Potent new inhibitors of human renin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-10

AUTHORS

M. Szelke, B. Leckie, A. Hallett, D. M. Jones, J. Sueiras, B. Atrash, A. F. Lever

ABSTRACT

The renal acid protease renin selectively cleaves its plasma substrate angiotensinogen to release the decapeptide angiotensin I, which in turn is cleaved by a carboxydipeptidase converting enzyme to yield the pressor octapeptide angiotensin II1. It is generally accepted that the renin–angiotensin system has a physiological role in blood pressure and electrolyte homeostasis2, and that abnormalities of the system contribute to certain forms of hypertension3. We previously showed that reduction of the Leu10–Leu11 scissile peptide bond in the (6–13) octapeptide sequence 2 of equine angiotensinogen produced potent and selective inhibitors of canine plasma renin5. We have now used the same approach to modify the recently elucidated N-terminal sequence6 of human angiotensinogen and report here the production of highly active and species-specific in vitro inhibitors of endogenous human renin cleaving renin substrate in human plasma. Whereas the (6–13) octapeptide H-112 of human angiotensinogen is only a weak inhibitor of human plasma renin (IC50 = 313 µM), the analogue H-113, in which the scissile Leu–Val bond has been reduced, has IC50 = 0.19 µM. Extension of H-113 with Pro at the N-terminus and with Lys at the C-terminus7, giving the decapeptide derivative H-142, increases inhibitory potency further (IC50 = 10 nM). We believe that the high in vitro inhibitory potencies of H-113 and H-142 are due to the ability of the reduced moiety —CH2—NH— to act as a non-hydrolysable analogue of the tetrahedral transition state formed during hydrolysis of the (10–11) peptide bond. H-113 and H-142 are strongly species specific, and are highly specific for renin among acid proteases: H-142 has no inhibitory effect in vitro on human cathepsin D or renal acid protease at a concentration of 712 µM. More... »

PAGES

555-557

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/299555a0

DOI

http://dx.doi.org/10.1038/299555a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010842288

