Results 151 to 160 of about 54,326 (298)

‘Candidatus Liberibacter Asiaticus’ Effector SECP8 Subverts Salicylic Acid‐Mediated Citrus Immunity via a Two‐Pronged Impairment of CsTCP15 Dimerization

Plant Biotechnology Journal, EarlyView.
ABSTRACT Citrus Huanglongbing (HLB), a devastating disease caused by the unculturable bacterium ‘Candidatus Liberibacter asiaticus’ (CLas), poses a severe threat to global citrus production. CLas secretes effectors to suppress host immune responses and facilitate its colonisation. Previously, the CLas effector SECP8 (CLIBASIA_05330) has been identified
Mingyue Qin, Rongyu Pan, Yaqian Shi, Pan Shen, Yuanjian Qiu, Xuejin Cui, Xuefeng Wang, Changyong Zhou, Shimin Fu   +8 more
wiley   +1 more source

Evidence for Covalent Modification of the Nuclear Dot–associated Proteins PML and Sp100 by PIC1/SUMO-1 [PDF]

, 1997
Thomas Sternsdorf, Kirsten Jensen, Hans Will   +2 more
openalex   +1 more source

A Bacterial Effector Hijacks NBR1 to Modulate Both Autophagy and Ubiquitination‐Mediated Degradation That Promotes Bacterial Infection

Plant Biotechnology Journal, EarlyView.
ABSTRACT Autophagy and the ubiquitin/26S proteasome system (UPS) play critical roles in the immune defence of the host against pathogen invasion. As a countermeasure, pathogens deploy effector proteins to subvert or hijack autophagy and UPS processes.
Yaqian Shi, Fang Fang, Xuejin Cui, Hongwei Shi, Zaiyu Yang, Xueyi Li, Changyong Zhou, Xuefeng Wang   +7 more
wiley   +1 more source

Canonical and non‐canonical functions of proteins regulating mitochondrial dynamics in mammalian physiology

The Journal of Physiology, EarlyView.
Abstract figure legend Mitochondria are highly dynamic organelles that continuously remodel their architecture through coordinated cycles of fusion and fission. This review examines the four key GTPases that orchestrate mitochondrial dynamics in mammals: MFN1, MFN2, OPA1, and DRP1.
Rémi Chaney, Vincent Marcangeli, Krystel Desjardins, Shima Taherkhani, Gilles Gouspillou   +4 more
wiley   +1 more source

The role of SUMOylation in biomolecular condensate dynamics and protein localization

Cell Insight
As a type of protein post-translational modification, SUMOylation is the process that attaches a small ubiquitin-like modifier (SUMO) to lysine residues of protein substrates. Not only do SUMO and ubiquitin exhibit structure similarity, but the enzymatic
Emily Gutierrez-Morton, Yanchang Wang
doaj   +1 more source

Phosphorylation-Dependent Control of Pc2 SUMO E3 Ligase Activity by Its Substrate Protein HIPK2 [PDF]

, 2006
Ana Roscic, Andreas Möller, Marco A. Calzado, Florian Renner, Verena C. Wimmer, Ekaterina Gresko, Katharina Schmid Lüdi, M. Lienhard Schmitz   +7 more
openalex   +1 more source

Hypoxia and the cytoskeleton

The Journal of Physiology, EarlyView.
Abstract figure legend Schematic outlining the activation of hypoxia‐sensitive pathways, the influence of hypoxia and associated pathways on the cytoskeleton, and the impact of these on disease progression. Abstract A highly‐regulated and dynamic cytoskeleton is vital for functional cellular physiology and the maintenance of homeostasis.
Darragh Flood, Cormac T. Taylor
wiley   +1 more source

Identification of SUMO modification sites in the base excision repair protein, Ntg1

, 2016
Daniel B. Swartzlander, Annie McPherson, H. R. Powers, Kristin Limpose, Emily G. Kuiper, Natalya Degtyareva, Anita H. Corbett, Paul W. Doetsch   +7 more
openalex   +1 more source

PIAS proteins promote SUMO-1 conjugation to STAT1 [PDF]

, 2003
Daniela Ungureanu, Sari Vanhatupa, Noora Kotaja, Jie Yang, Saara Aittomäki, Olli A. Jänne, Jorma J. Palvimo, Olli Silvennoinen   +7 more
openalex   +1 more source

Regulation of pyruvate dehydrogenase complex: Dancing to different drums in cancer

International Journal of Cancer, Volume 158, Issue 6, Page 1464-1480, 15 March 2026.
Abstract Mechanisms governing the regulation of pyruvate dehydrogenase complex (PDC) are markedly modified in cancer cells compared to normal cells. PDC activity in normal cells is controlled by the reversible phosphorylation of three serine residues by dedicated kinases and phosphatases.
Mulchand S. Patel, Todd C. Rideout
wiley   +1 more source