Rawlings ND


Full name : Rawlings Neil D

First name : Neil D

Mail : Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, Cb10 1SD

Zip Code :

City :

Country : United Kingdom

Email :

Phone :

Fax :

Website :

Directory :

References (18)

Title : Alan Barrett: an appreciation (21 August 1937-23 November 2020) - Rawlings_2021_Biochem.(Lond)_43_73
Author(s) : Rawlings ND
Ref : Biochem (Lond) , 43 :73 , 2021
Abstract : Alan John Barrett was born in Battersea, London, on 21 August 1937, the son of the eminent Cambridge pathologist Dr Max Barrett and his wife Win. Alan was the eldest of five children and brother of Roger 'Syd' Barrett, one of the founder members of the rock band Pink Floyd. Alan's family moved to Cambridge while he was a child, and Alan spent his life and academic career in the Cambridge area. He studied natural sciences at Pembroke College, University of Cambridge, graduating in 1961. His PhD, awarded in 1964, under the supervision of Don H. Northcote at the University's Biochemistry Department was on the 'Pectic Polysaccharides of Higher Plants". In 1965 he joined the Strangeways Research Laboratory, where the research was focussed around osteoarthritis. Alan led his own group and eventually became co-deputy director. In 1977, Alan was awarded a Higher Doctorate (Sc.D) from the University of Cambridge. In 1982, Alan was made a member of the external scientific staff of the Medical Research Council. When the retirement of the director in 1994 forced research at Strangeways into new directions, Alan and his team joined the Immunology Department at the Babraham Institute. Eventually, Alan led the Molecular Enzymology group at Babraham. When Alan retired from the Medical Research Council in 2002, he was invited to join Alex Bateman's team at the Sanger Institute and remained as a visiting scientist when the Bateman team moved to the EMBL-European Bioinformatics Institute. At Strangeways, Alan's interest was in the lysosomal endopeptidases able to digest native collagen. Alan's approach was to devise a purification method, characterize the specificity of the peptidase from its interactions with synthetic substrates and inhibitors and to calculate the kinetics. Initially, Alan worked on the aspartic endopeptidase cathepsin D, then the cysteine endopeptidases cathepsins B, H and L. He and his PhD student, Phyllis Starkey, put forward the "trap mechanism' for the inhibitory activity of the large plasma protein alpha2-macroglobulin, which inhibits endopeptidases of all catalytic types. Alan's team also characterized the cysteine endopeptidase inhibitors known as cystatins. In collaboration with pharmaceutical companies, Alan's team worked on cysteine endopeptidases from papaya (especially chymopapain) that were used for chemonucleolysis of intervertebral discs, and peptidases from pineapple (bromelain and ananain) and fig (ficain) that were used for debridement of burns. Alan's team also developed a blood test for amoebic dysentery by detecting the cysteine endopeptidase histolysain from the pathogenic protozoan Entamoeba histolytica. The discovery of haemoglobinase in the platyhelminth Schistosoma prompted Alan to look for a human homologue, leading to the discovery of legumain, a lysosomal asparagine-specific cysteine endopeptidase previously overlooked. Alan's team also worked on the metallo-oligopeptidases thimet oligopeptidase and neurolysin. It was the action of these oligopeptidases on peptides derived from digestion of proteins by the proteasome that led to the invitation to join the Babraham Institute, where there was an interest in the cell surface presentation of antigenic peptides by the major histocompatibility complex. Alan had an interest in the classification and naming of peptidases, and in the 1980s he and J. Ken McDonald wrote the two volume Mammalian Proteases: A Glossary and Bibliography. When I joined Alan's lab in 1982, eventually becoming his PhD student, we developed a classification of peptidases based on sequence and structural similarities. At Babraham we had better internet access and decided to post our classification online. Eventually, this developed into the MEROPS website, dedicated to the classification and nomenclature of peptidases. The classification was quickly adopted by the SwissProt database and became internationally recognized. It was because of our shared interest in classifying protein sequences into families that we joined Alex Bateman's group at the Sanger Institute who were working on the Pfam database. At Sanger, we expanded the MEROPS website to include peptidase inhibitors, extended the classification to include all proteolytic enzymes and added small molecule inhibitors and collections of known substrate cleavages and peptidase/inhibitor interactions. Alan was instrumental in setting up the International Committee on Proteolysis (now the International Proteolysis Society) and chaired an expert committee on peptidases for Enzyme Nomenclature. He became the first non-American to organize a Gordon Conference ('Proteolytic Enzymes and Their Inhibitors' in 1990). He was a member of several grant review panels and editorial boards, and held consultancy posts with several pharmaceutical and biotech companies. At Strangeways, Alan was supervisor for eight PhD students. He edited two volumes of Methods in Enzymology and he, Fred Woessner and myself were editors of the first two editions of the Handbook of Proteolytic Enzymes. Alan died on 23 November 2020
ESTHER : Rawlings_2021_Biochem.(Lond)_43_73
PubMedSearch : Rawlings_2021_Biochem.(Lond)_43_73

