LTO1 Antibody

1. involved in abscisic acid-mediated response to osmotic stress PMID: 25171375
2. Results identified HCF164 as a direct target of LTO1 interacting with its thioredoxin-like domain suggesting that VKOR may play an important role in regulating the redox state of proteins in the thylakoid lume. PMID: 25412899
3. The conserved cysteines in the AtVKOR domain also played critical roles in phylloquinone reduction. When each of the four conserved cysteines was mutated to alanine, the mutants lost reduction activity entirely. PMID: 25267254
4. LTO1 is involved in the xanthophyll cycle and the acceleration of D1 protein degradation. PMID: 24300993
5. Lumen Thiol Oxidoreductase1 (LTO1) is a disulfide bond-forming enzyme in the thylakoid lumen. Loss of LTO1 produces a photosynthetic defect.[LTO1] PMID: 22209765
6. LTO1 plays important roles in redox regulation, ROS homeostasis and maintenance of PSII. PMID: 23689258
7. characterization of protein encoded by At4g35760 as disulfide bond oxidoreductase with 2 distinct domains (membrane domain homologous to catalytic subunit of VKOR and soluble DsbA-like domain) with protein sorting signal that targets to thylakoids PMID: 21781282
8. The VKORC1 domain of At4g35760 functions as a stringent naphthoquinone reductase, and that its reduced thioredoxin-like partner can serve as its electron donor. PMID: 20626653

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KEGG: ath:AT4G35760

STRING: 3702.AT4G35760.1

UniGene: At.43284