Microbiology: loading the type III cannon

scientific article published in October 2005

Microbiology: loading the type III cannon is …
instance of (P31):
scholarly articleQ13442814

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P6179Dimensions Publication ID1034550470
P356DOI10.1038/437821A
P698PubMed publication ID16208351

P50authorOlaf SchneewindQ64624932
P2093author name stringBill Blaylock
P2860cites workStructural insights into the assembly of the type III secretion needle complex.Q24547949
Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretionQ27635933
Chaperone release and unfolding of substrates in type III secretionQ28275782
Sculpting the proteome with AAA(+) proteases and disassembly machines.Q35904074
Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein exportQ37095412
Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of EnteropathogenicEscherichia coliQ40173948
Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerizationQ42440794
Interactions among components of the Salmonella flagellar export apparatus and its substratesQ42484827
FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activityQ50119364
P433issue7060
P407language of work or nameEnglishQ1860
P304page(s)821
P577publication date2005-10-01
P1433published inNatureQ180445
P1476titleMicrobiology: loading the type III cannon
P478volume437

Reverse relations

Q90259043Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase From Shigella flexnericites workP2860

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