Pages that link to "Q35763213"
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The following pages link to Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease (Q35763213):
Displaying 15 items.
- Activation of the epithelial sodium channel (ENaC) by the alkaline protease from Pseudomonas aeruginosa (Q28492964) (← links)
- Interdomain Contacts and the Stability of Serralysin Protease from Serratia marcescens (Q28548135) (← links)
- Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease (Q34379678) (← links)
- Regulation of ABCC6 trafficking and stability by a conserved C-terminal PDZ-like sequence (Q35170848) (← links)
- Modulation of the epithelial sodium channel (ENaC) by bacterial metalloproteases and protease inhibitors (Q35194638) (← links)
- Identification of SlpB, a Cytotoxic Protease from Serratia marcescens (Q35745546) (← links)
- Proteases, cystic fibrosis and the epithelial sodium channel (ENaC). (Q38021378) (← links)
- SlpE is a calcium-dependent cytotoxic metalloprotease associated with clinical isolates of Serratia marcescens (Q38709348) (← links)
- Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications. (Q41669187) (← links)
- Draft genome sequence of Pseudomonas sp. strain M47T1, carried by Bursaphelenchus xylophilus isolated from Pinus pinaster (Q42268893) (← links)
- Serralysin family metalloproteases protects Serratia marcescens from predation by the predatory bacteria Micavibrio aeruginosavorus (Q58719792) (← links)
- Calcium-Dependent RTX Domains in the Development of Protein Hydrogels (Q64105042) (← links)
- Receptor-Based Peptides for Inhibition of Leukotoxin Activity (Q88615459) (← links)
- Calcium-Induced Activity and Folding of a Repeat in Toxin Lipase from Antarctic Pseudomonas fluorescens Strain AMS8 (Q92447056) (← links)
- Enhanced catalytic activity of Bacillus aryabhattai P1 protease by modulation with nanoactivator (Q96305100) (← links)