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1. Full Text Cyclic Peptides Arising by Evolutionary Parallelism via Asparaginyl-Endopeptidase—Mediated Biosynthesis
by Joshua S. Mylne and Lai Yue Chan and Aurelie H. Chanson and Norelle L. Daly and Hanno Schaefer and Timothy L. Bailey and Philip Nguyencong and Laura Cascales and David J. Craik
The Plant Cell, ISSN 1040-4651, 7/2012, Volume 24, Issue 7, pp. 2765 - 2778
The cyclic miniprotein Momordica cochinchinensis Trypsin Inhibitor II (MCoTI-II) (34 amino acids) is a potent trypsin inhibitor (TI) and a favored scaffold for... 
Proteins | Polymerase chain reaction | Cyclic peptides | DNA | Squashes | Protein precursors | Amino acids | Biosynthesis | Open reading frames | Free energy | CIRCULAR PROTEINS | CYSTINE KNOT MOTIF | ARABIDOPSIS-THALIANA | BACKBONE CYCLIZATION | MOMORDICA-COCHINCHINENSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | VACUOLAR PROCESSING ENZYME | STRUCTURAL MOTIFS | INHIBITOR MCOTI-II | PLANT SCIENCES | CELL BIOLOGY | PLANT CYCLOTIDES | TRYPSIN-INHIBITOR | Cyclotides - chemistry | Cystine-Knot Miniproteins - metabolism | Molecular Sequence Data | Cystine-Knot Miniproteins - genetics | Phylogeny | Peptides, Cyclic - chemistry | Peptides, Cyclic - metabolism | Cysteine Endopeptidases - metabolism | Peptides, Cyclic - genetics | Cystine-Knot Miniproteins - chemistry | DNA, Plant - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Models, Molecular | Momordica - metabolism | Cyclotides - genetics | Arabidopsis - metabolism | Arabidopsis - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Gene Amplification | Cyclotides - metabolism | Momordica - genetics | Protein Conformation | Evolution, Molecular | Arabidopsis thaliana | Synthesis | Peptides | Plant genetics | Genetic aspects | Research | Observations
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2. Proteolytic enzymes
: serine and cysteine peptidases
by Barrett, Alan J
1994, Methods in enzymology, ISBN 0121821455, Volume 244., xxi, 765
Enzymes protéolytiques
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3. Full Text The role of KDEL-tailed cysteine endopeptidases of Arabidopsis (AtCEP2 and AtCEP1) in root development
by Höwing, Timo and Dann, Marcel and Müller, Benedikt and Helm, Michael and Scholz, Sebastian and Schneitz, Kay and Hammes, Ulrich Z and Gietl, Christine
PLoS ONE, ISSN 1932-6203, 12/2018, Volume 13, Issue 12, p. e0209407
Plants encode a unique group of papain-type cysteine endopeptidases (CysEP) characterized by a C-terminal KDEL endoplasmic reticulum retention signal... 
PROGRAMMED CELL-DEATH | LOCALIZATION | CASTOR BEAN ENDOSPERM | EXPRESSION ANALYSIS | MULTIDISCIPLINARY SCIENCES | GENES | RICINUS | MATURATION | RICINOSOMES | EMERGENCE | PROTEASE | Roots (Botany) | Research | Arabidopsis | Cell death | Proteases | Plant genetics | Enzymes | Cysteine | Seeds | Cell walls | Developmental biology | Papain | Epidermis | Glycoproteins | Biochemistry | Root development | Substrates | Proteins | Peptidases | Plant tissues | Substrate specificity | Emergence | Primordia | Trends | Plant sciences | Endoplasmic reticulum | Elongation | Food | Apoptosis
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4. Full Text IgG Endopeptidase in Highly Sensitized Patients Undergoing Transplantation
by Jordan, Stanley C and Lorant, Tomas and Choi, Jua and Kjellman, Christian and Winstedt, Lena and Bengtsson, Mats and Zhang, Xiaohai and Eich, Torsten and Toyoda, Mieko and Eriksson, Britt-Marie and Ge, Shili and Peng, Alice and Järnum, Sofia and Wood, Kathryn J and Lundgren, Torbjorn and Wennberg, Lars and Bäckman, Lars and Larsson, Erik and Villicana, Rafael and Kahwaji, Joe and Louie, Sabrina and Kang, Alexis and Haas, Mark and Nast, Cynthia and Vo, Ashley and Tufveson, Gunnar and Medicinska fakulteten and Medicinska och farmaceutiska vetenskapsområdet and Institutionen för immunologi, genetik och patologi and Klinisk och experimentell patologi and Klinisk immunologi and Infektionssjukdomar and Uppsala universitet and Institutionen för medicinska vetenskaper and Institutionen för kirurgiska vetenskaper and Transplantationskirurgi
The New England Journal of Medicine, ISSN 0028-4793, 08/2017, Volume 377, Issue 5, pp. 442 - 453
In this study, an IgG-degrading enzyme derived from Streptococcus pyogenes (IdeS) that cleaves human IgG into F(ab′) 2 and Fc fragments reduced or eliminated... 
