Design and Development of Autotaxin Inhibitors

Autotaxin (ATX) is the only enzyme of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP2) family with lysophospholipase D (lysoPLD) activity, which is mainly responsible for the hydrolysis of extracellular lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA). LPA can induce vario...

Full description

Saved in:
Bibliographic Details
Published inPharmaceuticals (Basel, Switzerland) Vol. 14; no. 11; p. 1203
Main Authors Jia, Yi, Li, Yan, Xu, Xu-Dong, Tian, Yu, Shang, Hai
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 22.11.2021
MDPI
Subjects
Online AccessGet full text
ISSN1424-8247
1424-8247
DOI10.3390/ph14111203

Cover

Loading…
Abstract Autotaxin (ATX) is the only enzyme of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP2) family with lysophospholipase D (lysoPLD) activity, which is mainly responsible for the hydrolysis of extracellular lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA). LPA can induce various responses, such as cell proliferation, migration, and cytokine production, through six G protein-coupled receptors (LPA1-6). This signaling pathway is associated with metabolic and inflammatory disorder, and inhibiting this pathway has a positive effect on the treatment of related diseases, while ATX, as an important role in the production of LPA, has been shown to be associated with the occurrence and metastasis of tumors, fibrosis and cardiovascular diseases. From mimics of ATX natural lipid substrates to the rational design of small molecule inhibitors, ATX inhibitors have made rapid progress in structural diversity and design over the past 20 years, and three drugs, GLPG1690, BBT-877, and BLD-0409, have entered clinical trials. In this paper, we will review the structure of ATX inhibitors from the perspective of the transformation of design ideas, discuss the advantages and disadvantages of each inhibitor type, and put forward prospects for the development of ATX inhibitors in the future.
AbstractList Autotaxin (ATX) is the only enzyme of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP2) family with lysophospholipase D (lysoPLD) activity, which is mainly responsible for the hydrolysis of extracellular lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA). LPA can induce various responses, such as cell proliferation, migration, and cytokine production, through six G protein-coupled receptors (LPA1-6). This signaling pathway is associated with metabolic and inflammatory disorder, and inhibiting this pathway has a positive effect on the treatment of related diseases, while ATX, as an important role in the production of LPA, has been shown to be associated with the occurrence and metastasis of tumors, fibrosis and cardiovascular diseases. From mimics of ATX natural lipid substrates to the rational design of small molecule inhibitors, ATX inhibitors have made rapid progress in structural diversity and design over the past 20 years, and three drugs, GLPG1690, BBT-877, and BLD-0409, have entered clinical trials. In this paper, we will review the structure of ATX inhibitors from the perspective of the transformation of design ideas, discuss the advantages and disadvantages of each inhibitor type, and put forward prospects for the development of ATX inhibitors in the future.
