WordNet

the hydrolysis of proteins into peptides and amino acids by cleavage of their peptide bonds
of or relating to proteolysis

English Journal

Selective Removal of FG Repeat Domains from the Nuclear Pore Complex by Enterovirus 2Apro.

Park N1, Schweers NJ1, Gustin KE2.
Journal of virology.J Virol.2015 Nov 1;89(21):11069-79. doi: 10.1128/JVI.00956-15. Epub 2015 Aug 26.
Enteroviruses proteolyze nuclear pore complex (NPC) proteins (Nups) during infection, leading to disruption of host nuclear transport pathways and alterations in nuclear permeability. To better understand how enteroviruses exert these effects on nuclear transport, the mechanisms and consequences of
PMID 26311873

High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune TTP syndrome.

Casina VC1, Hu W2, Mao JH1, Lu RN1, Hanby HA1, Pickens B1, Kan ZY3, Lim WK4, Mayne L3, Ostertag EM1, Kacir S1, Siegel DL1, Englander SW2, Zheng XL5.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Aug 4;112(31):9620-5. doi: 10.1073/pnas.1512561112. Epub 2015 Jul 22.
Acquired thrombotic thrombocytopenic purpura (TTP), a thrombotic disorder that is fatal in almost all cases if not treated promptly, is primarily caused by IgG-type autoantibodies that inhibit the ability of the ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member
PMID 26203127

Proteolysis of virulence regulator ToxR is associated with entry of Vibrio cholerae into a dormant state.

Almagro-Moreno S1, Kim TK1, Skorupski K1, Taylor RK1.
PLoS genetics.PLoS Genet.2015 Apr 7;11(4):e1005145. doi: 10.1371/journal.pgen.1005145. eCollection 2015.
Vibrio cholerae O1 is a natural inhabitant of aquatic environments and causes the diarrheal disease, cholera. Two of its primary virulence regulators, TcpP and ToxR, are localized in the inner membrane. TcpP is encoded on the Vibrio Pathogenicity Island (VPI), a horizontally acquired mobile genetic
PMID 25849031

Heterogeneous Nuclear Ribonucleoprotein K Interacts with and Is Proteolyzed by Calpain in vivo(Biochemistry & Molecular Biology)

Kimura Eiichi,Abe Keiko,Suzuki Koichi [他],SORIMACHI Hiroyuki
Bioscience, biotechnology, and biochemistry 67(8), 1786-1796, 2003-08-23
… Now, hnRNP K is considered to function as a scaffold protein for its binding proteins, such as PKCδ and C/EBPβ, which were reported to be calpain substrates, suggesting that hnRNP-K is a scaffold for calpain to proteolyze these proteins. …
NAID 110002694302