SURVIVAL | MEDICINE, GENERAL & INTERNAL | ANTIBODY-MEDIATED REJECTION | KIDNEY-TRANSPLANTATION | INTRAVENOUS IMMUNOGLOBULIN | DESENSITIZATION | RITUXIMAB | IDES | RECIPIENTS | STAGE RENAL-DISEASE | HLA ANTIBODIES | Bacterial Proteins - adverse effects | Immunoglobulin G - blood | Histocompatibility Testing | Immunosuppression - methods | Complement C1q - immunology | Humans | Middle Aged | HLA Antigens - immunology | Male | Kidney Transplantation | Bacterial Proteins - therapeutic use | Cysteine Endopeptidases - adverse effects | Adult | Antibodies - blood | Cysteine Endopeptidases - therapeutic use | Female | Transplantation Immunology | Immunoglobulin G - metabolism | Transplantation of organs, tissues, etc | Immunoglobulin G | Research | Immunoglobulin M | Mycophenolic acid | Intravenous administration | Renal function | Glucocorticoids | Transplants & implants | Syngeneic grafts | Clinical trials | Cytotoxicity | Transplantation | Immunoglobulin A | Immunology | Immunoglobulins | Kidneys | Rituximab | Graft rejection | Studies | Pathology | Immunosuppression | Tacrolimus | Globulins | Perfusion | Endopeptidase | Histocompatibility antigen HLA | Kidney diseases | Mycophenolate mofetil | Kidney transplantation | Medical and Health Sciences | Medicin och hälsovetenskap
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5. Full Text Critical Role for Asparagine Endopeptidase in Endocytic Toll-like Receptor Signaling in Dendritic Cells
by Sepulveda, Fernando E and Maschalidi, Sophia and Colisson, Renaud and Heslop, Lea and Ghirelli, Cristina and Sakka, Emna and Lennon-Duménil, Ana-Maria and Amigorena, Sebastian and Cabanie, Lucien and Manoury, Bénédicte
Immunity, ISSN 1074-7613, 2009, Volume 31, Issue 5, pp. 737 - 748
Intracellular Toll-like receptor 3 (TLR3), TLR7, and TLR9 localize in endosomes and recognize single-stranded RNA and nucleotides from viruses and bacteria.... 
MOLIMMUNO | CELLIMMUNO | ACTIVATION | CATHEPSIN-L | CPG-DNA | MICE | TOLL-LIKE-RECEPTOR-9 | INVARIANT CHAIN | INHIBITORS | IMMUNOLOGY | EXPRESSION | ANTIGEN | Animals | Signal Transduction | Cathepsins - metabolism | Cysteine Endopeptidases - genetics | Dendritic Cells - immunology | Mice | Toll-Like Receptor 9 - metabolism | Cysteine Endopeptidases - physiology | Mice, Knockout | Asparagine | Cysteine | Nucleotides | Dendritic cells | RNA | Proteases | Proteins | Medical research | Mutagenesis | Molecular weight
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6. Full Text SUMO-specific proteases: a twist in the tail
by Hay, Ronald Thomas
Trends in Cell Biology, ISSN 0962-8924, 2007, Volume 17, Issue 8, pp. 370 - 376
The small ubiquitin-like modifier (SUMO) is involved in many cellular processes and is required for normal growth and development in all eukaryotes. Whereas... 
