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References from Sequence comparison, molecular modeling, and network analysis predict structural diversity in cysteine proteases from the Cape sundew, Drosera capensis. Local targets link to admitted publications; unresolved targets remain external evidence.
In situ enzyme activity in the dissolved and particulate fraction of the fluid from four pitcher plant species of the genus Nepenthes
10.1371/journal.pone.0025144 · 2011 · External reference
10.1093/aob/mcq238
10.1093/aob/mcq238 · External reference
Physical and chemical properties of the mucin secreted by Drosera capensis
10.1016/s0031-9422(00)88783-x · 1977 · External reference
Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco
10.1007/s004250100665 · 2002 · External reference
Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases
10.1042/bj20031575 · 2004 · External reference
Nepenthesin, a unique member of a novel subfamily of aspartic proteinases: enzymatic and structural characteristics
10.2174/138920305774933259 · 2005 · External reference
Gastrointestinal absorption and biological activities of serine and cysteine proteases of animal and plant origin: review on absorption of serine and cysteine proteases
2012 · External reference
10.1371/journal.pone.0130556
10.1371/journal.pone.0130556 · External reference
10.1093/nar/gkt953
10.1093/nar/gkt953 · External reference
Papain-like peptidases: structure, function, and evolution
10.1515/bmc-2012-0054 · 2013 · External reference
10.1016/j.bbapap.2011.10.002
10.1016/j.bbapap.2011.10.002 · External reference
10.1104/pp.110.158030
10.1104/pp.110.158030 · External reference
Nepenthesin protease activity indicates digestive fluid dynamics in carnivorous Nepenthes plants
10.1371/journal.pone.0118853 · 2015 · External reference
10.1371/journal.pone.0104424
10.1371/journal.pone.0104424 · External reference
A carnivorous sundew plant prefers protein over chitin as a source of nitrogen from its traps
10.1016/j.plaphy.2016.03.008 · 2016 · External reference
10.1093/jxb/ern179
10.1093/jxb/ern179 · External reference
Jasmonates trigger prey-induced formation of outer stomach in carnivorous sundew plants
10.1098/rspb.2013.0228 · 2013 · External reference
Novel proteases from the genome of the carnivorous plant Drosera capensis: Structural prediction and comparative analysis
2016 · External reference
Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria
10.1111/j.1742-4658.2007.06211.x · 2008 · External reference
The 2.0 åcrystal structure and substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm
10.1016/j.jmb.2003.12.075 · 2004 · External reference
10.1074/jbc.m115.672550
10.1074/jbc.m115.672550 · External reference
10.1093/nar/gkh468
10.1093/nar/gkh468 · External reference
10.1002/prot.22540
10.1002/prot.22540 · External reference
Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
10.1038/msb.2011.75 · 2011 · External reference
10.1038/nmeth.1701
10.1038/nmeth.1701 · External reference
10.1038/nprot.2007.131
10.1038/nprot.2007.131 · External reference
10.1002/jcc.20289
10.1002/jcc.20289 · External reference
10.1021/jp973084f
10.1021/jp973084f · External reference
10.1002/jcc.20065
10.1002/jcc.20065 · External reference
10.1063/1.445869
10.1063/1.445869 · External reference
10.1006/jmbi.1998.2401
10.1006/jmbi.1998.2401 · External reference
A chemical group graph representation for efficient high-throughput analysis of atomistic protein simulations
10.1142/s0219720012500084 · 2012 · External reference
10.1016/0263-7855(96)00018-5
10.1016/0263-7855(96)00018-5 · External reference
10.18637/jss.v024.i01
10.18637/jss.v024.i01 · External reference
Network: a package for managing relational data in R
10.18637/jss.v024.i02 · 2008 · External reference
Unresolved reference
2015 · External reference
Some simple algorithms for structural comparison
10.1007/s10588-005-5586-6 · 2005 · External reference
Social network analysis with sna
10.18637/jss.v024.i06 · 2008 · External reference
MAKER-P: a tool-kit for the rapid creation, management, and quality control of plant genome annotations
10.1104/pp.113.230144 · 2013 · External reference
10.1093/nar/gki442
10.1093/nar/gki442 · External reference
10.1016/j.phytochem.2003.09.005
10.1016/j.phytochem.2003.09.005 · External reference
Protease gene families in Populus and Arabidopsis
10.1186/1471-2229-6-30 · 2006 · External reference
Cysteine protease and cystatin expression and activity during soybean nodule development and senescence
10.1186/s12870-014-0294-3 · 2014 · External reference
10.1104/pp.112.194001
10.1104/pp.112.194001 · External reference
Hierarchical clustering via joint between-within distances: Extending Ward's minimum variance method
10.1007/s00357-005-0012-9 · 2005 · External reference
10.1074/jbc.270.28.16645
10.1074/jbc.270.28.16645 · External reference
Modification of the electrostatic environment is tolerated in the oxyanion hole of the cysteine protease papain
10.1021/bi00002a010 · 1995 · External reference
Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale
10.1046/j.1432-1327.2000.01152.x · 2000 · External reference
The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases
10.1016/s0014-5793(98)01018-7 · 1998 · External reference
Prodomain peptide of HGCP-Iv cysteine proteinase inhibits nematode cysteine proteinases
2004 · External reference
Inhibitory properties of cysteine protease pro-peptides from barley confer resistance to spider mite feeding
10.1371/journal.pone.0128323 · 2015 · External reference
Protective effects of a cysteine proteinase propeptide expressed in transgenic soybean roots
10.1016/j.peptides.2009.01.022 · 2009 · External reference
Altered host plant preference of Tetranychus urticae and prey preference of its predator Phytoseiulus persimilis (Acari: Tetranychidae, Phytoseiidae) on transgenic Cry3Bb-eggplants
10.1016/j.biocontrol.2005.03.017 · 2005 · External reference
Two distinct gene subfamilies within the family of cysteine protease genes
10.1073/pnas.90.7.3063 · 1993 · External reference
Cathepsin H functions as an aminopeptidase in secretory vesicles for production of enkephalin and galanin peptide neurotransmitters
10.1111/j.1471-4159.2012.07788.x · 2012 · External reference
Purification and characterization of Aleurain 1: a plant thiol protease functionally homologous to mammalian Cathepsin H
10.1104/pp.99.3.848 · 1992 · External reference
10.1006/bbrc.1999.0461
10.1006/bbrc.1999.0461 · External reference
The digestive fluid of drosera indica contains a cysteine endopeptidase (“droserain”) similar to dionain from Dionaea muscipula
10.55360/cpn414.kt962 · 2012 · External reference
Analysis of a truncated form of cathepsin h in human prostate tumor cells
10.1074/jbc.m109557200 · 2002 · External reference
10.1074/jbc.m112.436394
10.1074/jbc.m112.436394 · External reference
Crystal structure of porcine cathepsin H determined at 2.1Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
10.1016/s0969-2126(98)00007-0 · 1998 · External reference
Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidaseh: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase
10.1515/bc.2003.149 · 2003 · External reference
10.1016/j.pbi.2014.09.003
10.1016/j.pbi.2014.09.003 · External reference
10.1146/annurev-arplant-043014-115547
10.1146/annurev-arplant-043014-115547 · External reference
10.1016/s0981-9428(02)01404-3
10.1016/s0981-9428(02)01404-3 · External reference
10.1105/tpc.111.084095
10.1105/tpc.111.084095 · External reference
Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP)
10.1016/0014-5793(94)00809-4 · 1994 · External reference
10.1371/journal.pone.0029317
10.1371/journal.pone.0029317 · External reference
A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis
10.1093/pcp/pce144 · 2001 · External reference
A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves
10.1104/pp.010551 · 2001 · External reference
10.1371/journal.pone.0032422
10.1371/journal.pone.0032422 · External reference
Granulins: the structure and function of an emerging family of growth factors
10.1677/joe.0.1580145 · 1998 · External reference
10.1021/cr3003533
10.1021/cr3003533 · External reference
10.1021/ja9542193
10.1021/ja9542193 · External reference
The value of using multiple proteases for large-scale mass spectrometry-based proteomics
10.1021/pr900863u · 2010 · External reference
Decision tree-driven tandem mass spectrometry for shotgun proteomics
10.1038/nmeth.1260 · 2008 · External reference
10.1021/ac9004309
10.1021/ac9004309 · External reference
10.1007/s00018-003-2287-5
10.1007/s00018-003-2287-5 · External reference
Detection and quantitation of succinimide in intact protein via hydrazine trapping and chemical derivatizationuantitation of succinimide in intact protein via hydrazine trapping and chemical derivatization
10.1002/jps.24074 · 2014 · External reference
Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: consequences for MALDI and HPLC-MALDI analysis
10.1021/ac061017o · 2006 · External reference
Determination of deamidation artifacts introduced by sample preparation using 18O-labeling and tandem mass spectrometry analysis
2012 · External reference
Evaluation of the effect of trypsin digestion buffers on artificial deamidation
2015 · External reference
Neighboring side chain effects on asparaginyl and aspartyl degradation: an ab initio study of the relationship between peptide conformation and backbone NH acidity
10.1021/ja0026814 · 2001 · External reference
10.1016/j.bbagen.2009.05.008
10.1016/j.bbagen.2009.05.008 · External reference
10.1016/j.pbiomolbio.2014.02.004
10.1016/j.pbiomolbio.2014.02.004 · External reference
Chemical deamidation: a common pitfall in large-scale N-linked glycoproteomic mass spectrometry-based analyses
10.1021/pr2011268 · 2012 · External reference
Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease GluC at pH4.5
10.1007/s00726-015-2166-z · 2016 · External reference
10.1002/jms.1609
10.1002/jms.1609 · External reference
Interpretation of pH–activity profiles for acid–base catalysis from molecular simulations
10.1021/bi5012833 · 2015 · External reference