Title : How to use the MEROPS database and website to help understand peptidase specificity - Rawlings_2021_Protein.Sci_30_83
Author(s) : Rawlings ND , Bateman A
Ref : Protein Science , 30 :83 , 2021
Abstract : The MEROPS website (https://www.ebi.ac.uk/merops) and database was established in 1996 to present the classification and nomenclature of proteolytic enzymes. This was expanded to include a classification of protein inhibitors of proteolytic enzymes in 2004. Each peptidase or inhibitor is assigned to a distinct identifier, based on its biochemical and biological properties, and homologous sequences are assembled into a family. Families in which the proteins share similar tertiary structures are assembled into a clan. The MEROPS classification is thus a hierarchy with at least three levels (protein-species, family, and clan) showing the evolutionary relationship. Several other data collections have been assembled, which are accessed from all levels in the hierarchy. These include, sequence homologs, selective bibliographies, substrate cleavage sites, peptidase-inhibitor interactions, alignments, and phylogenetic trees. The substrate cleavage collection has been assembled from the literature and includes physiological, pathological, and nonphysiological cleavages in proteins, peptides, and synthetic substrates. In this article, we make recommendations about how best to analyze these data and show analyses to indicate peptidase binding site preferences and exclusions. We also identify peptidases where co-operative binding occurs between adjacent binding sites.
ESTHER : Rawlings_2021_Protein.Sci_30_83
PubMedSearch : Rawlings_2021_Protein.Sci_30_83
PubMedID: 32920969

Title : Origins of peptidases - Rawlings_2019_Biochimie_166_4
Author(s) : Rawlings ND , Bateman A
Ref : Biochimie , 166 :4 , 2019
Abstract : The distribution of all peptidase homologues across all phyla of organisms was analysed to determine within which kingdom each of the 271 families originated. No family was found to be ubiquitous and even peptidases thought to be essential for life, such as signal peptidase and methionyl aminopeptides are missing from some clades. There are 33 peptidase families common to archaea, bacteria and eukaryotes and are assumed to have originated in the last universal common ancestor (LUCA). These include peptidases with different catalytic types, exo- and endopeptidases, peptidases with different tertiary structures and peptidases from different families but with similar structures. This implies that the different catalytic types and structures pre-date LUCA. Other families have had their origins in the ancestors of viruses, archaea, bacteria, fungi, plants and animals, and a number of families have had their origins in the ancestors of particular phyla. The evolution of peptidases is compared to recent hypotheses about the evolution of organisms.
ESTHER : Rawlings_2019_Biochimie_166_4
PubMedSearch : Rawlings_2019_Biochimie_166_4
PubMedID: 31377195

Title : Using the MEROPS Database for Investigation of Lysosomal Peptidases, Their Inhibitors, and Substrates - Rawlings_2017_Methods.Mol.Biol_1594_213
Author(s) : Rawlings ND
Ref : Methods Mol Biol , 1594 :213 , 2017
Abstract : This chapter describes how to retrieve data on lysosomal peptidases from the MEROPS database for proteolytic enzymes, their substrates and inhibitors ( http://merops.sanger.ac.uk ). Features described in this chapter include the summary page, pages for structure, interactions with inhibitors, substrates, literature and involvement in physiological pathways, and how to download data from the MEROPS FTP site. The lysosomal peptidase legumain is used as an example.
ESTHER : Rawlings_2017_Methods.Mol.Biol_1594_213
PubMedSearch : Rawlings_2017_Methods.Mol.Biol_1594_213
PubMedID: 28456986

