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|a pubmed24n0514.xml
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|a (DE-627)NLM154178322
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|a (NLM)15763661
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Zhang, Chun
|e verfasserin
|4 aut
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|a Co-immunoprecipitation of Hsp101 with cytosolic Hsc70
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|c 2005
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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 04.05.2005
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a In animals and yeast, cytosolic Hsp70s function in concert with other molecular chaperones. Hsp70 is a major chaperone in the Hsp90 multi-chaperone complexes that participate in maturation of steroid receptors and several other proteins. Hsp70s also appear to form a complex with Hsp90 and Hsp110/sHsp. A 100 kDa protein was co-immunoprecipitated with cytosolic Hsc70 from maize seedlings (Zea mays). The presence of this complex was further confirmed using gel-filtration chromatography. Mass spectrometric analysis showed that the 100 kDa protein is homologous with Arabidopsis Hsp101. Treatment with apyrase enhanced the co-immunoprecipitation of Hsp101 with Hsc70, while ATP had the opposite effect. In the presence of carboxymethylated alpha-lactalbumin (CMLA), which is permanently unfolded, the complex dissociated. Based on these observations, it is concluded that Hsc70 and Hsp101 are present in a complex in the plant cytosol
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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 HSP101 protein, plant
|2 NLM
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|a HSP70 Heat-Shock Proteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Transcription Factors
|2 NLM
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|a Adenosine Triphosphate
|2 NLM
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|a 8L70Q75FXE
|2 NLM
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|a Lactalbumin
|2 NLM
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|a 9013-90-5
|2 NLM
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|a Apyrase
|2 NLM
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|a EC 3.6.1.5
|2 NLM
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|a Guy, Charles L
|e verfasserin
|4 aut
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 43(2005), 1 vom: 28. Jan., Seite 13-8
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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773 |
1 |
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|g volume:43
|g year:2005
|g number:1
|g day:28
|g month:01
|g pages:13-8
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|d 43
|j 2005
|e 1
|b 28
|c 01
|h 13-8
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