Results 61 to 70 of about 3,959 (198)

Unfolding Plant Defence: Endoplasmic Reticulum Stress Signalling at the Plant‐Pathogen Interface

open access: yesPlant Biotechnology Journal, EarlyView.
ABSTRACT The endoplasmic reticulum (ER) stress response, a conserved proteostasis network, has emerged as a central hub that reprograms plant immunity during pathogen attack. This review synthesises how plants harness ER‐stress signalling to mount multilayered defences and how pathogens have evolved counterstrategies to subvert these pathways.
Zhe Meng   +8 more
wiley   +1 more source

Table_3_Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein.xlsx

open access: yes, 2022
Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides (142926)
core   +1 more source

Genomic and Transcriptomic Insights Into Salinity Tolerance in Dry Pea

open access: yesLegume Science, Volume 8, Issue 2, June 2026.
ABSTRACT Salinity is a major crop production constraint in dry pea (Pisum sativum L.), making the development of salt‐tolerant varieties essential to improve crop productivity and land‐use efficiency. The genetic mechanisms of salt tolerance in dry pea are largely unknown, and research on salt‐tolerant genes is limited.
Shailesh Raj Acharya   +11 more
wiley   +1 more source

Light‐Activated Protein‐Imprinted Hydrogels Capable of Translating Protein Surface Accessibility Into Missing‐Peptide Footprints

open access: yesSmall Structures, Volume 7, Issue 6, June 2026.
Light‐activated protein‐imprinted PFPA‐functionalized hydrogels crosslink captured proteins and report protein surface accessibility as missing‐peptide patterns readable by standard LC‐MS/MS. Mass spectrometry (MS)‐based structural proteomics can reveal higher‐order structural features in complex biological samples, but many covalent footprinting and ...
Eisuke Kanao   +10 more
wiley   +1 more source

The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling. [PDF]

open access: yesPLoS ONE, 2015
FKBP52 and β-catenin have emerged in recent years as attractive targets for prostate cancer treatment. β-catenin interacts directly with the androgen receptor (AR) and has been characterized as a co-activator of AR-mediated transcription.
Cheryl Storer Samaniego   +12 more
doaj   +1 more source

Image_1_Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein.tif

open access: yes, 2022
Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides (142926)
core   +1 more source

The GmGT‐2F, a trihelix transcription factor, regulates seed oil content by directly activating GmAGAL transcription in soybean

open access: yesJournal of Integrative Plant Biology, Volume 68, Issue 6, Page 1794-1814, June 2026.
In soybean, the trihelix transcription factor GmGT‐2F positively regulates the expression of the α‐galactosidase gene GmAGAL, thereby modulating seed oil content. The cyclophilin GmCYP2 interacts with GmGT‐2F and suppresses GmAGAL activation. Haplotype diversity analysis of GmGT‐2F, GmCYP2, and GmAGAL identified favorable haplotype combinations ...
Shuangzhe Li   +6 more
wiley   +1 more source

TAL effectors target the C-terminal domain of RNA polymerase II (CTD) by inhibiting the prolyl-isomerase activity of a CTD-associated cyclophilin. [PDF]

open access: yesPLoS ONE, 2012
Transcriptional activator-like (TAL) effectors of plant pathogenic bacteria function as transcription factors in plant cells. However, how TAL effectors control transcription in the host is presently unknown.
Mariane Noronha Domingues   +4 more
doaj   +1 more source

Table_4_Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein.docx

open access: yes, 2022
Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides (142926)
core   +1 more source

Requirement of a mip-Like Gene for Virulence in the Phytopathogenic Bacterium Xanthomonas campestris pv. campestris

open access: yesMolecular Plant-Microbe Interactions, 2007
Macrophage infectivity potentiators (Mips) are FKBP domain-containing proteins reported as virulence factors in several human pathogens, such as members of genera Legionella, Salmonella and Chlamydia.
Ning Zang   +9 more
doaj   +1 more source

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