Title : Creating a specialist protein resource network: a meeting report for the protein bioinformatics and community resources retreat - Babbitt_2015_Database.(Oxford)_2015_bav063
Author(s) : Babbitt PC , Bagos PG , Bairoch A , Bateman A , Chatonnet A , Chen MJ , Craik DJ , Finn RD , Gloriam D , Haft DH , Henrissat B , Holliday GL , Isberg V , Kaas Q , Landsman D , Lenfant N , Manning G , Nagano N , Srinivasan N , O'Donovan C , Pruitt KD , Sowdhamini R , Rawlings ND , Saier MH, Jr. , Sharman JL , Spedding M , Tsirigos KD , Vastermark A , Vriend G
Ref : Database (Oxford) , 2015 :bav063 , 2015
Abstract : During 11-12 August 2014, a Protein Bioinformatics and Community Resources Retreat was held at the Wellcome Trust Genome Campus in Hinxton, UK. This meeting brought together the principal investigators of several specialized protein resources (such as CAZy, TCDB and MEROPS) as well as those from protein databases from the large Bioinformatics centres (including UniProt and RefSeq). The retreat was divided into five sessions: (1) key challenges, (2) the databases represented, (3) best practices for maintenance and curation, (4) information flow to and from large data centers and (5) communication and funding. An important outcome of this meeting was the creation of a Specialist Protein Resource Network that we believe will improve coordination of the activities of its member resources. We invite further protein database resources to join the network and continue the dialogue.
ESTHER : Babbitt_2015_Database.(Oxford)_2015_bav063
PubMedSearch : Babbitt_2015_Database.(Oxford)_2015_bav063
PubMedID: 26284514

Title : Key challenges for the creation and maintenance of specialist protein resources - Holliday_2015_Proteins_83_1005
Author(s) : Holliday GL , Bairoch A , Bagos PG , Chatonnet A , Craik DJ , Finn RD , Henrissat B , Landsman D , Manning G , Nagano N , O'Donovan C , Pruitt KD , Rawlings ND , Saier MH, Jr. , Sowdhamini R , Spedding M , Srinivasan N , Vriend G , Babbitt PC , Bateman A
Ref : Proteins , 83 :1005 , 2015
Abstract : As the volume of data relating to proteins increases, researchers rely more and more on the analysis of published data, thus increasing the importance of good access to these data that vary from the supplemental material of individual articles, all the way to major reference databases with professional staff and long-term funding. Specialist protein resources fill an important middle ground, providing interactive web interfaces to their databases for a focused topic or family of proteins, using specialized approaches that are not feasible in the major reference databases. Many are labors of love, run by a single lab with little or no dedicated funding and there are many challenges to building and maintaining them. This perspective arose from a meeting of several specialist protein resources and major reference databases held at the Wellcome Trust Genome Campus (Cambridge, UK) on August 11 and 12, 2014. During this meeting some common key challenges involved in creating and maintaining such resources were discussed, along with various approaches to address them. In laying out these challenges, we aim to inform users about how these issues impact our resources and illustrate ways in which our working together could enhance their accuracy, currency, and overall value. Proteins 2015; 83:1005-1013. (c) 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.
ESTHER : Holliday_2015_Proteins_83_1005
PubMedSearch : Holliday_2015_Proteins_83_1005
PubMedID: 25820941

