Xenopus 8 claims

genus · family Pipidae · animal · NCBI Taxonomy ↗

XenopusKuribo · CC BY-SA 4.0 · iNaturalist ↗

8 claims

Open in search (filters, sorting) →

Observationobservedoriginal resultnegativemeasured

Claim · model-written summary

Two Lsi2-like proteins showed no silicon efflux activity in Xenopus oocytes.

Taxon: XenopusXenopuse0
Organ / stage: oocytese0
Gene: Lsi2-like proteinse0
Outcome: efflux transport activity for Sie0

Verbatim

e0
“two Lsi2-like proteins did not show efflux transport activity for Si in Xenopus oocytes.”
✓ located verbatim in the source · abstract, characters 782–870

Title

Tomato roots have a functional silicon influx transporter but not a functional silicon efflux transporter

Hao Sun; Yaoke Duan; Namiki Mitani‐Ueno; et al. Plant Cell & Environment 2019. doi:10.1111/pce.13679

Other claims from this paper (9)

Observation SlLsi1 transported silicon in rice mutants and Xenopus oocytes.
Observation SlLsi1 was constitutively expressed in tomato roots.
Observation SlLsi1 localized to the plasma membrane of root tips and basal regions without polarity.
Intervention effect SlLsi1 overexpression raised silicon concentration in tomato roots and root cell sap.
Intervention effect SlLsi1 overexpression did not alter silicon concentration in tomato shoots.
Intervention effect Expressing cucumber CsLsi2 in tomato significantly increased silicon uptake.
Intervention effect Expressing CsLsi2 increased silicon accumulation in tomato leaves.
Intervention effect Expressing CsLsi2 enhanced tomato leaf tolerance to water deficit and heat.
Mechanism The authors attribute low tomato silicon accumulation to the lack of a functional Lsi2 efflux transporter.

Intervention effectobservedoriginal resultnegativesignificant (as stated)measured

Claim · model-written summary

PLP significantly repressed AKT1 activity in Xenopus oocytes.

Taxon: XenopusXenopuse0
Organ / stage: oocytee0
Treatment: PLPe0
Gene: AKT1e0
Outcome: activity of K(+) channel AKT1e0
Direction: repressede0

Not reportedComparator

Verbatim

e0
“PLP significantly repressed the activity of K(+) channel AKT1 in the Xenopus oocyte system and Arabidopsis root protoplasts.”
✓ located verbatim in the source · abstract, characters 1034–1158

Title

Nitric oxide negatively regulates AKT1-mediated potassium uptake through modulating vitamin B6 homeostasis in Arabidopsis

Jinchan Xia; Dongdong Kong; Shaowu Xue; et al. Proceedings of the National Academy of Sciences 2014. doi:10.1073/pnas.1417473111

Other claims from this paper (8)

Mechanism NO lowers AKT1-mediated potassium uptake by modulating vitamin B6 biosynthesis.
Observation The isolated NO-hypersensitive sno1 mutant is allelic to sos4.
Intervention effect NO increased plant PLP levels.
Intervention effect NO decreased plant potassium levels.
Intervention effect NO induced SNO1 expression and enzyme activity.
Mechanism NO-triggered PLP accumulation mainly proceeds through SNO1-mediated vitamin B6 salvage biosynthesis.
Intervention effect PLP significantly repressed AKT1 activity in Arabidopsis root protoplasts.
Mechanism NO is inferred to reduce Arabidopsis potassium absorption through PLP synthesis and subsequent AKT1 repression.

Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Heterologous ZmYS1 Fe-phytosiderophore transport was stimulated at acidic pH.

Taxon: XenopusXenopuse0
Treatment: acidic pHe0
Gene: ZmYS1e0
Outcome: ZmYS1-dependent Fe-phytosiderophore transporte0
Direction: stimulatede0
Qualifier: an iron uptake-defective yeast mutant and in Xenopus oocytese0

Not reportedComparator

Verbatim

e0
“ZmYS1 was expressed in an iron uptake-defective yeast mutant and in Xenopus oocytes, where ZmYS1-dependent Fe-phytosiderophore transport was stimulated at acidic pH and sensitive to CCCP.”
✓ located verbatim in the source · abstract, characters 631–818

Title

ZmYS1 Functions as a Proton-coupled Symporter for Phytosiderophore- and Nicotianamine-chelated Metals

Gabriel Schaaf; Uwe Ludewig; Bülent E. Erenoglu; et al. Journal of Biological Chemistry 2004. doi:10.1074/jbc.m311799200

Other claims from this paper (9)

Intervention effect Maize root Fe-phytosiderophore uptake was greater at acidic pH.
Intervention effect Maize Fe-phytosiderophore uptake was sensitive to CCCP.
Intervention effect Heterologous ZmYS1 transport was sensitive to CCCP.
Mechanism Transport depends on proton cotransport and membrane potential, permitting transport at alkaline pH.
Intervention effect ZmYS1 complemented the zinc uptake-defective zap1 yeast growth defect.
Observation ZmYS1 transported phytosiderophore-bound zinc, copper and nickel into oocytes.
Observation ZmYS1 transported phytosiderophore-bound manganese and cadmium at a lower rate.
Observation ZmYS1 also transported nicotianamine complexes of Ni(II), Fe(II) and Fe(III).
Mechanism The biochemical properties suggest a novel YS1 role in plant heavy metal homeostasis.

Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Heterologous ZmYS1 transport was sensitive to CCCP.

Taxon: XenopusXenopuse0
Treatment: CCCPe0
Gene: ZmYS1e0
Outcome: ZmYS1-dependent Fe-phytosiderophore transporte0

Not reportedComparatorDirection

Verbatim

e0
“ZmYS1 was expressed in an iron uptake-defective yeast mutant and in Xenopus oocytes, where ZmYS1-dependent Fe-phytosiderophore transport was stimulated at acidic pH and sensitive to CCCP.”
✓ located verbatim in the source · abstract, characters 631–818

Title

ZmYS1 Functions as a Proton-coupled Symporter for Phytosiderophore- and Nicotianamine-chelated Metals

Gabriel Schaaf; Uwe Ludewig; Bülent E. Erenoglu; et al. Journal of Biological Chemistry 2004. doi:10.1074/jbc.m311799200

Other claims from this paper (9)

Intervention effect Maize root Fe-phytosiderophore uptake was greater at acidic pH.
Intervention effect Maize Fe-phytosiderophore uptake was sensitive to CCCP.
Intervention effect Heterologous ZmYS1 Fe-phytosiderophore transport was stimulated at acidic pH.
Mechanism Transport depends on proton cotransport and membrane potential, permitting transport at alkaline pH.
Intervention effect ZmYS1 complemented the zinc uptake-defective zap1 yeast growth defect.
Observation ZmYS1 transported phytosiderophore-bound zinc, copper and nickel into oocytes.
Observation ZmYS1 transported phytosiderophore-bound manganese and cadmium at a lower rate.
Observation ZmYS1 also transported nicotianamine complexes of Ni(II), Fe(II) and Fe(III).
Mechanism The biochemical properties suggest a novel YS1 role in plant heavy metal homeostasis.

Mechanismobservedoriginal resultmeasured

Claim · model-written summary

Transport depends on proton cotransport and membrane potential, permitting transport at alkaline pH.

Taxon: XenopusXenopuse1
Gene: ZmYS1e0
Outcome: Fephytosiderophore transporte0
Qualifier: proton cotransport and on the membrane potentiale0

Verbatim

e0
“Electrophysiological analysis in oocytes demonstrated that Fephytosiderophore transport depends on proton cotransport and on the membrane potential, which allows ZmYS1-mediated transport even at alkaline pH.”
✓ located verbatim in the source · abstract, characters 819–1026

e1
“in Xenopus oocytes”
✓ located verbatim in the source · abstract, characters 696–714

Title

ZmYS1 Functions as a Proton-coupled Symporter for Phytosiderophore- and Nicotianamine-chelated Metals

Gabriel Schaaf; Uwe Ludewig; Bülent E. Erenoglu; et al. Journal of Biological Chemistry 2004. doi:10.1074/jbc.m311799200

Other claims from this paper (9)

Intervention effect Maize root Fe-phytosiderophore uptake was greater at acidic pH.
Intervention effect Maize Fe-phytosiderophore uptake was sensitive to CCCP.
Intervention effect Heterologous ZmYS1 Fe-phytosiderophore transport was stimulated at acidic pH.
Intervention effect Heterologous ZmYS1 transport was sensitive to CCCP.
Intervention effect ZmYS1 complemented the zinc uptake-defective zap1 yeast growth defect.
Observation ZmYS1 transported phytosiderophore-bound zinc, copper and nickel into oocytes.
Observation ZmYS1 transported phytosiderophore-bound manganese and cadmium at a lower rate.
Observation ZmYS1 also transported nicotianamine complexes of Ni(II), Fe(II) and Fe(III).
Mechanism The biochemical properties suggest a novel YS1 role in plant heavy metal homeostasis.

Observationobservedoriginal resultmeasured

Claim · model-written summary

ZmYS1 transported phytosiderophore-bound zinc, copper and nickel into oocytes.

