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231222s2002 xx ||||| 00| ||eng c |
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|a (DE-627)NLM118666541
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|a (NLM)11989489
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Li, Xiangyang
|e verfasserin
|4 aut
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|a Sucrose regulation of ADP-glucose pyrophosphorylase subunit genes transcript levels in leaves and fruits
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|c 2002
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 04.06.2002
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|a Date Revised 13.12.2023
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|a published: Print
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|a Citation Status MEDLINE
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|a c2002 Elsevier Science Ireland Ltd. All rights reserved.
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|a ADP-glucose pyrophosphorylase (AGPase, EC2.7.7.27) is a key regulatory enzyme in starch biosynthesis. The enzyme is a heterotetramer with two S and two B subunits. In tomato, there are three multiple forms of the S subunit gene. Agp S1, S2 and B are highly expressed in fruit from 10 to 25 days after anthesis. Agp S3 is only weakly expressed in fruit. Sucrose significantly elevates expression of Agp S1, S2 and B in both leaves and fruits. Agp S1 exhibits the highest degree of regulation by sucrose. In fact, sucrose may be required for Agp S1 expression. For excised leaves incubated in water, no transcripts for Agp S1 could be detected in the absence of sucrose, whereas it took up to 16 h in water before transcripts were no longer detectable for Agp S2 and B. Neither Agp S3 nor the tubulin gene is affected by sucrose, demonstrating that this response is specifically regulated by a carbohydrate metabolic signal, and is not due to a general increase in metabolism caused by sucrose treatment. Truncated versions of the promoter for Agp S1 indicate that a specific region 1.3-3.0 kb upstream from the transcription site is responsible for sucrose sensitivity. This region of the S1 promoter contains several cis-acting elements present in the promoters of other genes that are also regulated by sucrose
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|a Comparative Study
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a NASA Discipline Life Support Systems
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|a Non-NASA Center
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|a Sucrose
|2 NLM
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|a 57-50-1
|2 NLM
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|a Nucleotidyltransferases
|2 NLM
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| 650 |
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|a EC 2.7.7.-
|2 NLM
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| 650 |
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|a Glucose-1-Phosphate Adenylyltransferase
|2 NLM
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| 650 |
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|a EC 2.7.7.27
|2 NLM
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| 650 |
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|a Glucuronidase
|2 NLM
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| 650 |
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|a EC 3.2.1.31
|2 NLM
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| 700 |
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|a Xing, Jinpeng
|e verfasserin
|4 aut
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| 700 |
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|a Gianfagna, Thomas J
|e verfasserin
|4 aut
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| 700 |
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|a Janes, Harry W
|e verfasserin
|4 aut
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| 700 |
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|a Gianfagna, Thomas J
|e investigator
|4 oth
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| 700 |
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|a Janes, Harry W
|e investigator
|4 oth
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| 773 |
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|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 162(2002), 2 vom: 03. Feb., Seite 239-44
|w (DE-627)NLM098174193
|x 0168-9452
|7 nnns
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| 773 |
1 |
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|g volume:162
|g year:2002
|g number:2
|g day:03
|g month:02
|g pages:239-44
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a AR
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|d 162
|j 2002
|e 2
|b 03
|c 02
|h 239-44
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