Oligomeric Aip2p/Dld2p forms a novel grapple-like structure and has an ATP-dependent F-actin conformation modifying activity in vitro
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
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1. Closing the gap: yeast electron‐transferring flavoprotein links the oxidation of d ‐lactate and d ‐α‐hydroxyglutarate to energy production via the respiratory chain;The FEBS Journal;2019-05-25
2. Existence of Unprocessed a Mitochondrial Enzyme: YDL178wp in the Membrane Fraction as an Oligomeric Formation with a Protein-Unfolding Activity;MOJ Cell Science & Report;2017-04-06
3. Investigation of Laser‐Microdissected Inclusion Bodies;Methods in Cell Biology;2007
4. More than a 100-fold increase in immunoblot signals of laser-microdissected inclusion bodies with an excessive aggregation property by oligomeric actin interacting protein 2/d-lactate dehydrogenase protein 2;Analytical Biochemistry;2005-12
5. Oligomeric Aip2p/Dld2p modifies the protein conformation of both properly folded and misfolded substrates in vitro;Biochemical and Biophysical Research Communications;2004-10
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