Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
about
Human mesotrypsin is a unique digestive protease specialized for the degradation of trypsin inhibitorsStructural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsinFunctional and Structural Roles of the Cys14–Cys38 Disulfide of Bovine Pancreatic Trypsin InhibitorMutant N143P Reveals How Na+ Activates ThrombinDeterminants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with MesotrypsinThe P 2 ′ residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activityPresence versus absence of hydrogen bond donor Tyr-39 influences interactions of cationic trypsin and mesotrypsin with protein protease inhibitorsSpecificity profiling of seven human tissue kallikreins reveals individual subsite preferencesSequence and conformational specificity in substrate recognition: several human Kunitz protease inhibitor domains are specific substrates of mesotrypsin.Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors as SubstratesHuman mesotrypsin exhibits restricted S1' subsite specificity with a strong preference for small polar side chainsThe amyloid precursor protein/protease nexin 2 Kunitz inhibitor domain is a highly specific substrate of mesotrypsin.PRSS3 is a prognostic marker in invasive ductal carcinoma of the breast.Small molecule inhibitors of mesotrypsin from a structure-based docking screen.Functional role of residue 193 (chymotrypsin numbering) in serine proteases: influence of side chain length and beta-branching on the catalytic activity of blood coagulation factor XIa.Mesotrypsin promotes malignant growth of breast cancer cells through shedding of CD109Molecular basis for the resistance of an insect chymotrypsin to a potato type II proteinase inhibitorNeurobiology of butyrylcholinesterase.Design of a high fragment efficiency library by molecular graph theoryMesotrypsin Signature Mutation in a Chymotrypsin C (CTRC) Variant Associated with Chronic Pancreatitis.Combinatorial protein engineering of proteolytically resistant mesotrypsin inhibitors as candidates for cancer therapyHuman mesotrypsin defies natural trypsin inhibitors: from passive resistance to active destruction.PRSS3/mesotrypsin is a therapeutic target for metastatic prostate cancerBiochemical and structural insights into mesotrypsin: an unusual human trypsin.Mass spectrometric detection of tyrosine sulfation in human pancreatic trypsinogens, but not in tumor-associated trypsinogen.Activity of recombinant trypsin isoforms on human proteinase-activated receptors (PAR): mesotrypsin cannot activate epithelial PAR-1, -2, but weakly activates brain PAR-1.Genetic and biochemical characterization of the E32del polymorphism in human mesotrypsinogen.Purification and characterization of cocoonase from the silkworm Bombyx mori.Alginate as a protease inhibitor in vitro and in a model gut system; selective inhibition of pepsin but not trypsin.Identification of novel peptide inhibitors for human trypsins.Trypsin IV, a novel agonist of protease-activated receptors 2 and 4.Structural role of Gly(193) in serine proteases: investigations of a G555E (GLY193 in chymotrypsin) mutant of blood coagulation factor XI.Severe factor XI deficiency caused by a Gly555 to Glu mutation (factor XI-Glu555): a cross-reactive material positive variant defective in factor IX activation.Thermodynamic analysis reveals structural rearrangement during the acylation step in human trypsin 4 on 4-methylumbelliferyl 4-guanidinobenzoate substrate analogue.Unconventional translation initiation of human trypsinogen 4 at a CUG codon with an N-terminal leucine. A possible means to regulate gene expression.Mesotrypsin, a brain trypsin, activates selectively proteinase-activated receptor-1, but not proteinase-activated receptor-2, in rat astrocytes.Pre-equilibrium competitive library screening for tuning inhibitor association rate and specificity toward serine proteases.Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4.Mapping protein selectivity landscapes using multi-target selective screening and next-generation sequencing of combinatorial libraries
P2860
Q24295201-9AFC400F-4108-4093-9C87-04CDB331E8BCQ27649308-F118568E-F8DB-4A4A-B7B4-35ED920F0FEDQ27651502-BC530913-DAAC-4C95-874D-B5B9B084A7C3Q27657884-D0F5467F-DE84-455E-9014-D65BEC61081BQ27664637-E4B6318F-DE78-4B14-B31D-44E1E0B43082Q27671330-30BF9537-5E45-4F50-B4BA-E3E98B6924D5Q27679201-47FF7534-3B84-4AD9-8591-BD772DD30E1DQ28243373-DA451DF1-70D4-48F7-A2BE-EF2B01DCF215Q30367678-853A84C8-CC68-4D47-87C0-ECA30337D320Q30376720-B287EBCC-94C3-4B8B-B167-A113E07C6D3CQ33246025-846AB611-13A0-4271-BE57-AA1A8F855B28Q33581987-C58C80C3-FF5D-4481-A5E8-FDFC4679D03CQ33591558-CD68B1DA-8F42-4E95-AA23-B5D56CF2F77FQ33626452-F2413563-0DCD-4C4F-B7FE-B4E879C30045Q33912334-D873E0FB-DF52-4875-BA90-18A53DE38307Q34088459-DB634834-636E-4752-B50C-D7BCEEE5EA8FQ34093579-4CFD4843-9EB0-42F5-B3FA-FD3AD19721A5Q35058510-9375BC67-6311-4283-BF89-B8EE5C106137Q35181886-EBAFDF44-BEA3-49A4-A711-9FE90E4B93F5Q35837145-AE86BB7E-E185-4FA4-84A8-B619C2DCB100Q35950487-A7B57495-3636-48BF-9B95-0E5D668392A1Q36200333-A14C9A24-5607-47FF-82D4-30634B0FBE1EQ36493144-272A5181-8D01-4F59-A7AB-77603EB7C6C6Q37180025-AF6241C7-B521-4DA7-A754-1DD1012651FEQ40036264-70D5BB33-72C0-45FA-A18C-685E05CAE7C1Q40360819-16300D62-8EAF-4216-8EA5-5034909A4C2DQ41966158-7CFBB4C0-1495-4247-A066-6EB9F6AEEFC7Q42002518-A92C9640-803A-418C-959D-89CA5412207DQ42562212-FEBB5556-D0CD-4325-8E20-F45EF6E9DA56Q43175517-12644F39-BE80-4F0A-BE13-3CD6005ACB45Q44730652-910B5F53-D776-4AF6-A70E-0AD078B4A175Q44848234-97B08E57-0898-4ACF-9781-DFF25E5B9096Q45084612-D9D7466B-9F1B-486B-A4BB-5680EF9A5D83Q46955951-C351BA8E-A9A6-4835-91C8-0EE196856DC7Q48178704-0BD43FC0-6CAF-4168-B238-41BED62ED04EQ48449125-6AC6FA46-1F65-41F5-A572-C497BDC794C1Q52657347-20071064-C4D7-4EAE-9562-7B0C503BB08DQ53640728-72EF5721-D760-4B50-BA23-2B831BBDBC46Q58695396-F8A433FF-9499-4E84-8193-2529A6FADD85
P2860
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@ast
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@en
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@nl
type
label
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@ast
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@en
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@nl
prefLabel
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@ast
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@en
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@nl
P2093
P921
P356
P1476
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
@en
P2093
Gunnar I Berglund
Janos Hajdu
László Gráf
László Szilágyi
P304
P356
10.1006/JMBI.2001.5305
P407
P577
2002-02-01T00:00:00Z