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01000caa a22002652 4500 |
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NLM167894811 |
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DE-627 |
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20250207232852.0 |
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231223s2007 xx ||||| 00| ||eng c |
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|a pubmed25n0560.xml
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|a (DE-627)NLM167894811
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|a (NLM)17244628
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Gucciardo, Sébastian
|e verfasserin
|4 aut
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| 245 |
1 |
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|a A germin-like protein with superoxide dismutase activity in pea nodules with high protein sequence identity to a putative rhicadhesin receptor
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|c 2007
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 11.07.2007
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|a Date Revised 09.01.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The cDNAs encoding three germin-like proteins (PsGER1, PsGER2a, and PsGER2b) were isolated from Pisum sativum. The coding sequence of PsGER1 transiently expressed in tobacco leaves gave a protein with superoxide dismutase activity but no detectable oxalate oxidase activity according to in-gel activity stains. The transient expression of wheat germin gf-2.8 oxalate oxidase showed oxalate oxidase but no superoxide dismutase activity under the same conditions. The superoxide dismutase activity of PsGER1 was resistant to high temperature, denaturation by detergent, and high concentrations of hydrogen peroxide. In salt-stressed pea roots, a heat-resistant superoxide dismutase activity was observed with an electrophoretic mobility similar to that of the PsGER1 protein, but this activity was below the detection limit in non-stressed or H(2)O(2)-stressed pea roots. Oxalate oxidase activity was not detected in either pea roots or nodules. Following in situ hybridization in developing pea nodules, PsGER1 transcript was detected in expanding cells just proximal to the meristematic zone and also in the epidermis, but to a lesser extent. PsGER1 is the first known germin-like protein with superoxide dismutase activity to be associated with nodules. It shared protein sequence identity with the N-terminal sequence of a putative plant receptor for rhicadhesin, a bacterial attachment protein. However, its primary location in nodules suggests functional roles other than as a rhicadhesin receptor required for the first stage of bacterial attachment to root hairs
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Adhesins, Bacterial
|2 NLM
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| 650 |
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|a DNA, Complementary
|2 NLM
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| 650 |
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|a DNA, Plant
|2 NLM
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| 650 |
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|a Glycoproteins
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Receptors, Cell Surface
|2 NLM
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| 650 |
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|a adhesin, Rhizobium
|2 NLM
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| 650 |
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7 |
|a germin
|2 NLM
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| 650 |
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|a 123339-15-1
|2 NLM
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| 650 |
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|a Superoxide Dismutase
|2 NLM
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| 650 |
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7 |
|a EC 1.15.1.1
|2 NLM
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| 700 |
1 |
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|a Wisniewski, Jean-Pierre
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Brewin, Nicholas J
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Bornemann, Stephen
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 58(2007), 5 vom: 16., Seite 1161-71
|w (DE-627)NLM098182706
|x 0022-0957
|7 nnns
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| 773 |
1 |
8 |
|g volume:58
|g year:2007
|g number:5
|g day:16
|g pages:1161-71
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_350
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| 951 |
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|a AR
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| 952 |
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|d 58
|j 2007
|e 5
|b 16
|h 1161-71
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