Kinetic study on the dimer-tetramer interconversion of phosphorylase b by a stopped-flow X-ray scattering method-Reference-Cited by-同舟云学术

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Kinetic study on the dimer-tetramer interconversion of phosphorylase b by a stopped-flow X-ray scattering method

Published:1989-05 Issue:2 Volume:33 Page:153-160
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Wang Zhi-Xin,Tsuruta Hirotsugu,Honda Yoko,Tachi-iri Yoshiaki,Wakabayashi Katsuzo,Amemiya Yoshiyuki,Kihara Hiroshi

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference23 articles.

1. Calorimtric study of the interactions between phophorylase b and its nucleotide activators

2. AMP Analogs: Their Function in the Activation of Glycogen Phosphorylase b

3. Effect of temperature on the allosteric transitions of rabbit skeletal muscle phosphorylase b

Cited by 7 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. Structural NMR of protein oligomers using hybrid methods;Journal of Structural Biology;2011-03

2. Kinetic study on the dimer-tetramer interconvertion of glycogen  phosphorylase a;European Journal of Biochemistry;2001-12-25

3. Stopped-Flow Apparatus for X-ray Scattering and XAFS;Journal of Synchrotron Radiation;1994-10-01

4. The kinetics of conformational changes of α2-macroglobulin determined by time resolved X-ray solution scattering;FEBS Letters;1994-01-10

5. Dissociation of Limulus polyphemus (horseshoe crab) hemocyanin. II. Stopped-flow X-ray scattering study;Biophysical Chemistry;1992-05

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