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The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers.
Koonin EV, Makarova KS, Rogozin IB, Davidovic L, Letellier MC, Pellegrini L
Genome Biol
2003,
4
:R19
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PubMed Central articles that cite the above article:
1.
Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.
Lemberg MK, Menendez J, Misik A, Garcia M, Koth CM, Freeman M
EMBO J
2005 Feb 9,
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A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma.
Brossier F, Jewett TJ, Sibley LD, Urban S
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2005 Mar 15,
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Structural basis for intramembrane proteolysis by rhomboid serine proteases.
Ben-Shem A, Fass D, Bibi E
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2007 Jan 9,
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Open-cap conformation of intramembrane protease GlpG.
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Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.
Baker RP, Young K, Feng L, Shi Y, Urban S
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Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases.
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Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite.
O'Donnell RA, Hackett F, Howell SA, Treeck M, Struck N, Krnajski Z, Withers-Martinez C, Gilberger TW, Blackman MJ
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Site-2 protease regulated intramembrane proteolysis: sequence homologs suggest an ancient signaling cascade.
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