Pathology | TRANSCRIPTIONAL ACTIVITY | TOPOISOMERASE-II | DEPENDENT TRANSCRIPTION | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | NUCLEAR-PORE COMPLEX | AXIN-BINDING PROTEIN | BETA-CATENIN | SACCHAROMYCES-CEREVISIAE | DIFFERENTIAL REGULATION | CELL BIOLOGY | Endopeptidases - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Gene Expression Regulation | Ubiquitin - metabolism | Models, Molecular | Humans - classification | Phylogeny | Humans - genetics | Endopeptidases - chemistry | Cysteine Endopeptidases - metabolism | Endopeptidases - genetics | Protein Isoforms - metabolism | Cysteine Endopeptidases - genetics | Saccharomyces cerevisiae Proteins - metabolism | Endopeptidases - classification | Protein Conformation | Protein Processing, Post-Translational | Cysteine Endopeptidases - classification | Ubiquitin | Proteases | Sumo
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7. Full Text Aza-peptidyl michael acceptor and epoxide inhibitors - Potent and selective inhibitors of Schistosoma mansoni and Ixodes ricinus legumains (asparaginyl endopeptidases)
by Ovat, Asli and Muindi, Fanuel and Fagan, Crystal and Brouner, Michelle and Hansell, Elizabeth and Dvořák, Jan and Sojka, Daniel and Kopáček, Petr and McKerrow, James H and Caffrey, Conor R and Powers, James C
Journal of Medicinal Chemistry, ISSN 0022-2623, 11/2009, Volume 52, Issue 22, pp. 7192 - 7210
Aza-peptide Michael acceptors and epoxides with the general structure of YCO-Ala-Ala-AAsn-trans-CH=CHCOR and YCO-Ala-Ala-AAsn-EP-COR, respectively, are shown... 
NETWORK | DESIGN | CHEMISTRY, MEDICINAL | SPECIFICITY | CLONING | CASPASE-3 | MAMMALIAN LEGUMAIN | ISOCYANATES | IDENTIFICATION | EXPRESSION | CD CYSTEINE PROTEASES | Amino Acid Sequence | Oligopeptides - chemical synthesis | Schistosoma mansoni - enzymology | Oligopeptides - pharmacokinetics | Enzyme Inhibitors - pharmacology | Aza Compounds - chemistry | Biological Availability | Enzyme Inhibitors - chemical synthesis | Ixodes - enzymology | Animals | Cysteine Endopeptidases - metabolism | Enzyme Inhibitors - pharmacokinetics | Enzyme Inhibitors - chemistry | Epoxy Compounds - chemistry | Drug Design | Kinetics | Oligopeptides - pharmacology | Oligopeptides - chemistry
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8. Full Text Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
by Jackson, M.A and Gilding, E.K and Shafee, T and Harris, K.S and Kaas, Q and Poon, S and Yap, K and Jia, H and Guarino, R and Chan, L.Y and Durek, T and Anderson, M.A and Craik, D.J
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2411 - 12
Asparaginyl endopeptidases (AEPs) are proteases that have crucial roles in plant defense and seed storage protein maturation. Select plant AEPs, however, do... 
CYCLOTIDES | LEGUMAIN | KNOTTED PROTEINS | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | HOST-DEFENSE | CYSTINE KNOT | KALATA B1 | CYCLIZATION | CELL-DEATH | FAMILY | Plant Proteins - genetics | Plants - metabolism | Cysteine Endopeptidases - metabolism | Sequence Analysis, RNA | Plants - genetics | Cysteine Endopeptidases - genetics | Plants, Genetically Modified | Models, Molecular | Plant Proteins - metabolism | RNA, Plant - genetics | Peptides, Cyclic - biosynthesis | Proteins | Engineering | Molecular modelling | Peptides | Proteolysis | Functional testing | Catalysis | Substrates | Molecular chains
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9. Full Text Asparagine endopeptidase cleaves α-synuclein and mediates pathologic activities in Parkinson's disease
by Zhang, Zhentao and Kang, Seong Su and Liu, Xia and Ahn, Eun Hee and Zhang, Zhaohui and He, Li and Iuvone, P Michael and Duong, Duc M and Seyfried, Nicholas T and Benskey, Matthew J and Manfredsson, Fredric P and Jin, Lingjing and Sun, Yi E and Wang, Jian-Zhi and Ye, Keqiang
Nature Structural and Molecular Biology, ISSN 1545-9993, 08/2017, Volume 24, Issue 8, pp. 632 - 642
Aggregated forms of alpha-synuclein play a crucial role in the pathogenesis of synucleinopathies such as Parkinson's disease (PD). However, the molecular... 
