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Modeling and structural analysis of PA clan serine proteasesCombinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin FoldA Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional SpecializationTma108, a putative M1 aminopeptidase, is a specific nascent chain-associated protein in Saccharomyces cerevisiae.Exported Epoxide Hydrolases Modulate Erythrocyte Vasoactive Lipids during Plasmodium falciparum InfectionAnimal-microbe interactions and the evolution of nervous systemsInsights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies.Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.The threonine protease activity of testes-specific protease 50 (TSP50) is essential for its function in cell proliferation.An atypical proprotein convertase in Giardia lamblia differentiation.A computational module assembled from different protease family motifs identifies PI PLC from Bacillus cereus as a putative prolyl peptidase with a serine protease scaffoldKinetics and magnitude of antibody responses against the conserved 47-kilodalton antigen and the variable 56-kilodalton antigen in scrub typhus patientsThe venom gland transcriptome of the parasitoid wasp Nasonia vitripennis highlights the importance of novel genes in venom functionInterspecies comparison of peptide substrate reporter metabolism using compartment-based modeling.Three-Dimensional Molecular Modeling of a Diverse Range of SC Clan Serine Proteases.Next Generation Sequencing Identifies Five Major Classes of Potentially Therapeutic Enzymes Secreted by Lucilia sericata Medical MaggotsSerine proteases.Sol narae (Sona) is a Drosophila ADAMTS involved in Wg signalingDifferent Culture Metabolites of the Red Sea Fungus Fusarium equiseti Optimize the Inhibition of Hepatitis C Virus NS3/4A Protease (HCV PR).Proteases as therapeutics.Microbial and fungal protease inhibitors--current and potential applications.Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.Getting intimate with trypsin, the leading protease in proteomics.Fungal lifestyle reflected in serine protease repertoire.A receptor dependent-4D QSAR approach to predict the activity of mutated enzymes.Insights into the Cyanobacterial Deg/HtrA ProteasesThrombin a-chain: activation remnant or allosteric effector?Proteolytic activity in the meibomian gland: Implications to health and disease.Proteolytic Activities Expressed by Gastrointestinal Pathogens Bacillus cereus, Listeria monocytogenes and Enterococcus faecium in Different Growth Phases.Engineering trypsin for inhibitor resistance.The Serine Protease Pic From Enteroaggregative Escherichia coli Mediates Immune Evasion by the Direct Cleavage of Complement Proteins.Two cap residues in the S1 subsite of a Plasmodium falciparum M1-family aminopeptidase promote broad specificity and enhance catalysis.Quantitative and Comparative Profiling of Protease Substrates through a Genetically Encoded Multifunctional Photocrosslinker.Ahp cyclodepsipeptides: the impact of the Ahp residue on the "canonical inhibition" of S1 serine proteases.Proteomics of Nasonia vitripennis and the effects of native Wolbachia infection on N. vitripennis.Matrix Proteases and the DegradomeFunction of Serine Protease HtrA in the Lifecycle of the Foodborne Pathogen
P2860
Q21199586-479F3B32-59E5-4756-B009-DB38E1B56FF0Q27660588-02FED441-FE5E-49E9-B6BC-F5185DF849C7Q27679264-184FCB95-466B-4F16-9FA7-56EF15491E5AQ27934303-B4165FDA-841B-422D-B869-C103E538CF46Q27974556-B58320BF-43BC-4344-A404-A0A056340D08Q28603831-FBFC9B62-F8C4-4A2C-98A2-775B6C2877EFQ33532266-DFBF3EED-FCD1-48CA-A8D6-B28ACB8C370EQ34023640-18ABCD79-5546-40EC-8360-FE96A51147EBQ34264487-CB1B571D-046C-4386-A433-CD10E796A618Q34477392-4D62BAF8-6222-4657-9258-3EB78EC7DF2CQ34936357-C97DABF0-0C64-48F2-8943-74AE97881F16Q35066475-7AD3FAC7-EF6D-4343-87E4-50CA22A6A0C2Q36098197-F5599ED5-C871-4ABA-9B9C-EBF2F8F1E88AQ36207414-463D49C6-0C22-4C20-AF78-0EDFDB84914FQ36425467-C34F8BB3-EF2B-42A6-B834-98BFFC375CF8Q36784772-95F87A12-8BDA-4034-BACE-90087C240742Q37175533-56676816-12C3-4499-A094-C27840F7A86EQ37184855-F347D1E9-3515-449F-990F-C632182871E5Q37370644-117CBAFA-89C9-47D3-92B8-2AA471965170Q37853216-895EE1D2-A9CE-4666-9EF1-81149011F95BQ37973268-13A4A955-080E-4560-9425-725C137E0AA4Q38027076-BB0046D6-C317-4DE3-8469-6B3DDEA2C3D9Q38115212-C05C2565-6BD2-4191-BCC3-72652F8A9972Q38613280-089A3F8E-F6E5-443E-BA7D-BB45ED0C69EEQ38663511-FC651B24-9603-4DC5-8691-C9109782B305Q38851276-A2695229-9CDC-4CFB-A832-50D3DA060AC7Q38989460-9233FAC8-71B4-4129-8928-B08179BF98D6Q39174470-B6972647-52C0-4A99-A8D0-C07618A86248Q40196616-3B915968-0E01-4209-BA15-4A7B64B6CAE1Q40803596-1B5FEB6C-36C2-4A96-A66A-EF1D448296CAQ41547882-71630A63-6371-4D1C-B1A0-65722E3B192DQ45065398-DF84A16C-A3F2-454B-829B-24F46B92F760Q47643783-4C47B732-74F4-4515-A81A-33B00E3C6B99Q50883904-349DEB5E-CEBB-46C2-B05C-EB42E631D8F0Q55208812-60A8EA57-C877-4ACD-B473-B3FA3E449A46Q57082617-C11B0C96-77B4-4F91-988C-07EADC0FFF41Q57824808-A650DDF8-5972-432C-A9AA-9EEADA499D8A
P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Evolution of peptidase diversity.
@en
type
label
Evolution of peptidase diversity.
@en
prefLabel
Evolution of peptidase diversity.
@en
P2860
P356
P1476
Evolution of peptidase diversity.
@en
P2093
Enrico Di Cera
Michael J Page
P2860
P304
30010-30014
P356
10.1074/JBC.M804650200
P407
P577
2008-09-03T00:00:00Z