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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1111/nph.14827
|2 doi
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|a pubmed24n0931.xml
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|a (DE-627)NLM279347227
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|a (NLM)29271039
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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 Pulido, Pablo
|e verfasserin
|4 aut
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|a Novel DNAJ-related proteins in Arabidopsis thaliana
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 12.09.2019
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|a Date Revised 30.09.2020
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|a published: Print
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|a Citation Status MEDLINE
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|a © 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.
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|a Classical DNAJ proteins are co-chaperones that together with HSP70s control protein homeostasis. All three classical types of DNAJ proteins (DNAJA, DNAJB and DNAJC types) possess the J-domain for interaction with HSP70. DNAJA proteins contain, in addition, both the zinc-finger motif and the C-terminal domain which are involved in substrate binding, while DNAJB retains only the latter and DNAJC comprises only the J-domain. There is increasing evidence that some of the activities of DNAJ proteins do not require the J-domain, highlighting the functional significance of the other two domains. Indeed, the so-called DNAJ-like proteins with a degenerate J-domain have been previously coined as DNAJD proteins, and also proteins containing only a DNAJ-like zinc-finger motif appear to be involved in protein homeostasis. Therefore, we propose to extend the classification of DNAJ-related proteins into three different groups. The DNAJD type comprises proteins with a J-like domain only, and has 15 members in Arabidopsis thaliana, whereas proteins of the DNAJE (33 Arabidopsis members) and DNAJF (three Arabidopsis members) types contain a DNAJA-like zinc-finger domain and DNAJA/B-like C-terminal domain, respectively. Here, we provide an overview of the entire repertoire of these proteins in A. thaliana with respect to their physiological function and possible evolutionary origin
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a DNAJ
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|a DNAJ-related
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|a HSP70
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|a aggregation
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|a assembly factor
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|a chaperone
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|a protein folding
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|a protein quality control
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|a Arabidopsis Proteins
|2 NLM
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|a HSP40 Heat-Shock Proteins
|2 NLM
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|a Leister, Dario
|e verfasserin
|4 aut
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|i Enthalten in
|t The New phytologist
|d 1979
|g 217(2018), 2 vom: 01. Jan., Seite 480-490
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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|g volume:217
|g year:2018
|g number:2
|g day:01
|g month:01
|g pages:480-490
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|u http://dx.doi.org/10.1111/nph.14827
|3 Volltext
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|d 217
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|h 480-490
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