Title : MEROPS: the database of proteolytic enzymes, their substrates and inhibitors - Rawlings_2012_Nucleic.Acids.Res_40_D343
Author(s) : Rawlings ND , Barrett AJ , Bateman A
Ref : Nucleic Acids Research , 40 :D343 , 2012
Abstract : Peptidases, 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 database has hierarchical classifications in which homologous sets of peptidases and protein inhibitors are grouped into protein species, which are grouped into families, which are in turn grouped into clans. The database has been expanded to include proteolytic enzymes other than peptidases. Special identifiers for peptidases from a variety of model organisms have been established so that orthologues can be detected in other species. A table of predicted active-site residue and metal ligand positions and the residue ranges of the peptidase domains in orthologues has been added to each peptidase summary. New displays of tertiary structures, which can be rotated or have the surfaces displayed, have been added to the structure pages. New indexes for gene names and peptidase substrates have been made available. Among the enhancements to existing features are the inclusion of small-molecule inhibitors in the tables of peptidase-inhibitor interactions, a table of known cleavage sites for each protein substrate, and tables showing the substrate-binding preferences of peptidases derived from combinatorial peptide substrate libraries.
ESTHER : Rawlings_2012_Nucleic.Acids.Res_40_D343
PubMedSearch : Rawlings_2012_Nucleic.Acids.Res_40_D343
PubMedID: 22086950

Title : Peptidase inhibitors in the MEROPS database - Rawlings_2010_Biochimie_92_1463
Author(s) : Rawlings ND
Ref : Biochimie , 92 :1463 , 2010
Abstract : The MEROPS website (http://merops.sanger.ac.uk) includes information on peptidase inhibitors as well as on peptidases and their substrates. Displays have been put in place to link peptidases and inhibitors together. The classification of protein peptidase inhibitors is continually being revised, and currently inhibitors are grouped into 67 families based on comparisons of protein sequences. These families can be further grouped into 38 clans based on comparisons of tertiary structure. Small molecule inhibitors are important reagents for peptidase characterization and, with the increasing importance of peptidases as drug targets, they are also important to the pharmaceutical industry. Small molecule inhibitors are now included in MEROPS and over 160 summaries have been written.
ESTHER : Rawlings_2010_Biochimie_92_1463
PubMedSearch : Rawlings_2010_Biochimie_92_1463
PubMedID: 20430064

Title : The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome - Rawlings_2008_Biochimie_90_243
Author(s) : Rawlings ND , Morton FR
Ref : Biochimie , 90 :243 , 2008
Abstract : Many of the 181 families of peptidases contain homologues that are known to have functions other than peptide bond hydrolysis. Distinguishing an active peptidase from a homologue that is not a peptidase requires specialist knowledge of the important active site residues, because replacement or lack of one of these catalytic residues is an important clue that the homologue in question is unlikely to hydrolyse peptide bonds. Now that the rate at which proteins are characterized is outstripped by the rate that genome sequences are determined, many genes are being incorrectly annotated because only sequence similarity is taken into consideration. We present a tool called the MEROPS batch BLAST which not only performs a comparison against the MEROPS sequence collection, but also does a pair-wise alignment with the closest homologue detected and calculates the position of the active site residues. A non-peptidase homologue can be distinguished by the absence or unacceptable replacement of any of these residues. An analysis of peptidase homologues in the genome of the bacterium Erythrobacter litoralis is presented as an example.
ESTHER : Rawlings_2008_Biochimie_90_243
PubMedSearch : Rawlings_2008_Biochimie_90_243
PubMedID: 17980477

Title : MEROPS: the peptidase database - Rawlings_2008_Nucleic.Acids.Res_36_D320
Author(s) : Rawlings ND , Morton FR , Kok CY , Kong J , Barrett AJ
Ref : Nucleic Acids Research , 36 :D320 , 2008
Abstract : 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.
ESTHER : Rawlings_2008_Nucleic.Acids.Res_36_D320
PubMedSearch : Rawlings_2008_Nucleic.Acids.Res_36_D320
PubMedID: 17991683