Autotaxin (ATX) is the only enzyme of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP2) family with lysophospholipase D (lysoPLD) activity, which is mainly responsible for the hydrolysis of extracellular lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA). LPA can induce various responses, such as cell proliferation, migration, and cytokine production, through six G protein-coupled receptors (LPA1-6). This signaling pathway is associated with metabolic and inflammatory disorder, and inhibiting this pathway has a positive effect on the treatment of related diseases, while ATX, as an important role in the production of LPA, has been shown to be associated with the occurrence and metastasis of tumors, fibrosis and cardiovascular diseases. From mimics of ATX natural lipid substrates to the rational design of small molecule inhibitors, ATX inhibitors have made rapid progress in structural diversity and design over the past 20 years, and three drugs, GLPG1690, BBT-877, and BLD-0409, have entered clinical trials. In this paper, we will review the structure of ATX inhibitors from the perspective of the transformation of design ideas, discuss the advantages and disadvantages of each inhibitor type, and put forward prospects for the development of ATX inhibitors in the future.Autotaxin (ATX) is the only enzyme of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP2) family with lysophospholipase D (lysoPLD) activity, which is mainly responsible for the hydrolysis of extracellular lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA). LPA can induce various responses, such as cell proliferation, migration, and cytokine production, through six G protein-coupled receptors (LPA1-6). This signaling pathway is associated with metabolic and inflammatory disorder, and inhibiting this pathway has a positive effect on the treatment of related diseases, while ATX, as an important role in the production of LPA, has been shown to be associated with the occurrence and metastasis of tumors, fibrosis and cardiovascular diseases. From mimics of ATX natural lipid substrates to the rational design of small molecule inhibitors, ATX inhibitors have made rapid progress in structural diversity and design over the past 20 years, and three drugs, GLPG1690, BBT-877, and BLD-0409, have entered clinical trials. In this paper, we will review the structure of ATX inhibitors from the perspective of the transformation of design ideas, discuss the advantages and disadvantages of each inhibitor type, and put forward prospects for the development of ATX inhibitors in the future.
Author Jia, Yi
Tian, Yu
Shang, Hai
Li, Yan
Xu, Xu-Dong
AuthorAffiliation Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100193, China; jiayi_91@163.com (Y.J.); w19990921ly@163.com (Y.L.); xdxu@implad.ac.cn (X.-D.X.)
AuthorAffiliation_xml – name: Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100193, China; jiayi_91@163.com (Y.J.); w19990921ly@163.com (Y.L.); xdxu@implad.ac.cn (X.-D.X.)
Author_xml – sequence: 1
  givenname: Yi
  surname: Jia
  fullname: Jia, Yi
– sequence: 2
  givenname: Yan
  surname: Li
  fullname: Li, Yan
– sequence: 3
  givenname: Xu-Dong
  surname: Xu
  fullname: Xu, Xu-Dong
– sequence: 4
  givenname: Yu
  orcidid: 0000-0002-5997-1456
  surname: Tian
  fullname: Tian, Yu
– sequence: 5
  givenname: Hai
  surname: Shang
  fullname: Shang, Hai
BookMark eNptkUtrGzEQgEVIaRKnl_yChV5CwKkeo135Egh5GgK95C60q1lbZi25kjak_75yHJoHOWnQfPMxjyOy74NHQk4YPRdiRn9tlgwYY5yKPXLIgMNUcWj238UH5CilFaWyKeR3ciBACT5T8pCcX2NyC18Zb6trfMIhbNbocxX66nLMIZtn56u5X7rW5RDTMfnWmyHhj9d3Qh5vbx6v7qcPv-_mV5cP004ymafQ1iCFBMAauZEzMFSoXglTsrZTPRe0pdj3CiVF2wjJlWqtKgACdlRMyHyntcGs9Ca6tYl_dTBOv3yEuNAmZtcNqFEoU3QWTI0guG2FaAFUU1tFGQhWXBc712Zs12i7Ml00wwfpx4x3S70IT1rVnKuyqAk5fRXE8GfElPXapQ6HwXgMY9K8pkCpatQW_fkJXYUx-rKpLcUZ1EI2hTrbUV0MKUXs_zfDqN5eVL9dtMD0E9y5bLIL22bd8FXJP6NVoSQ