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6750410


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biological Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biochemistry and Cell Biology", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Amino Acid Sequence", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Angiotensinogen", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Cathepsins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Humans", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Peptide Fragments", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protease Inhibitors", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Renin", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Species Specificity", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Stereoisomerism", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Substrate Specificity", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Szelke", 
        "givenName": "M.", 
        "id": "sg:person.0747520133.37", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0747520133.37"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Leckie", 
        "givenName": "B.", 
        "id": "sg:person.01240176361.23", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01240176361.23"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Hallett", 
        "givenName": "A.", 
        "id": "sg:person.0677134061.59", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0677134061.59"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Jones", 
        "givenName": "D. M.", 
        "id": "sg:person.01013362461.91", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01013362461.91"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Sueiras", 
        "givenName": "J.", 
        "id": "sg:person.01052301345.43", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01052301345.43"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Atrash", 
        "givenName": "B.", 
        "id": "sg:person.0671150441.95", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0671150441.95"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.7445.2", 
          "name": [
            "Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Lever", 
        "givenName": "A. F.", 
        "id": "sg:person.010160653772.18", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010160653772.18"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/291329a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1001285573", 
          "https://doi.org/10.1038/291329a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/217456a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1046041661", 
          "https://doi.org/10.1038/217456a0"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1982-10", 
    "datePublishedReg": "1982-10-01", 
    "description": "The renal acid protease renin selectively cleaves its plasma substrate angiotensinogen to release the decapeptide angiotensin I, which in turn is cleaved by a carboxydipeptidase converting enzyme to yield the pressor octapeptide angiotensin II1. It is generally accepted that the renin\u2013angiotensin system has a physiological role in blood pressure and electrolyte homeostasis2, and that abnormalities of the system contribute to certain forms of hypertension3. We previously showed that reduction of the Leu10\u2013Leu11 scissile peptide bond in the (6\u201313) octapeptide sequence 2 of equine angiotensinogen produced potent and selective inhibitors of canine plasma renin5. We have now used the same approach to modify the recently elucidated N-terminal sequence6 of human angiotensinogen and report here the production of highly active and species-specific in vitro inhibitors of endogenous human renin cleaving renin substrate in human plasma. Whereas the (6\u201313) octapeptide H-112 of human angiotensinogen is only a weak inhibitor of human plasma renin (IC50 = 313 \u00b5M), the analogue H-113, in which the scissile Leu\u2013Val bond has been reduced, has IC50 = 0.19 \u00b5M. Extension of H-113 with Pro at the N-terminus and with Lys at the C-terminus7, giving the decapeptide derivative H-142, increases inhibitory potency further (IC50 = 10 nM). We believe that the high in vitro inhibitory potencies of H-113 and H-142 are due to the ability of the reduced moiety \u2014CH2\u2014NH\u2014 to act as a non-hydrolysable analogue of the tetrahedral transition state formed during hydrolysis of the (10\u201311) peptide bond. H-113 and H-142 are strongly species specific, and are highly specific for renin among acid proteases: H-142 has no inhibitory effect in vitro on human cathepsin D or renal acid protease at a concentration of 712 \u00b5M.", 
    "genre": "article", 
    "id": "sg:pub.10.1038/299555a0", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1018957", 
        "issn": [
          "0028-0836", 
          "1476-4687"
        ], 
        "name": "Nature", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "5883", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "299"
      }
    ], 
    "keywords": [
      "renin-angiotensin system", 
      "human angiotensinogen", 
      "decapeptide angiotensin I", 
      "inhibitory potency", 
      "blood pressure", 
      "plasma renin", 
      "human plasma renin", 
      "renin substrate", 
      "renin", 
      "substrate angiotensinogen", 
      "angiotensin I", 
      "angiotensinogen", 
      "non-hydrolysable analogue", 
      "inhibitory effect", 
      "converting enzyme", 
      "human renin", 
      "protease renin", 
      "cathepsin D", 
      "selective inhibitor", 
      "inhibitors", 
      "potent new inhibitor", 
      "physiological role", 
      "weak inhibitor", 
      "human plasma", 
      "potency", 
      "abnormalities", 
      "acid protease", 
      "human cathepsin D", 
      "certain forms", 
      "IC50", 
      "new inhibitors", 
      "protease", 
      "report", 
      "sequence 2", 
      "plasma", 
      "role", 
      "reduction", 
      "effect", 
      "pressure", 
      "concentration", 
      "enzyme", 
      "ability", 
      "pros", 
      "analogues", 
      "peptide bond", 
      "Lys", 
      "production", 
      "same approach", 
      "terminus", 
      "system", 
      "form", 
      "Leu-Val bond", 
      "turn", 
      "II1", 
      "approach", 
      "hydrolysis", 
      "state", 
      "extension", 
      "species", 
      "substrate", 
      "scissile peptide bond", 
      "bonds", 
      "tetrahedral transition state", 
      "transition state", 
      "renal acid protease renin", 
      "acid protease renin", 
      "plasma substrate angiotensinogen", 
      "carboxydipeptidase converting enzyme", 
      "pressor octapeptide angiotensin II1", 
      "angiotensin II1", 
      "electrolyte homeostasis2", 
      "homeostasis2", 
      "hypertension3", 
      "Leu10\u2013Leu11 scissile peptide bond", 
      "equine angiotensinogen", 
      "canine plasma renin5", 
      "plasma renin5", 
      "renin5", 
      "terminal sequence6", 
      "sequence6", 
      "endogenous human renin cleaving renin substrate", 
      "human renin cleaving renin substrate", 
      "renin cleaving renin substrate", 
      "cleaving renin substrate", 
      "H-112", 
      "analogue H-113", 
      "H-113", 
      "scissile Leu\u2013Val bond", 
      "Extension of H-113", 
      "terminus7", 
      "derivative H-142", 
      "H-142", 
      "moiety \u2014CH2\u2014NH", 
      "renal acid protease"
    ], 
    "name": "Potent new inhibitors of human renin", 
    "pagination": "555-557", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1010842288"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/299555a0"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "6750410"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/299555a0", 
      "https://app.dimensions.ai/details/publication/pub.1010842288"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2021-11-01T17:55", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20211101/entities/gbq_results/article/article_160.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1038/299555a0"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/299555a0'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/299555a0'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/299555a0'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/299555a0'


 

This table displays all metadata directly associated to this object as RDF triples.