Title : Unusual phyletic distribution of peptidases as a tool for identifying potential drug targets - Rawlings_2007_Biochem.J_401_e5
Author(s) : Rawlings ND
Ref : Biochemical Journal , 401 :e5 , 2007
Abstract : Eukaryote homologues of carboxypeptidases Taq have been discovered by Niemirowicz et al. in the protozoan Trypanosoma cruzi, the causative agent of Chagas' disease. This is surprising, because the peptidase family was thought to be restricted to bacteria and archaea. In this issue of the Biochemical Journal, the authors propose that the Trypanosoma carboxypeptidases are potential drug targets for treatment of the disease. The authors also propose that the presence of the genes in the zooflagellates can be explained by a horizontal transfer of an ancestral gene from a prokaryote. Because peptidases are popular drug targets, identifying parasite or pathogen peptidases that have no homologues in their hosts would be a method to select the most promising targets. To understand how unusual this phyletic distribution is among the 183 families of peptidases, several other examples of horizontal transfers are presented, as well as some unusual losses of peptidase genes.
ESTHER : Rawlings_2007_Biochem.J_401_e5
PubMedSearch : Rawlings_2007_Biochem.J_401_e5
PubMedID: 17173540

Title : 'Species' of peptidases - Barrett_2007_Biol.Chem_388_1151
Author(s) : Barrett AJ , Rawlings ND
Ref : Biol Chem , 388 :1151 , 2007
Abstract : A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser number of what we term 'species' of peptidases. Just over 2000 peptidase species are recognised today, but we estimate that 25 000 will one day be known. Each species is built around a peptidase protein that has been adequately characterised. The cluster of peptidase proteins that represent the single species is then assembled primarily by analysis of a sequence 'tree' for the family. Each peptidase species is given a systematic identifier and a summary page of data regarding it is assembled. Because the characterisation of new peptidases lags far behind the sequencing, the majority of peptidase proteins are so far known only as amino acid sequences and cannot yet be assigned to species. We suggest that new forms of analysis of the sequences of the unassigned peptidases may give early indications of how they will cluster into the new species of the future.
ESTHER : Barrett_2007_Biol.Chem_388_1151
PubMedSearch : Barrett_2007_Biol.Chem_388_1151
PubMedID: 17976007

Title : MEROPS: the peptidase database - Rawlings_2006_Nucleic.Acids.Res_34_D270
Author(s) : Rawlings ND , Morton FR , Barrett AJ
Ref : Nucleic Acids Research , 34 :D270 , 2006
Abstract : Peptidases (proteolytic enzymes) and their natural, protein 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 proteins. The organizational principle of the database is a hierarchical classification in which homologous sets of proteins of interest are grouped into families and the homologous families are grouped in clans. The most important addition to the database has been newly written, concise text annotations for each peptidase family. Other forms of information recently added include highlighting of active site residues (or the replacements that render some homologues inactive) in the sequence displays and BlastP search results, dynamically generated alignments and trees at the peptidase or inhibitor level, and a curated list of human and mouse homologues that have been experimentally characterized as active. A new way to display information at taxonomic levels higher than species has been devised. In the Literature pages, references have been flagged to draw attention to particularly 'hot' topics.
ESTHER : Rawlings_2006_Nucleic.Acids.Res_34_D270
PubMedSearch : Rawlings_2006_Nucleic.Acids.Res_34_D270
PubMedID: 16381862

Title : Genome of the host-cell transforming parasite Theileria annulata compared with T. parva - Pain_2005_Science_309_131
Author(s) : Pain A , Renauld H , Berriman M , Murphy L , Yeats CA , Weir W , Kerhornou A , Aslett M , Bishop R , Bouchier C , Cochet M , Coulson RM , Cronin A , de Villiers EP , Fraser A , Fosker N , Gardner M , Goble A , Griffiths-Jones S , Harris DE , Katzer F , Larke N , Lord A , Maser P , McKellar S , Mooney P , Morton F , Nene V , O'Neil S , Price C , Quail MA , Rabbinowitsch E , Rawlings ND , Rutter S , Saunders D , Seeger K , Shah T , Squares R , Squares S , Tivey A , Walker AR , Woodward J , Dobbelaere DA , Langsley G , Rajandream MA , McKeever D , Shiels B , Tait A , Barrell B , Hall N
Ref : Science , 309 :131 , 2005
Abstract : Theileria annulata and T. parva are closely related protozoan parasites that cause lymphoproliferative diseases of cattle. We sequenced the genome of T. annulata and compared it with that of T. parva to understand the mechanisms underlying transformation and tropism. Despite high conservation of gene sequences and synteny, the analysis reveals unequally expanded gene families and species-specific genes. We also identify divergent families of putative secreted polypeptides that may reduce immune recognition, candidate regulators of host-cell transformation, and a Theileria-specific protein domain [frequently associated in Theileria (FAINT)] present in a large number of secreted proteins.
ESTHER : Pain_2005_Science_309_131
PubMedSearch : Pain_2005_Science_309_131
PubMedID: 15994557
Gene_locus related to this paper: thean-q4u9u6 , thean-q4ub48 , thean-q4ubz1 , thean-q4uc78 , thean-q4uc93 , thean-q4uck1 , thean-q4udw9 , thean-q4ue56 , thean-q4uf06 , thean-q4ug98 , thean-q4uhj9 , thepa-q4n349

