Results 91 to 100 of about 444 (152)

Direct Zinc Finger Protein Persulfidation by H\textsubscript2 S Is Facilitated by Zn\textsuperscript2+

, 2019
H 2 S is a gaseous signaling molecule that modifies cysteine residues in proteins to form persulfides (P-SSH). One family of proteins modified by H 2 S are zinc finger (ZF) proteins, which contain multiple zinc-coordinating cysteine residues.
Kiwon Ok, Michel, Sarah L. J., Ivana Ivanović‐Burmazović, Lange, Mike, Biljana Bursac, Bursac, Biljana, Ok, Kiwon, Markó, Lajos, Filipovic, Milos R., Geoffrey D. Shimberg, Shimberg, Geoffrey D., Sarah L. J. Michel, Lajos Markó, Ivanovic-Burmazovic, Ivana, Mike Lange, Milos R. Filipovic   +15 more
core   +1 more source

Persulfidome of Sweet Pepper Fruits during Ripening: The Case Study of Leucine Aminopeptidase That Is Positively Modulated by H₂S

Antioxidants
Protein persulfidation is a thiol-based oxidative posttranslational modification (oxiPTM) that involves the modification of susceptible cysteine thiol groups present in peptides and proteins through hydrogen sulfide (H2S), thus affecting their function ...
María A. Muñoz-Vargas, Salvador González-Gordo, Angeles Aroca, Luis C. Romero, Cecilia Gotor, José M. Palma, Francisco J. Corpas   +6 more
doaj   +1 more source

Abstracts

Molecular Oncology, Volume 19, Issue S1, Page 1-940, June 2025.
Abstracts submitted to the ‘EACR 2025 Congress: Innovative Cancer Science’, from 16–19 June 2025 and accepted by the Congress Organising Committee are published in this Supplement of Molecular Oncology, an affiliated journal of the European Association for Cancer Research (EACR).
wiley   +1 more source

Quantification of persulfidation on specific proteins: are we nearly there yet? [PDF]

Hydrogen sulfide (H2S) played a pivotal role in the early evolution of life on Earth before the predominance of atmospheric oxygen. The legacy of a persistent role for H2S in life’s processes recently emerged through its discovery in modern biochemistry ...
Liu, H, Negoita, F, Liu, Hongling, Brook, Matthew; id_orcid, Morton, Nicholas M, Brook, M, Brook, Matthew, Negoita, Florentina, Sakamoto, Kei, Morton, Nicholas M., Sakamoto, K, Morton, NM   +11 more
core   +1 more source

Versatile roles of cysteine persulfides in tumor biology

Current Opinion in Chemical Biology
Rewiring the transsulfuration pathway is recognized as a rapid adaptive metabolic response to environmental conditions in cancer cells to support their increased cysteine demand and to produce Reactive Sulfur Species (RSS) including hydrogen sulfide (H2S) and cysteine persulfide.
Klaudia Borbényi-Galambos, Ágnes Czikora, Katalin Erdélyi, Péter Nagy   +3 more
openaire   +2 more sources

Polysulfide and persulfide-mediated activation of the PERK-eIF2α-ATF4 pathway increases Sestrin2 expression and reduces methylglyoxal toxicity

Redox Biology
Unfolded protein response (UPR) is activated in cells under endoplasmic reticulum (ER) stress. One sensor protein involved in this response is PERK, which is activated through its redox-dependent oligomerization.
Shin Koike, Hideo Kimura, Yuki Ogasawara
doaj   +1 more source

Insights from Structure-Based Simulations into the Persulfidation of Uridine Diphosphate-Glycosyltransferase71c5 Facilitating the Reversible Inactivation of Abscisic Acid

The action of abscisic acid (ABA) is closely related to its level in plant tissues. Uridine diphosphate-glycosyltransferase71c5 (UGT71C5) was characterized as a major UGT enzyme to catalyze the formation of the ABA-glucose ester (ABA-GE), a reversible ...
Guojing Chen, Lingxi Geng, Taotao Qiu, Sisong Lai, Siqi Huang, Lihui Xiao, Ke Sun, Yanjie Xie, Miaomiao Li   +8 more
core   +1 more source

Metabolic dysfunction-associated steatohepatitis reduces hepatic H2S-producing enzymes altering persulfidome composition

Redox Biology
Metabolic dysfunction–associated steatohepatitis (MASH) is a progressive disease driven by obesity-related hepatic inflammation and oxidative stress.
Tzu Keng Shen, Thibaut Vignane, Eduardo H. Gilglioni, Leonardo Traini, Elisavet Kalaitsidou, Pierre Conan, Ao Li, Wadsen St-Pierre-Wijckmans, Jose M. Herranz, Bernat Elvira, Lukas Otero Sanchez, Eric Trépo, Leo Deelman, Wei Wu, Milos R. Filipovic, Joris Messens, Daria Ezeriņa, Esteban N. Gurzov   +17 more
doaj   +1 more source

Self-S-sulfonation in a bacterial persulfide dioxygenase mediates thiol persulfide detoxification

A ubiquitous class of non-heme Fe(II) enzymes, the persulfide dioxygenases (PDOs), provide protection against hydrogen sulfide (H2S) poisoning. The PDO in humans is a single-domain enzyme, while bacterial PDOs, such as CstB of Staphylococcus aureus, are often fused to a sulfurtransferase (rhodanese) module.
Julius O. Campecino, Sofia S. Costa, Brenna J.C. Walsh, Jonathan C. Trinidad, Jyoti Kannoujia, Andrew T. Poor, Casey M. Van Stappen, Giovanni Gonzalez-Gutierrez, Margarida Archer, Jose A. Brito, David P. Giedroc   +10 more
openaire   +1 more source

Sulfite oxidase deficiency causes persulfidation loss and hydrogen sulfide release [PDF]

Sulfite oxidase (SOX) deficiency is a rare inborn error of cysteine metabolism resulting in severe neurological damage. In patients, sulfite accumulates to toxic levels, causing a rise in the downstream products S-sulfocysteine, which mediates ...
D'Andrea, Davide, Kohl, Joshua B., Kozich, Viktor, Filipovic, Milos, Mai, Max, Morita, Masanobu, Santamaria-Araujo, José Angel, Kouroussis, Emilia, Yeo, Sin Yuin, Ditrói, Tamás, Nagy, Peter, Gehling, Titus, Křížková, Michaela, Krueger, Marcus, Hennermann, Julia B., Mellis, Anna T., Endepols, Heike, Fu, Chun-Yu, Schwarz, Guenter, Ogata, Seiryo, Barayeu, Uladzimir, Akaike, Takaaki, Neuser, Franziska, Liebsch, Filip   +23 more
core   +1 more source