245 TRIPLES      21 PREDICATES      132 URIs      122 LITERALS      17 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/299555a0 schema:about N12dae0cb175f42e3a7a7a4e5e3a4a632
2 N4dd0635e05e84921a4771fea192b79fe
3 N812383c77951450db85c1495737cbae5
4 N9f2f6aad9dfe4d91b08b4e29214219af
5 Nb194d0df2d81474684341b823c19ed4e
6 Nf0acb417eb4d4c4497fe27a1cf0eb40a
7 Nf2f708e53f4d463db8b6743b55f25010
8 Nf4b279f2191e4ba5871883ec5db3ed53
9 Nf618204012784fe79aee70715d052d86
10 Nf6f0c20ec60d40de95660383fb812de8
11 anzsrc-for:06
12 anzsrc-for:0601
13 schema:author Nd7caae364fec4877b08d85a40b334920
14 schema:citation sg:pub.10.1038/217456a0
15 sg:pub.10.1038/291329a0
16 schema:datePublished 1982-10
17 schema:datePublishedReg 1982-10-01
18 schema:description The renal acid protease renin selectively cleaves its plasma substrate angiotensinogen to release the decapeptide angiotensin I, which in turn is cleaved by a carboxydipeptidase converting enzyme to yield the pressor octapeptide angiotensin II1. It is generally accepted that the renin–angiotensin system has a physiological role in blood pressure and electrolyte homeostasis2, and that abnormalities of the system contribute to certain forms of hypertension3. We previously showed that reduction of the Leu10–Leu11 scissile peptide bond in the (6–13) octapeptide sequence 2 of equine angiotensinogen produced potent and selective inhibitors of canine plasma renin5. We have now used the same approach to modify the recently elucidated N-terminal sequence6 of human angiotensinogen and report here the production of highly active and species-specific in vitro inhibitors of endogenous human renin cleaving renin substrate in human plasma. Whereas the (6–13) octapeptide H-112 of human angiotensinogen is only a weak inhibitor of human plasma renin (IC50 = 313 µM), the analogue H-113, in which the scissile Leu–Val bond has been reduced, has IC50 = 0.19 µM. Extension of H-113 with Pro at the N-terminus and with Lys at the C-terminus7, giving the decapeptide derivative H-142, increases inhibitory potency further (IC50 = 10 nM). We believe that the high in vitro inhibitory potencies of H-113 and H-142 are due to the ability of the reduced moiety —CH2—NH— to act as a non-hydrolysable analogue of the tetrahedral transition state formed during hydrolysis of the (10–11) peptide bond. H-113 and H-142 are strongly species specific, and are highly specific for renin among acid proteases: H-142 has no inhibitory effect in vitro on human cathepsin D or renal acid protease at a concentration of 712 µM.
19 schema:genre article
20 schema:isAccessibleForFree false
21 schema:isPartOf N734cdb9ff843468c8e599cfa8972a118
22 N9646ab022c334f768a276e319ebedc62
23 sg:journal.1018957
24 schema:keywords Extension of H-113
25 H-112
26 H-113
27 H-142
28 IC50
29 II1
30 Leu-Val bond
31 Leu10–Leu11 scissile peptide bond
32 Lys
33 ability
34 abnormalities
35 acid protease
36 acid protease renin
37 analogue H-113
38 analogues
39 angiotensin I
40 angiotensin II1
41 angiotensinogen
42 approach
43 blood pressure
44 bonds
45 canine plasma renin5
46 carboxydipeptidase converting enzyme
47 cathepsin D
48 certain forms
49 cleaving renin substrate
50 concentration
51 converting enzyme
52 decapeptide angiotensin I
53 derivative H-142
54 effect
55 electrolyte homeostasis2
56 endogenous human renin cleaving renin substrate
57 enzyme
58 equine angiotensinogen
59 extension
60 form
61 homeostasis2
62 human angiotensinogen
63 human cathepsin D
64 human plasma
65 human plasma renin
66 human renin
67 human renin cleaving renin substrate
68 hydrolysis
69 hypertension3
