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Q34552800-C10AB2C2-1505-46E3-940C-B1E8FAACC4F2
Q34552800-C10AB2C2-1505-46E3-940C-B1E8FAACC4F2
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http://www.wikidata.org/entity/statement/Q34552800-C10AB2C2-1505-46E3-940C-B1E8FAACC4F2
trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.
P2860
Q34552800-C10AB2C2-1505-46E3-940C-B1E8FAACC4F2
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34552800-C10AB2C2-1505-46E3-940C-B1E8FAACC4F2
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wasDerivedFrom
3a81d0185c11796b75a20fda668e21a6580cbd3b
P2860
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.