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1
Q41098204-DFAED1E9-6055-4A4D-BA8B-FA096533DDAA
Q41098204-DFAED1E9-6055-4A4D-BA8B-FA096533DDAA
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http://www.wikidata.org/entity/statement/Q41098204-DFAED1E9-6055-4A4D-BA8B-FA096533DDAA
Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.
P2860
Q41098204-DFAED1E9-6055-4A4D-BA8B-FA096533DDAA
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41098204-DFAED1E9-6055-4A4D-BA8B-FA096533DDAA
rank
NormalRank
type
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Statement
wasDerivedFrom
35b6dcc237aaedea6e0ffeea128a725379a90bde
P2860
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.