LEGUMAIN | PROTEIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | IN-VITRO | BIOPHYSICS | MUTATION | ANIMAL-MODELS | DEGRADATION | MICE | CATHEPSIN-D | AGGREGATION | Proteins | Parkinson Disease - pathology | Animals | Cysteine Endopeptidases - metabolism | Proteolysis | Asparagine - metabolism | Humans | Mice | alpha-Synuclein - metabolism | Protein Aggregation, Pathological | Disease Models, Animal | Index Medicus
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10. Full Text Blockade of Asparagine Endopeptidase Inhibits Cancer Metastasis
by Qi, Qi and Obianyo, Obiamaka and Du, Yuhong and Fu, Haian and Li, Shiyong and Ye, Keqiang
Journal of Medicinal Chemistry, ISSN 0022-2623, 2017, Volume 60, Issue 17, pp. 7244 - 7255
Asparagine endopeptidase (AEP), also called legumain, is highly expressed in various solid tumors, promoting cancer cell invasion, migration, and metastasis.... 
BREAST-CANCER | LEGUMAIN EXPRESSION | ACTIVATION | CHEMISTRY, MEDICINAL | PROGNOSTIC-FACTOR | ORAL BIOAVAILABILITY | CELL INVASION | TUMOR-ASSOCIATED MACROPHAGES | MAMMALIAN LEGUMAIN | MATRIX METALLOPROTEINASE-2 | EXTRACELLULAR-MATRIX | Humans | Lung Neoplasms - metabolism | Neoplasm Invasiveness - prevention & control | Lung Neoplasms - pathology | Antineoplastic Agents - therapeutic use | Structure-Activity Relationship | Breast - metabolism | Breast Neoplasms - metabolism | Cysteine Endopeptidases - metabolism | Lung Neoplasms - secondary | Neoplasm Invasiveness - pathology | Xanthine - pharmacology | Cysteine Proteinase Inhibitors - chemistry | Female | Antineoplastic Agents - pharmacology | Lung - metabolism | Breast - pathology | Cysteine Proteinase Inhibitors - therapeutic use | Lung - pathology | Xanthine - chemistry | Antineoplastic Agents - chemistry | Breast Neoplasms - drug therapy | Animals | Lung Neoplasms - prevention & control | Breast - drug effects | Breast Neoplasms - pathology | Mice, Nude | Cysteine Proteinase Inhibitors - pharmacology | Lung - drug effects | Cell Line, Tumor | Mice | Xanthine - therapeutic use
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11. Full Text Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12
by Singh, Santosh Kumar and SaiSree, L and Amrutha, Ravi N and Reddy, Manjula
Molecular Microbiology, ISSN 0950-382X, 12/2012, Volume 86, Issue 5, pp. 1036 - 1051
Bacterial peptidoglycan ( PG or murein) is a single, large, covalently cross‐linked macromolecule and forms a mesh‐like sacculus that completely encases the... 
MORPHOGENESIS | WALL | PENICILLIN-BINDING-PROTEINS | DAUGHTER CELL-SEPARATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH | INDUCED LYSIS | BETA-LACTAM ANTIBIOTICS | P-BAD PROMOTER | MICROBIOLOGY | COLI MUREIN | DD-ENDOPEPTIDASE | Peptidoglycan - metabolism | Endopeptidases - metabolism | Microscopy, Electron, Scanning | Cysteine Endopeptidases - metabolism | Endopeptidases - genetics | Escherichia coli K12 - growth & development | Cysteine Endopeptidases - genetics | Escherichia coli Proteins - genetics | Escherichia coli Proteins - metabolism | Escherichia coli K12 - genetics | Escherichia coli K12 - enzymology | Escherichia coli K12 - ultrastructure | Enzymes | Crosslinked polymers | Chemical properties | Escherichia coli
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12. Full Text The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis
by Beers, Eric P and Jones, Alan M and Dickerman, Allan W
Phytochemistry, ISSN 0031-9422, 01/2004, Volume 65, Issue 1, pp. 43 - 58
The Arabidopsis thaliana genome has over 550 protease sequences representing all five catalytic types: serine, cysteine, aspartic acid, metallo and threonine... 
