Structural and Kinetic Investigations on the 15−21 and 42−45 Loops of Muscle Acylphosphatase: Evidence for Their Involvement in Enzyme Catalysis and Conformational Stabilization-Reference-Cited by-同舟云学术

Structural and Kinetic Investigations on the 15−21 and 42−45 Loops of Muscle Acylphosphatase: Evidence for Their Involvement in Enzyme Catalysis and Conformational Stabilization

Published:1997-06-01 Issue:23 Volume:36 Page:7217-7224
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Taddei Niccolò¹,Chiti Fabrizio¹,Magherini Francesca¹,Stefani Massimo¹,Thunnissen Marjolein M. G. M.¹,Nordlund Pär¹,Ramponi Giampietro¹

Affiliation:

1. Department of Biochemical Sciences, University of Florence, Florence, Italy, and Department of Molecular Biology, University of Stockholm, Stockholm, Sweden

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi970173%2B

Reference53 articles.

1. Effect of exogenously added acylphosphatases on inositol lipid metabolism in human platelets

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