemical reviews, 2021 - ACS Publications
Biological mass spectrometry (MS) encompasses a range of methods for characterizing
proteins and other biomolecules. MS is uniquely powerful for the structural analysis of …

Single-pot, solid-phase-enhanced sample preparation for proteomics experiments

CS Hughes, S Moggridge, T Müller, PH Sorensen… - Nature protocols, 2019 - nature.com
A critical step in proteomics analysis is the optimal extraction and processing of protein
material to ensure the highest sensitivity in downstream detection. Achieving this requires a …

Extending the compatibility of the SP3 paramagnetic bead processing approach for proteomics

S Moggridge, PH Sorensen, GB Morin… - Journal of proteome …, 2018 - ACS Publications
The diversity in protein and peptide biochemistry necessitates robust protocols and reagents
for efficiently handling and enriching these molecules prior to analysis with mass …

Emerging technologies in adipose tissue research

D Avtanski, N Hadzi-Petrushev, S Josifovska… - Adipocyte, 2023 - Taylor & Francis
Technologies are transforming the understanding of adipose tissue as a complex and
dynamic tissue that plays a critical role in energy homoeostasis and metabolic health. This …

Ultrafast and reproducible proteomics from small amounts of heart tissue enabled by Azo and timsTOF pro

TJ Aballo, DS Roberts, JA Melby, KM Buck… - Journal of Proteome …, 2021 - ACS Publications
Global bottom-up mass spectrometry (MS)-based proteomics is widely used for protein
identification and quantification to achieve a comprehensive understanding of the …

Evaluation of six sample preparation procedures for qualitative and quantitative proteomics analysis of milk fat globule membrane

Y Yang, E Anderson, S Zhang - Electrophoresis, 2018 - Wiley Online Library
Proteomic analysis of membrane proteins is challenged by the proteins solubility and
detergent incompatibility with MS analysis. No single perfect protocol can be used to …

The mammalian CTLH complex is an E3 ubiquitin ligase that targets its subunit muskelin for degradation

MER Maitland, G Onea, CA Chiasson, XU Wang… - Scientific reports, 2019 - nature.com
The multi-subunit C-terminal to LisH (CTLH) complex is the mammalian homologue of the
yeast Gid E3 ubiquitin ligase complex. In this study, we investigated the human CTLH …

[HTML][HTML] Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex‐dependent regulation of glycolysis

MER Maitland, M Kuljanin, X Wang, GA Lajoie… - The FASEB …, 2021 - ncbi.nlm.nih.gov
Ubiquitination is an essential post‐translational modification that regulates protein stability
or function. Its substrate specificity is dictated by various E3 ligases. The human C‐terminal …

Distinct nuclear and cytoplasmic assemblies and interactomes of the mammalian CTLH E3 ligase complex

G Onea, MER Maitland, X Wang… - Journal of Cell …, 2022 - journals.biologists.com
The C-terminal to LisH (CTLH) complex is a newly discovered multi-subunit E3 ubiquitin
ligase and its cellular functions are poorly characterized. Although some CTLH subunits …

Interplay between β-propeller subunits WDR26 and muskelin regulates the CTLH E3 ligase supramolecular complex

MER Maitland, G Onea, DDG Owens… - Communications …, 2024 - nature.com
The Pro/N-degron recognizing C-terminal to LisH (CTLH) complex is an E3 ligase of
emerging interest in the developmental biology field and for targeted protein degradation …