Arabidopsis thaliana | Cysteine protease | Crucifereae | Papain | Serine protease | Aspartic protease | Subtilisin | Pepsin | Cysteine Endopeptidases - chemistry | Amino Acid Sequence | Aspartic Acid Endopeptidases - chemistry | Arabidopsis - enzymology | Molecular Sequence Data | Serine Endopeptidases - chemistry | Aspartic Acid Endopeptidases - genetics | Phylogeny | Sequence Alignment | Cysteine Endopeptidases - metabolism | Aspartic Acid Endopeptidases - metabolism | Cysteine Endopeptidases - genetics | Databases, Protein | Serine Endopeptidases - genetics | Serine Endopeptidases - metabolism | Genetic Structures | Embryonic development | Thiols | Genomics | Family | Thrombin | Amino acids | Cellular signal transduction
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13. Full Text Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease
by Zhang, Zhentao and Zhang, Zhentao and Song, Mingke and Liu, Xia and Kang, Seong S.u and Kwon, Il-Sun and Duong, Duc M and Seyfried, Nicholas T and Hu, William T and Liu, Zhixue and Wang, Jian-Zhi and Cheng, Liming and Sun, Yi E and Yu, Shan P.ing and Levey, Allan I and Ye, Keqiang
Nature medicine, ISSN 1078-8956, 11/2014, Volume 20, Issue 11, pp. 1254 - 1262
Neurofibrillary tangles (NFTs), composed of truncated and hyperphosphorylated tau, are a common feature of numerous aging-related neurodegenerative diseases,... 
MEDICINE, RESEARCH & EXPERIMENTAL | ACTIVATION | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CEREBROSPINAL-FLUID | DEGENERATION | CELL BIOLOGY | FILAMENTS | EARLY EVENT | CASPASE-CLEAVAGE | IN-VIVO | TANGLES | BRAIN | Memory Disorders - physiopathology | Up-Regulation | Phosphorylation | Alzheimer Disease - complications | Calpain - metabolism | Humans | Brain - enzymology | Molecular Sequence Data | tau Proteins - metabolism | Cognition | Synapses - pathology | Memory Disorders - complications | tau Proteins - chemistry | Alzheimer Disease - pathology | Caspases - metabolism | Cysteine Endopeptidases - metabolism | Synapses - metabolism | HEK293 Cells | Memory Disorders - pathology | Neurofibrillary Tangles - pathology | Protein Structure, Tertiary | Amino Acid Sequence | Alzheimer Disease - physiopathology | Solubility | Mice, Transgenic | Alzheimer Disease - enzymology | Gene Knockout Techniques | Aging - pathology | Animals | Asparagine - metabolism | Neurofibrillary Tangles - enzymology | Brain - pathology | Neurotoxins - metabolism | Aged | Asparagine | Physiological aspects | Research | Proteases | Alzheimer's disease | Analysis | Proteins | Pathology | Alzheimers disease | Neurodegeneration
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14. Full Text Multiple Associated Proteins Regulate Proteasome Structure and Function
by Leggett, David S and Hanna, John and Borodovsky, Anna and Crosas, Bernat and Schmidt, Marion and Baker, Rohan T and Walz, Thomas and Ploegh, Hidde and Finley, Daniel
Molecular Cell, ISSN 1097-2765, 2002, Volume 10, Issue 3, pp. 495 - 507
We have identified proteins that are abundant in affinity-purified proteasomes, but absent from proteasomes as previously defined because elevated salt... 
YEAST | COMPLEX | DOMAIN | DOA4 DEUBIQUITINATING ENZYME | PATHWAY | UBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | 26S PROTEASOME | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | CORE PARTICLE | CELL BIOLOGY | Cysteine Endopeptidases - chemistry | Ligases - isolation & purification | Ligases - genetics | Multienzyme Complexes - metabolism | Proteasome Endopeptidase Complex | Recombinant Fusion Proteins - metabolism | Protein Subunits - metabolism | Saccharomyces cerevisiae - metabolism | Salts - chemistry | Cysteine Endopeptidases - metabolism | Protein Subunits - isolation & purification | Adenosine Triphosphate - metabolism | Saccharomyces cerevisiae Proteins - isolation & purification | Binding Sites | Endopeptidases - isolation & purification | Protein Subunits - genetics | Multienzyme Complexes - ultrastructure | Endopeptidases - metabolism | Ligases - metabolism | Saccharomyces cerevisiae Proteins - genetics | Canavanine - metabolism | Multienzyme Complexes - chemistry | Proteins - genetics | Ubiquitin-Protein Ligases | Endopeptidases - genetics | Proteins - metabolism | Cysteine Endopeptidases - isolation & purification | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Cysteine Endopeptidases - ultrastructure | Multienzyme Complexes - isolation & purification
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