Taxon: XenopusXenopuse1
Gene: ZmYS1e1
Outcome: zinc, copper, nickele0
Qualifier: phytosiderophore-bound metalse0

Verbatim

e0
“transported various phytosiderophore-bound metals into oocytes, including zinc, copper, nickel, and, at a lower rate, also manganese and cadmium.”
✓ located verbatim in the source · abstract, characters 1179–1324

e1
“in Xenopus oocytes, where ZmYS1-dependent Fe-phytosiderophore transport”
✓ located verbatim in the source · abstract, characters 696–767

Title

ZmYS1 Functions as a Proton-coupled Symporter for Phytosiderophore- and Nicotianamine-chelated Metals

Gabriel Schaaf; Uwe Ludewig; Bülent E. Erenoglu; et al. Journal of Biological Chemistry 2004. doi:10.1074/jbc.m311799200

Other claims from this paper (9)

Intervention effect Maize root Fe-phytosiderophore uptake was greater at acidic pH.
Intervention effect Maize Fe-phytosiderophore uptake was sensitive to CCCP.
Intervention effect Heterologous ZmYS1 Fe-phytosiderophore transport was stimulated at acidic pH.
Intervention effect Heterologous ZmYS1 transport was sensitive to CCCP.
Mechanism Transport depends on proton cotransport and membrane potential, permitting transport at alkaline pH.
Intervention effect ZmYS1 complemented the zinc uptake-defective zap1 yeast growth defect.
Observation ZmYS1 transported phytosiderophore-bound manganese and cadmium at a lower rate.
Observation ZmYS1 also transported nicotianamine complexes of Ni(II), Fe(II) and Fe(III).
Mechanism The biochemical properties suggest a novel YS1 role in plant heavy metal homeostasis.

Observationobservedoriginal resultmeasured

Claim · model-written summary

ZmYS1 transported phytosiderophore-bound manganese and cadmium at a lower rate.

Taxon: XenopusXenopuse1
Gene: ZmYS1e1
Outcome: manganese and cadmiume0
Direction: lowere0
Qualifier: phytosiderophore-bound metalse0
Comparator: zinc, copper, nickele0

Verbatim

e0
“transported various phytosiderophore-bound metals into oocytes, including zinc, copper, nickel, and, at a lower rate, also manganese and cadmium.”
✓ located verbatim in the source · abstract, characters 1179–1324

e1
“in Xenopus oocytes, where ZmYS1-dependent Fe-phytosiderophore transport”
✓ located verbatim in the source · abstract, characters 696–767

Title

ZmYS1 Functions as a Proton-coupled Symporter for Phytosiderophore- and Nicotianamine-chelated Metals

Gabriel Schaaf; Uwe Ludewig; Bülent E. Erenoglu; et al. Journal of Biological Chemistry 2004. doi:10.1074/jbc.m311799200

Other claims from this paper (9)

Intervention effect Maize root Fe-phytosiderophore uptake was greater at acidic pH.
Intervention effect Maize Fe-phytosiderophore uptake was sensitive to CCCP.
Intervention effect Heterologous ZmYS1 Fe-phytosiderophore transport was stimulated at acidic pH.
Intervention effect Heterologous ZmYS1 transport was sensitive to CCCP.
Mechanism Transport depends on proton cotransport and membrane potential, permitting transport at alkaline pH.
Intervention effect ZmYS1 complemented the zinc uptake-defective zap1 yeast growth defect.
Observation ZmYS1 transported phytosiderophore-bound zinc, copper and nickel into oocytes.
Observation ZmYS1 also transported nicotianamine complexes of Ni(II), Fe(II) and Fe(III).
Mechanism The biochemical properties suggest a novel YS1 role in plant heavy metal homeostasis.

Observationobservedoriginal resultmeasured

Claim · model-written summary

ZmYS1 also transported nicotianamine complexes of Ni(II), Fe(II) and Fe(III).

Taxon: XenopusXenopuse1
Gene: ZmYS1e0
Outcome: Ni(II), Fe(II), and Fe(III) complexes with nicotianaminee0

Verbatim

e0
“Unexpectedly, ZmYS1 also transported Ni(II), Fe(II), and Fe(III) complexes with nicotianamine”
✓ located verbatim in the source · abstract, characters 1325–1418

e1
“in Xenopus oocytes”
✓ located verbatim in the source · abstract, characters 696–714

Title

ZmYS1 Functions as a Proton-coupled Symporter for Phytosiderophore- and Nicotianamine-chelated Metals

Gabriel Schaaf; Uwe Ludewig; Bülent E. Erenoglu; et al. Journal of Biological Chemistry 2004. doi:10.1074/jbc.m311799200

Other claims from this paper (9)

Intervention effect Maize root Fe-phytosiderophore uptake was greater at acidic pH.
Intervention effect Maize Fe-phytosiderophore uptake was sensitive to CCCP.
Intervention effect Heterologous ZmYS1 Fe-phytosiderophore transport was stimulated at acidic pH.
Intervention effect Heterologous ZmYS1 transport was sensitive to CCCP.
Mechanism Transport depends on proton cotransport and membrane potential, permitting transport at alkaline pH.
Intervention effect ZmYS1 complemented the zinc uptake-defective zap1 yeast growth defect.
Observation ZmYS1 transported phytosiderophore-bound zinc, copper and nickel into oocytes.
Observation ZmYS1 transported phytosiderophore-bound manganese and cadmium at a lower rate.
Mechanism The biochemical properties suggest a novel YS1 role in plant heavy metal homeostasis.