Skip Navigation


Nucleic Acids Research Advance Access originally published online on November 8, 2007
Nucleic Acids Research 2008 36(Database issue):D320-D325; doi:10.1093/nar/gkm954
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (4769K) Freely available
Right arrow Screen PDF (577K) Freely available
Right arrowOA All Versions of this Article:
36/suppl_1/D320    most recent
gkm954v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Rawlings, N. D.
Right arrow Articles by Barrett, A. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rawlings, N. D.
Right arrow Articles by Barrett, A. J.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2008, Vol. 36, Database issue D320-D325
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This article appears in the following Nucleic Acids Research issue: Database issue [View the issue table of contents]

Articles

MEROPS: the peptidase database

Neil D. Rawlings*, Fraser R. Morton, Chai Yin Kok, Jun Kong and Alan J. Barrett

The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire, CB10 1SA, UK

*To whom correspondence should be addressed. Tel: +44 1223 494983; Fax: +44 1223 494919; Email: ndr{at}sanger.ac.uk

Received September 17, 2007. Revised October 15, 2007. Accepted October 15, 2007.

Peptidases (proteolytic enzymes or proteases), their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these. The organizational principle of the database is a hierarchical classification in which homologous sets of peptidases and protein inhibitors are grouped into protein species, which are grouped into families and in turn grouped into clans. Important additions to the database include newly written, concise text annotations for peptidase clans and the small molecule inhibitors that are outside the scope of the standard classification; displays to show peptidase specificity compiled from our collection of known substrate cleavages; tables of peptidase–inhibitor interactions; and dynamically generated alignments of representatives of each protein species at the family level. New ways to compare peptidase and inhibitor complements between any two organisms whose genomes have been completely sequenced, or between different strains or subspecies of the same organism, have been devised.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
DatabaseHome page
N. D. Rawlings
A large and accurate collection of peptidase cleavages in the MEROPS database
Database, November 2, 2009; 2009(0): bap015 - bap015.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
M. J. McBride, G. Xie, E. C. Martens, A. Lapidus, B. Henrissat, R. G. Rhodes, E. Goltsman, W. Wang, J. Xu, D. W. Hunnicutt, et al.
Novel Features of the Polysaccharide-Digesting Gliding Bacterium Flavobacterium johnsoniae as Revealed by Genome Sequence Analysis
Appl. Envir. Microbiol., November 1, 2009; 75(21): 6864 - 6875.
[Abstract] [Full Text] [PDF]


Home page
Protein Eng Des SelHome page
B. Eldridge, R. N. Cooley, R. Odegrip, D. P. McGregor, K. J. FitzGerald, and C. G. Ullman
An in vitro selection strategy for conferring protease resistance to ligand binding peptides
Protein Eng. Des. Sel., November 1, 2009; 22(11): 691 - 698.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
M. J. Lingard and B. Bartel
Arabidopsis LON2 Is Necessary for Peroxisomal Function and Sustained Matrix Protein Import
Plant Physiology, November 1, 2009; 151(3): 1354 - 1365.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
M. Martinez, I. Cambra, L. Carrillo, M. Diaz-Mendoza, and I. Diaz
Characterization of the Entire Cystatin Gene Family in Barley and Their Target Cathepsin L-Like Cysteine-Proteases, Partners in the Hordein Mobilization during Seed Germination
Plant Physiology, November 1, 2009; 151(3): 1531 - 1545.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Prochazkova, L. A. Shuvalova, G. Minasov, Z. Voburka, W. F. Anderson, and K. J. F. Satchell
Structural and Molecular Mechanism for Autoprocessing of MARTX Toxin of Vibrio cholerae at Multiple Sites
J. Biol. Chem., September 25, 2009; 284(39): 26557 - 26568.
[Abstract] [Full Text] [PDF]


Home page
J. Histochem. Cytochem.Home page
T. T. Myohanen, J. A. Garcia-Horsman, J. Tenorio-Laranga, and P. T. Mannisto
Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity
J. Histochem. Cytochem., September 1, 2009; 57(9): 831 - 848.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
J. Haiko, M. Kukkonen, J. J. Ravantti, B. Westerlund-Wikstrom, and T. K. Korhonen
The Single Substitution I259T, Conserved in the Plasminogen Activator Pla of Pandemic Yersinia pestis Branches, Enhances Fibrinolytic Activity
J. Bacteriol., August 1, 2009; 191(15): 4758 - 4766.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
G. Debret, A. Martel, and P. Cuniasse
RASMOT-3D PRO: a 3D motif search webserver
Nucleic Acids Res., July 1, 2009; 37(suppl_2): W459 - W464.
[Abstract] [Full Text] [PDF]


