Psychoactive Plant Database - Neuroactive Phytochemical Collection

1. Electrophoresis. 2024 Nov 7. doi: 10.1002/elps.202400122. Online ahead of
print.

A Comprehensive Review on Capillary Electrophoresis-Mass Spectrometry in 
Advancing Biomolecular Research.

Pont L(1)(2), Vergara-Barberán M(3), Carrasco-Correa EJ(3).

Author information:
(1)Department of Chemical Engineering and Analytical Chemistry, Institute for 
Research on Nutrition and Food Safety (INSA·UB), University of Barcelona, 
Barcelona, Spain.
(2)Serra Húnter Program, Generalitat de Catalunya, Barcelona, Spain.
(3)CLECEM Group, Department of Analytical Chemistry, University of Valencia, 
Valencia, Spain.

This review provides an in-depth exploration of capillary electrophoresis-mass 
spectrometry (CE-MS) in biomolecular research from 2020 to 2024. CE-MS emerges 
as a versatile and powerful tool due to its numerous advantages, facilitating 
the analysis of various biomolecules, including proteins, peptides, 
oligonucleotides, and other metabolites, such as lipids, carbohydrates, or 
amines, among others. The review extends to various CE modes and interfaces for 
the CE-MS coupling, offering comprehensive insights into their applications 
within biomolecular research. Furthermore, it effectively summarizes the 
conditions employed in CE-MS while also addressing critical aspects such as 
sample preparation requirements. Despite its advantages, the review highlights a 
gap between discovery and practical implementation, underscoring the need for 
large-scale validation and method standardization to fully realize the potential 
of CE-MS in biomolecular research.

© 2024 The Author(s). Electrophoresis published by Wiley‐VCH GmbH.

DOI: 10.1002/elps.202400122
PMID: 39508247


2. Biol Direct. 2024 Nov 6;19(1):102. doi: 10.1186/s13062-024-00562-2.

RNF19A inhibits bladder cancer progression by regulating ILK ubiquitination and 
inactivating the AKT/mTOR signalling pathway.

Deng H(1)(2), Ji G(1), Ma J(3), Cai J(4), Cheng S(5), Cheng F(6).

Author information:
(1)Department of Urology, The First Affiliated Hospital of Yangtze University, 
The First people's Hospital of Jingzhou, Jingzhou, 434000, China.
(2)Department of Urology, Renmin Hospital of Wuhan University, Wuhan, 430060, 
China.
(3)Department of Urology, Shanghai Public Health Clinical Center, Shanghai, 
200083, China.
(4)Department of Oncology, The First Affiliated Hospital of Yangtze University, 
The First people's Hospital of Jingzhou, Jingzhou, 434000, China. 
caijun1816313@126.com.
(5)Department of Urology, The First Affiliated Hospital of Yangtze University, 
The First people's Hospital of Jingzhou, Jingzhou, 434000, China. 
chengsp0401@126.com.
(6)Department of Urology, Renmin Hospital of Wuhan University, Wuhan, 430060, 
China. urology1969@aliyun.com.

BACKGROUND: The role of the RING finger protein superfamily in carcinogenesis 
has been widely studied, but one member of this family, RNF19A, has not yet been 
thoroughly explored in bladder cancer (BCa).
METHODS: The expression levels of RNF19A in BCa samples and cell lines were 
analysed through data mining of public resources and further experiments. BCa 
cells in which RNF19A was stably overexpressed or knocked down were generated 
through lentivirus infection. The effects of RNF19A on cell proliferation, 
migration, and invasion were explored by performing a series of in vitro 
experiments, including CCK-8, colony formation, wound healing, and Transwell 
invasion assays. Using bioinformatics methods and multiple experiments, 
including western blot, qRT‒PCR, immunoprecipitation, cycloheximide, 
ubiquitination, and rescue assays, the mechanism underlying the effect of RNF19A 
on the progression of BCa was investigated.
RESULTS: Here, we found that RNF19A expression was reduced in BCa samples and 
cell lines and that lower RNF19A expression predicted shorter overall survival 
of BCa patients. Functionally, forced expression of RNF19A suppressed BCa cell 
proliferation, migration, and invasion by inactivating the AKT/mTOR signalling 
pathway, whereas silencing RNF19A had the opposite effects. Mechanistically, 
RNF19A could directly interact with ILK and promote its ubiquitination and 
degradation. Rescue experiments revealed that forced ILK expression partially 
rescued the decreased phosphorylation of AKT, mTOR, and S6K1 caused by RNF19A 
overexpression and that the increased levels of the p-AKT, p-mTOR, and p-S6K1 
proteins induced by RNF19A knockdown were eliminated after silencing ILK. 
Similarly, the effects of RNF19A overexpression or knockdown on the phenotypes 
of cell proliferation, migration, and invasion could also be restored by forced 
or decreased ILK expression.
CONCLUSIONS: RNF19A suppressed the proliferation, migration, and invasion 
abilities of BCa cells by regulating ILK ubiquitination and inactivating the 
AKT/mTOR signalling pathway. RNF19A might be a potential prognostic biomarker 
and promising therapeutic target for BCa.

© 2024. The Author(s).

DOI: 10.1186/s13062-024-00562-2
PMID: 39508245


3. Cytoskeleton (Hoboken). 2024 Nov 7. doi: 10.1002/cm.21955. Online ahead of 
print.

Alteration of Cytoskeletal Proteins Leads to Retinal Degeneration in Drosophila.