Title : MEROPS: the peptidase database - Rawlings_2004_Nucleic.Acids.Res_32_D160
Author(s) : Rawlings ND , Tolle DP , Barrett AJ
Ref : Nucleic Acids Research , 32 :D160 , 2004
Abstract : Peptidases (proteolytic enzymes) are of great relevance to biology, medicine and biotechnology. This practical importance creates a need for an integrated source of information about them, and also about their natural inhibitors. The MEROPS database (http:\/\/merops.sanger.ac.uk) aims to fill this need. The organizational principle of the database is a hierarchical classification in which homologous sets of the proteins of interest are grouped in families and the homologous families are grouped in clans. Each peptidase, family and clan has a unique identifier. The database has recently been expanded to include the protein inhibitors of peptidases, and these are classified in much the same way as the peptidases. Forms of information recently added include new links to other databases, summary alignments for peptidase clans, displays to show the distribution of peptidases and inhibitors among organisms, substrate cleavage sites and indexes for expressed sequence tag libraries containing peptidases. A new way of making hyperlinks to the database has been devised and a BlastP search of our library of peptidase and inhibitor sequences has been added.
ESTHER : Rawlings_2004_Nucleic.Acids.Res_32_D160
PubMedSearch : Rawlings_2004_Nucleic.Acids.Res_32_D160
PubMedID: 14681384

Title : Families of serine peptidases -
Author(s) : Rawlings ND , Barrett AJ
Ref : Methods Enzymol , 244 :19 , 1994
PubMedID: 7845208

Title : Oligopeptidases, and the emergence of the prolyl oligopeptidase family - Barrett_1992_Biol.Chem.Hoppe.Seyler_373_353
Author(s) : Barrett AJ , Rawlings ND
Ref : Biol Chem Hoppe Seyler , 373 :353 , 1992
Abstract : Oligopeptidases are endopeptidases that are not proteinases in the strict sense, since they do not hydrolyse peptide bonds in proteins, but act only on smaller polypeptides or oligopeptides. These enzymes apparently perform important, specialized biological functions that include the modification or destruction of peptide messenger molecules. Oligopeptidases have few naturally occurring inhibitors, and their distinctive specificity prevents them from interacting with alpha 2-macroglobulin, unlike the great majority of endopeptidases. The specificity of these specialized endopeptidases doubtless depends upon the three-dimensional structure of the active site, but no crystallographic structure is yet available for an oligopeptidase. Study of the primary structure of prolyl oligopeptidase has recently shown that it is a member of a new family of serine-type peptidases most of which are exopeptidases. The alignment of the sequences leads to the identification of some catalytic triad residues that have not yet been elucidated experimentally.
ESTHER : Barrett_1992_Biol.Chem.Hoppe.Seyler_373_353
PubMedSearch : Barrett_1992_Biol.Chem.Hoppe.Seyler_373_353
PubMedID: 1515061

Title : A new family of serine-type peptidases related to prolyl oligopeptidase [letter] - Rawlings_1991_Biochem.J_279_907
Author(s) : Rawlings ND , Polgar L , Barrett AJ
Ref : Biochemical Journal , 279 :907 , 1991
Abstract :
ESTHER : Rawlings_1991_Biochem.J_279_907
PubMedSearch : Rawlings_1991_Biochem.J_279_907
PubMedID: 1953688