Home page
GutHome page
D Bernardo, J A Garrote, I Nadal, A J Leon, C Calvo, L Fernandez-Salazar, A Blanco-Quiros, Y Sanz, and E Arranz
Is it true that coeliacs do not digest gliadin? Degradation pattern of gliadin in coeliac disease small intestinal mucosa
Gut, June 1, 2009; 58(6): 886 - 887.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Cedzich, F. Huttenlocher, B. M. Kuhn, J. Pfannstiel, L. Gabler, A. Stintzi, and A. Schaller
The Protease-associated Domain and C-terminal Extension Are Required for Zymogen Processing, Sorting within the Secretory Pathway, and Activity of Tomato Subtilase 3 (SlSBT3)
J. Biol. Chem., May 22, 2009; 284(21): 14068 - 14078.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C.-C. Wang, H.-C. Houng, C.-L. Chen, P.-J. Wang, C.-F. Kuo, Y.-S. Lin, J.-J. Wu, M. T. Lin, C.-C. Liu, W. Huang, et al.
Solution Structure and Backbone Dynamics of Streptopain: INSIGHT INTO DIVERSE SUBSTRATE SPECIFICITY
J. Biol. Chem., April 17, 2009; 284(16): 10957 - 10967.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
A. H. Camp and R. Losick
A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis
Genes & Dev., April 15, 2009; 23(8): 1014 - 1024.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Baniulis, E. Yamashita, J. P. Whitelegge, A. I. Zatsman, M. P. Hendrich, S. S. Hasan, C. M. Ryan, and W. A. Cramer
Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120
J. Biol. Chem., April 10, 2009; 284(15): 9861 - 9869.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B.-B. Xie, F. Bian, X.-L. Chen, H.-L. He, J. Guo, X. Gao, Y.-X. Zeng, B. Chen, B.-C. Zhou, and Y.-Z. Zhang
Cold Adaptation of Zinc Metalloproteases in the Thermolysin Family from Deep Sea and Arctic Sea Ice Bacteria Revealed by Catalytic and Structural Properties and Molecular Dynamics: NEW INSIGHTS INTO RELATIONSHIP BETWEEN CONFORMATIONAL FLEXIBILITY AND HYDROGEN BONDING
J. Biol. Chem., April 3, 2009; 284(14): 9257 - 9269.
[Abstract] [Full Text] [PDF]


Home page
Innate ImmunityHome page
J. Haiko, M. Suomalainen, T. Ojala, K. Lahteenmaki, and T. K. Korhonen
Invited review: Breaking barriers -- attack on innate immune defences by omptin surface proteases of enterobacterial pathogens
Innate Immunity, April 1, 2009; 15(2): 67 - 80.
[Abstract] [PDF]


Home page
Nucleic Acids ResHome page
V. Quesada, G. R. Ordonez, L. M. Sanchez, X. S. Puente, and C. Lopez-Otin
The Degradome database: mammalian proteases and diseases of proteolysis
Nucleic Acids Res., January 1, 2009; 37(suppl_1): D239 - D243.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
N. Padmanabhan, L. Fichtner, A. Dickmanns, R. Ficner, J. B. Schulz, and G. H. Braus
The Yeast HtrA Orthologue Ynm3 Is a Protease with Chaperone Activity that Aids Survival Under Heat Stress
Mol. Biol. Cell, January 1, 2009; 20(1): 68 - 77.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
C.-T. Chen, E.-W. Yang, H.-J. Hsu, Y.-K. Sun, W.-L. Hsu, and A.-S. Yang
Protease substrate site predictors derived from machine learning on multilevel substrate phage display data
Bioinformatics, December 1, 2008; 24(23): 2691 - 2697.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. J. Page and E. Di Cera
Evolution of Peptidase Diversity
J. Biol. Chem., October 31, 2008; 283(44): 30010 - 30014.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Kondas, G. Szlama, M. Trexler, and L. Patthy
Both WFIKKN1 and WFIKKN2 Have High Affinity for Growth and Differentiation Factors 8 and 11
J. Biol. Chem., August 29, 2008; 283(35): 23677 - 23684.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. K. Baral, N. Jajcanin-Jozic, S. Deller, P. Macheroux, M. Abramic, and K. Gruber
The First Structure of Dipeptidyl-peptidase III Provides Insight into the Catalytic Mechanism and Mode of Substrate Binding
J. Biol. Chem., August 8, 2008; 283(32): 22316 - 22324.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Bhaskaran, M. O. Palmier, J. L. Lauer-Fields, G. B. Fields, and S. R. Van Doren
MMP-12 Catalytic Domain Recognizes Triple Helical Peptide Models of Collagen V with Exosites and High Activity
J. Biol. Chem., August 1, 2008; 283(31): 21779 - 21788.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.