Sahu S(1), Mishra M(1).

Author information:
(1)Neural Developmental Biology Lab, Department of Life Science, NIT Rourkela, 
Rourkela, India.

The eye holds a special fascination for many neuroscientists because of its 
meticulously organized structure. Vertebrates typically possess a simple 
camera-type eye, whereas the compound eye structure is predominantly observed in 
arthropods including model organism Drosophila melanogaster. Cell shape, cell 
polarization, and tissue integrity are the cell biological processes crucial for 
shaping the eye, which directly or indirectly depends on the cytoskeleton. 
Henceforth the cytoskeleton, specifically actin microfilaments, essentially has 
a dynamic role in the normal development and growth of eye structure. This 
review provides insight into the roles played by the actin cytoskeleton during 
the development and maintenance of the Drosophila eye.

© 2024 Wiley Periodicals LLC.

DOI: 10.1002/cm.21955
PMID: 39508206


4. RNA Biol. 2024 Jan;21(1):70-81. doi: 10.1080/15476286.2024.2417152. Epub 2024 
Nov 7.

Plant ribosomes as a score to fathom the melody of 2'-O-methylation across 
evolution.

Neumann SA(1)(2), Gaspin C(3)(4), Sáez-Vásquez J(1)(2).

Author information:
(1)CNRS, Laboratoire Génome et Développement des Plantes (LGDP), UMR 5096, 
Perpignan, France.
(2)University Perpignan Via Domitia, LGDP, UMR 5096, Perpignan, France.
(3)Université Fédérale de Toulouse, INRAE, MIAT, Castanet-Tolosan, France.
(4)Université Fédérale de Toulouse, INRAE, BioinfOmics, Genotoul Bioinformatics 
Facility, Castanet-Tolosan, France.

2'-O-ribose methylation (2'-O-Me) is one of the most common RNA modifications 
detected in ribosomal RNAs (rRNA) from bacteria to eukaryotic cells. 2'-O-Me 
favours a specific RNA conformation and protects RNA from hydrolysis. Moreover, 
rRNA 2'-O-Me might stabilize its interactions with messenger RNA (mRNA), 
transfer RNA (tRNA) or proteins. The extent of rRNA 2'-O-Me fluctuates between 
species from 3-4 sites in bacteria to tens of sites in archaea, yeast, algae, 
plants and human. Depending on the organism as well as the rRNA targeting site 
and position, the 2'-O-Me reaction can be carried out by several site-specific 
RNA methyltransferases (RMTase) or by a single RMTase associated to specific RNA 
guides. Here, we review current progresses in rRNA 2'-O-Me (sites/Nm and 
RMTases) in plants and compare the results with molecular clues from unicellular 
(bacteria, archaea, algae and yeast) as well as multicellular (human and plants) 
organisms.

DOI: 10.1080/15476286.2024.2417152
PMID: 39508203 [Indexed for MEDLINE]


5. Mol Plant Pathol. 2024 Nov;25(11):e70027. doi: 10.1111/mpp.70027.

A single phosphorylatable amino acid residue is essential for the recognition of 
multiple potyviral HCPro effectors by potato Ny(tbr).

Alex BG(1), Zhang ZY(1)(2), Lasky D(1), Garcia-Ruiz H(3), Dewberry R(1), Allen 
C(1), Halterman D(4), Rakotondrafara AM(1).

Author information:
(1)Department of Plant Pathology, University of Wisconsin-Madison, Madison, 
Wisconsin, USA.
(2)Ministry of Agriculture and Rural Affairs Key Laboratory of Pest Monitoring 
and Green Management, College of Plant Protection, China Agricultural 
University, Beijing, China.
(3)Department of Plant Pathology and Nebraska Center for Virology, University of 
Nebraska-Lincoln, Lincoln, Nebraska, USA.
(4)United States Department of Agriculture-Agricultural Research Service, 
Madison, Wisconsin, USA.

Potato virus Y (PVY, Potyviridae) is among the most important viral pathogens of 
potato. The potato resistance gene Nytbr confers hypersensitive resistance to 
the ordinary strain of PVY (PVYO), but not the necrotic strain (PVYN). Here, we 
unveil that residue 247 of PVY helper component proteinase (HCPro) acts as a 
central player controlling Nytbr strain-specific activation. We found that 
substituting the serine at 247 in the HCPro of PVYO (HCProO) with an alanine as 
in PVYN HCPro (HCProN) disrupts Nytbr recognition. Conversely, an HCProN mutant 
carrying a serine at position 247 triggers defence. Moreover, we demonstrate 
that plant defences are induced against HCProO mutants with a phosphomimetic or 
another phosphorylatable residue at 247, but not with a phosphoablative residue, 
suggesting that phosphorylation could modulate Nytbr resistance. Extending 
beyond PVY, we establish that the same response elicited by the PVYO HCPro is 
also induced by HCPro proteins from other members of the Potyviridae family that 
have a serine at position 247, but not by those with an alanine. Together, our 
results provide further insights in the strain-specific PVY resistance in potato 
and infer a broad-spectrum detection mechanism of plant potyvirus effectors 
contingent on a single amino acid residue.

© 2024 The Author(s). Molecular Plant Pathology published by British Society for 
Plant Pathology and John Wiley & Sons Ltd.

DOI: 10.1111/mpp.70027
PMID: 39508202 [Indexed for MEDLINE]