70 inhibitors
71 inhibitory effect
72 inhibitory potency
73 moiety —CH2—NH
74 new inhibitors
75 non-hydrolysable analogue
76 peptide bond
77 physiological role
78 plasma
79 plasma renin
80 plasma renin5
81 plasma substrate angiotensinogen
82 potency
83 potent new inhibitor
84 pressor octapeptide angiotensin II1
85 pressure
86 production
87 pros
88 protease
89 protease renin
90 reduction
91 renal acid protease
92 renal acid protease renin
93 renin
94 renin cleaving renin substrate
95 renin substrate
96 renin-angiotensin system
97 renin5
98 report
99 role
100 same approach
101 scissile Leu–Val bond
102 scissile peptide bond
103 selective inhibitor
104 sequence 2
105 sequence6
106 species
107 state
108 substrate
109 substrate angiotensinogen
110 system
111 terminal sequence6
112 terminus
113 terminus7
114 tetrahedral transition state
115 transition state
116 turn
117 weak inhibitor
118 schema:name Potent new inhibitors of human renin
119 schema:pagination 555-557
120 schema:productId N821ff01c285945b39c0e790c144c7459
121 Nc1666030231c4e8dafc73f95ad167f0b
122 Nf05647bc99a24eee86326c210a687094
123 schema:sameAs https://app.dimensions.ai/details/publication/pub.1010842288
124 https://doi.org/10.1038/299555a0
125 schema:sdDatePublished 2021-11-01T17:55
126 schema:sdLicense https://scigraph.springernature.com/explorer/license/
127 schema:sdPublisher N0729b120632948f6a2c47d9848e0ff38
128 schema:url https://doi.org/10.1038/299555a0
129 sgo:license sg:explorer/license/
130 sgo:sdDataset articles
131 rdf:type schema:ScholarlyArticle
132 N011fa460af0044ddbf3cd19485cb4ab4 rdf:first sg:person.0677134061.59
133 rdf:rest N5944fdb3861d47d9970bcc0d7c21d9b2
134 N0729b120632948f6a2c47d9848e0ff38 schema:name Springer Nature - SN SciGraph project
135 rdf:type schema:Organization
136 N12dae0cb175f42e3a7a7a4e5e3a4a632 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
137 schema:name Species Specificity
138 rdf:type schema:DefinedTerm
139 N134496567b7240a0a1630285195c5fbe rdf:first sg:person.01240176361.23
140 rdf:rest N011fa460af0044ddbf3cd19485cb4ab4
141 N4dd0635e05e84921a4771fea192b79fe schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
142 schema:name Peptide Fragments
143 rdf:type schema:DefinedTerm
144 N5944fdb3861d47d9970bcc0d7c21d9b2 rdf:first sg:person.01013362461.91
145 rdf:rest Nd7d930f656b444fba9f25558cbe9d38e
146 N734cdb9ff843468c8e599cfa8972a118 schema:issueNumber 5883
147 rdf:type schema:PublicationIssue
148 N812383c77951450db85c1495737cbae5 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
149 schema:name Stereoisomerism
150 rdf:type schema:DefinedTerm
151 N821ff01c285945b39c0e790c144c7459 schema:name pubmed_id
152 schema:value 6750410
153 rdf:type schema:PropertyValue
154 N8feaed34302f4c36aaa1f79e8601ac64 rdf:first sg:person.0671150441.95
155 rdf:rest Nb3a2be9820924d17b68cc3fe8d18240f
156 N9646ab022c334f768a276e319ebedc62 schema:volumeNumber 299
157 rdf:type schema:PublicationVolume
158 N9f2f6aad9dfe4d91b08b4e29214219af schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
159 schema:name Humans
160 rdf:type schema:DefinedTerm
161 Nb194d0df2d81474684341b823c19ed4e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
162 schema:name Amino Acid Sequence
163 rdf:type schema:DefinedTerm
164 Nb3a2be9820924d17b68cc3fe8d18240f rdf:first sg:person.010160653772.18
165 rdf:rest rdf:nil
166 Nc1666030231c4e8dafc73f95ad167f0b schema:name dimensions_id
167 schema:value pub.1010842288
168 rdf:type schema:PropertyValue
169 Nd7caae364fec4877b08d85a40b334920 rdf:first sg:person.0747520133.37
170 rdf:rest N134496567b7240a0a1630285195c5fbe
