A homolog of ribulose bisphosphate carboxylase/oxygenase-binding protein in Chromatium vinosum
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. The most abundant protein in the world
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3. The Rubisco large subunit binding protein
4. Isolation of L8 and L8S8 forms of ribulose bisphosphate carboxylase/oxygenase from Chromatium vinosum
5. The nature of L8 and L8S8 forms of ribulose bisphosphate carboxylase/oxygenase from Chromatium vinosum
Cited by 19 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. [12] Chaperonin 6014 and co-chaperonin 107 from Chromatium vinosum;Methods in Enzymology;1998
2. Mutations in a sequence near the N-terminus of the small subunit alter the CO2/O-2 specificity factor for ribulose bisphosphate carboxylase/oxygenase;Photosynthesis Research;1997
3. Chaperonins of Photosynthetic Organisms;The Chaperonins;1996
4. Chaperonin-Repairable Subtle Incompleteness of Protein Assembly Induced by a Substitution of Hydrogen with Deuterium: Effect of GroE on Deuterated Ribulose 1,5-Bisphosphate Carboxylase;Plant and Cell Physiology;1995-04
5. Presence of Chromatium vinosum chaperonins 10 and 60 in mitochondria and peroxisomes of rat hepatocytes;Biology of the Cell;1995
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