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Cited by 191

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts

Open access
Houba‐Hérin, Nicole, Pethe, Claude, D’Alayer, Jacques, Laloue, Michel·1999·The Plant Journal

Abstract

Summary: Cytokinins are degraded by cytokinin oxidases (CKOs) which catalyse cleavage of the N 6‐(isopent‐2‐enyl)‐side chain resulting in formation of adenine‐type compounds. CKO activity has been recorded in many plants and is thought to play a key role in controlling cytokinin levels in plants. Several partially purified CKOs have been characterised but no genes have been isolated yet. CKO activity is known to be inhibited by phenylureas, cytokinin agonists. We used 1‐(2‐azido‐6‐chloropyrid‐4‐yl)‐3‐(4‐[3 H])phenylurea ([3 H]‐azidoCPPU) to photolabel a glycosylated CKO from maize kernels. This enabled us to purify the enzyme. Peptide sequences were determined and the corresponding cDNA was cloned. The deduced amino acid sequence shares homology domains with FAD‐dependent oxidases. An original assay based on transient expression of the enzyme in moss protoplasts allowed the functionality of the recombinant enzyme to be demonstrated.

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Crossref · 10.1046/j.1365-313x.1999.00408.x

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Metadata

Authors
Houba‐Hérin, N., Pethe, C., D’Alayer, J., & Laloue, M.
Venue
The Plant Journal
Publisher
Wiley
Published
1999-03
Volume
17
Issue
6
Pages
615-626
ISSN
  • 0960-7412 (ISSN-L)
  • 1365-313X
OpenAlex
W2030356145
Cited by
191
References
1
FWCI
13.81
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts. https://app.cochat.ai/papers/10.1046/j.1365-313x.1999.00408.x
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Houba‐Hérin, N., Pethe, C., D’Alayer, J., & Laloue, M. (1999). Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts. The Plant Journal. https://doi.org/10.1046/j.1365-313x.1999.00408.x

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