171 Nd7d930f656b444fba9f25558cbe9d38e rdf:first sg:person.01052301345.43
172 rdf:rest N8feaed34302f4c36aaa1f79e8601ac64
173 Nf05647bc99a24eee86326c210a687094 schema:name doi
174 schema:value 10.1038/299555a0
175 rdf:type schema:PropertyValue
176 Nf0acb417eb4d4c4497fe27a1cf0eb40a schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
177 schema:name Renin
178 rdf:type schema:DefinedTerm
179 Nf2f708e53f4d463db8b6743b55f25010 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
180 schema:name Substrate Specificity
181 rdf:type schema:DefinedTerm
182 Nf4b279f2191e4ba5871883ec5db3ed53 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
183 schema:name Angiotensinogen
184 rdf:type schema:DefinedTerm
185 Nf618204012784fe79aee70715d052d86 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
186 schema:name Cathepsins
187 rdf:type schema:DefinedTerm
188 Nf6f0c20ec60d40de95660383fb812de8 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
189 schema:name Protease Inhibitors
190 rdf:type schema:DefinedTerm
191 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
192 schema:name Biological Sciences
193 rdf:type schema:DefinedTerm
194 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
195 schema:name Biochemistry and Cell Biology
196 rdf:type schema:DefinedTerm
197 sg:journal.1018957 schema:issn 0028-0836
198 1476-4687
199 schema:name Nature
200 schema:publisher Springer Nature
201 rdf:type schema:Periodical
202 sg:person.01013362461.91 schema:affiliation grid-institutes:grid.7445.2
203 schema:familyName Jones
204 schema:givenName D. M.
205 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01013362461.91
206 rdf:type schema:Person
207 sg:person.010160653772.18 schema:affiliation grid-institutes:grid.7445.2
208 schema:familyName Lever
209 schema:givenName A. F.
210 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010160653772.18
211 rdf:type schema:Person
212 sg:person.01052301345.43 schema:affiliation grid-institutes:grid.7445.2
213 schema:familyName Sueiras
214 schema:givenName J.
215 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01052301345.43
216 rdf:type schema:Person
217 sg:person.01240176361.23 schema:affiliation grid-institutes:grid.7445.2
218 schema:familyName Leckie
219 schema:givenName B.
220 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01240176361.23
221 rdf:type schema:Person
222 sg:person.0671150441.95 schema:affiliation grid-institutes:grid.7445.2
223 schema:familyName Atrash
224 schema:givenName B.
225 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0671150441.95
226 rdf:type schema:Person
227 sg:person.0677134061.59 schema:affiliation grid-institutes:grid.7445.2
228 schema:familyName Hallett
229 schema:givenName A.
230 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0677134061.59
231 rdf:type schema:Person
232 sg:person.0747520133.37 schema:affiliation grid-institutes:grid.7445.2
233 schema:familyName Szelke
234 schema:givenName M.
235 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0747520133.37
236 rdf:type schema:Person
237 sg:pub.10.1038/217456a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1046041661
238 https://doi.org/10.1038/217456a0
239 rdf:type schema:CreativeWork
240 sg:pub.10.1038/291329a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1001285573
241 https://doi.org/10.1038/291329a0
242 rdf:type schema:CreativeWork
243 grid-institutes:grid.7445.2 schema:alternateName Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK
244 schema:name Department of Chemical Pathology, Royal Postgraduate Medical School, W12 0HS, London, UK
245 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...