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Chaperone-like properties of tobacco plastid thioredoxins f and m

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Chaperone-like properties of tobacco plastid thioredoxins f and m

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Sanz-Barrio, R.; Fernández-San Millán, A.; Carballeda, J.; Corral Martínez, P.; Seguí-Simarro, JM.; Farran, I. (2012). Chaperone-like properties of tobacco plastid thioredoxins f and m. Journal of Experimental Botany. 63(1):365-379. doi:10.1093/jxb/err282

Por favor, use este identificador para citar o enlazar este ítem: http://hdl.handle.net/10251/63108

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Title: Chaperone-like properties of tobacco plastid thioredoxins f and m
Author:
UPV Unit: Universitat Politècnica de València. Instituto Universitario de Conservación y Mejora de la Agrodiversidad Valenciana - Institut Universitari de Conservació i Millora de l'Agrodiversitat Valenciana
Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia
Issued date:
Abstract:
Thioredoxins (Trxs) are ubiquitous disulphide reductases that play important roles in the redox regulation of many cellular processes. However, some redox-independent functions, such as chaperone activity, have also been ...[+]
Subjects: Chaperone , Folding , Oligomerization , Plastid , Thioredoxin , Tobacco , Complementary DNA , Primer DNA , Amino acid sequence , Article , Chemical structure , Genetics , Molecular genetics , Nucleotide sequence , Physiology , Polymerase chain reaction , Sequence homology , Base Sequence , Chloroplast Thioredoxins , DNA Primers , DNA, Complementary , Models, Molecular , Molecular Chaperones , Molecular Sequence Data , Plastids , Sequence Homology, Amino Acid , Nicotiana tabacum
Copyrigths: Reconocimiento - No comercial (by-nc)
Source:
Journal of Experimental Botany. (issn: 0022-0957 )
DOI: 10.1093/jxb/err282
Publisher:
Oxford University Press (OUP): Policy B - Oxford Open Option A
Publisher version: http://dx.doi.org/10.1093/jxb/err282
Thanks:
The authors appreciate the assistance of Dr Santiago Mora (Instituto Leloir, Argentine) for his collaboration in the first steps of Trxs cDNA isolation. We gratefully acknowledge the provision of the FBPase enzyme by the ...[+]
Type: Artículo

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