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Metal binding by citrus dehydrin with histidine-rich domains

Metal binding by citrus dehydrin with histidine-rich domains

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_235006218

Metal binding by citrus dehydrin with histidine-rich domains

About this item

Full title

Metal binding by citrus dehydrin with histidine-rich domains

Publisher

Oxford: Oxford University Press

Journal title

Journal of experimental botany, 2005-10, Vol.56 (420), p.2695-2703

Language

English

Formats

Publication information

Publisher

Oxford: Oxford University Press

More information

Scope and Contents

Contents

Dehydrins are hydrophilic proteins that are responsive to osmotic stress, such as drought, cold, and salinity in plants. Although they have been hypothesized to stabilize macromolecules in stressed cells, their functions are not fully understood. Citrus dehydrin, which accumulates mainly in response to cold stress, enhances cold tolerance in transg...

Alternative Titles

Full title

Metal binding by citrus dehydrin with histidine-rich domains

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_235006218

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_235006218

Other Identifiers

ISSN

0022-0957

E-ISSN

1460-2431

DOI

10.1093/jxb/eri262

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