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Sucrose‐phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves

https://doi.org/10.1016/0014-5793(90)81267-r
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19/19 checkable references clean · checked 2026-07-23

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

3 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 19 checked references that resolve
resolves10.1126/science.225.4664.801
Crop Productivity and Photoassimilate Partitioning
resolves10.1146/annurev.pp.39.060188.002533
Enzymatic Regulation of Photosynthetic CO2, Fixation in C3 Plants
resolves10.1111/j.1399-3054.1989.tb05402.x
Photosynthetic carbon partitioning: its regulation and possibilities for manipulation
resolves10.1146/annurev.pp.41.060190.001101
Fructose-2,6-Bisphosphate as a Regulatory Molecule in Plants
resolves10.1016/0014-5793(83)80627-9
Spinach leaf sucrose phosphate synthase
resolves10.1016/0168-9452(90)90205-3
Partial purification of two forms of spinach leaf sucrose-phosphate synthase which differ in their kinetic properties
resolves10.1007/BF00394774
Coarse control of sucrose-phosphate synthase in leaves: Alterations of the kinetic properties in response to the rate of photosynthesis and the accumulation of sucrose
resolves10.1104/pp.76.4.910
Changes of Sucrose-Phosphate Synthase Activity in Barley Primary Leaves during Light/Dark Transitions
resolves10.1007/BF00397888
Coordinate control of sucrose formation in soybean leaves by sucrose-phosphate synthase and fructose-2,6-bisphosphate
resolves10.1016/0003-9861(89)90551-1
Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity
resolves10.1042/bj2620335
Identification of high levels of type 1 and type 2A protein phosphatases in higher plants
resolves10.1016/0076-6879(88)59042-0
[40] Protein phosphatase inhibitor-1 and inhibitor-2 from rabbit skeletal muscle
resolves10.1016/0968-0004(90)90192-E
Okadaic acid: a new probe for the study of cellular regulation
resolves10.1016/0014-5793(90)80245-E
Cyanobacterial microcystin‐LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants
resolves10.1016/0076-6879(88)59039-0
[37] Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle
resolves10.1016/0014-5793(89)80803-8
An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues
resolves10.1007/BF00392622
Short-term water stress leads to a stimulation of sucrose synthesis by activating sucrose-phosphate synthase
resolves10.1016/0014-5793(81)80428-0
Regulation of mammalian acetyl‐CoA carboxylase
resolves10.1016/0014-5793(90)81381-W
<i>Bryophyllum fedtschenkoi</i> protein phosphatase type 2A can dephosphorylate phosphoenolpyruvate carboxylase
The 3 references without a DOI — listed, not checked
no DOI — not checked1987 Academic Press London M. Stitt S. Huber P. Kerr M.D. Hatch N.K. Boardman The Biochemistry of Plant 327 409
no DOI — not checkede_1_2_1_4_1
no DOI — not checkede_1_2_1_15_1
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-07-23 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

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