CitedBy_id crossref_primary_10_29413_ABS_2024_9_1_2
crossref_primary_10_1016_j_bmcl_2024_130006
crossref_primary_10_1097_MD_0000000000032599
crossref_primary_10_1021_acs_jmedchem_3c01827
crossref_primary_10_1126_scitranslmed_abk0135
crossref_primary_10_1016_j_molimm_2023_06_002
crossref_primary_10_1183_16000617_0015_2024
crossref_primary_10_3390_molecules27175487
crossref_primary_10_1186_s13395_025_00375_5
crossref_primary_10_1111_cas_15980
crossref_primary_10_1016_j_chembiol_2022_12_006
crossref_primary_10_1016_j_jcmgh_2022_07_012
crossref_primary_10_3390_cancers14215437
crossref_primary_10_1016_j_molstruc_2025_141573
crossref_primary_10_1055_a_1842_3378
crossref_primary_10_1186_s12967_024_05126_6
crossref_primary_10_1158_0008_5472_CAN_23_0104
crossref_primary_10_1016_j_bmc_2023_117374
Cites_doi 10.1007/s12035-019-01719-1
10.1016/j.biochi.2013.04.010
10.1021/acs.jmedchem.7b00647
10.1016/j.bmc.2007.11.018
10.1021/jm9012328
10.7555/JBR.30.20150058
10.1016/j.jacbts.2020.06.012
10.1021/acsmedchemlett.0c00200
10.1074/jbc.M007552200
10.1021/acs.jmedchem.7b00032
10.1016/j.ejmech.2020.112456
10.14218/JCTH.2020.00045
10.1074/jbc.M205623200
10.3390/nu10040399
10.1074/jbc.RA118.004450
10.1016/j.bmcl.2011.03.068
10.1016/j.ejmech.2020.112614
10.1038/nsmb.1980
10.1021/jm1005012
10.1016/j.ejmech.2018.02.049
10.1016/j.bioorg.2020.104188
10.1016/j.bmcl.2010.09.030
10.1016/j.ejmech.2019.111904
10.1038/nm1685
10.1242/jcs.02438
10.1016/j.bmc.2020.115795
10.1038/s41598-019-43576-x
10.1002/med.21551
10.1507/endocrj.EJ18-0451
10.1021/acsmedchemlett.6b00207
10.1021/jm049609r
10.1371/journal.pone.0226050
10.1016/j.bmcl.2016.10.036
10.1021/acs.jmedchem.6b01743
10.1016/j.bcp.2019.03.035
10.3390/molecules24152808
10.1371/journal.pone.0070941
10.1038/ncomms11248
10.1111/cas.14689
10.1042/bj3400677
10.1038/nsmb.1998
10.3390/molecules24193419
10.1016/j.plipres.2015.02.001
10.3390/ijms21165938
10.1128/MCB.02419-05
10.1021/cb400150c
10.1053/j.gastro.2010.05.009
10.1074/jbc.M112.358416
10.1021/acs.jmedchem.6b01270
10.1021/acs.jmedchem.0c00506
10.1124/mol.115.100404
10.1016/j.bmcl.2017.07.022
10.1016/S0021-9258(18)45911-X
10.1016/j.bmcl.2005.08.096
10.3390/cancers11111626
10.1038/s41598-021-81048-3
10.1002/prot.1152
10.1186/1476-4598-9-140
10.1096/fj.13-232868
10.1124/mol.63.5.1032
10.1124/mol.113.087080
10.1002/cmdc.201000425
10.1124/jpet.110.165845
10.1371/journal.pone.0143083
10.1111/febs.12674
10.1016/j.prostaglandins.2020.106471
10.1016/j.bmcl.2010.09.115
10.1021/acs.jmedchem.9b01967
10.1016/j.bmcl.2020.127663
10.1073/pnas.1001529107
10.1242/jcs.184424
10.1194/jlr.R046391
10.1021/acsmedchemlett.7b00312
10.1182/blood-2014-04-568683
10.1007/s11302-005-5303-4
10.1016/j.bmc.2018.02.023
10.1016/j.ab.2007.05.004
10.1158/1535-7163.MCT-08-0463
10.1016/j.canlet.2008.02.052
10.1021/jm200310q
10.1016/j.bmc.2019.115216
10.7717/peerj.10328
10.1021/acs.jmedchem.8b00232
10.1002/hep.28973
10.1186/s12876-021-01635-6
10.1021/ml4003106
10.1016/j.plipres.2007.02.001
10.1021/acs.jmedchem.6b01597
10.1093/jb/mvr126
10.3390/molecules25051107
10.1186/1476-511X-4-5
10.1124/jpet.116.237156
10.1021/cr2003213
10.1016/j.bmcl.2005.10.031
10.1016/j.ejps.2017.07.002
10.1016/j.jaut.2019.102327
ContentType Journal Article
Copyright 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
2021 by the authors. 2021
Copyright_xml – notice: 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: 2021 by the authors. 2021
DBID AAYXX
CITATION
3V.
7XB
8FK
8G5
ABUWG
AFKRA
AZQEC
BENPR
CCPQU
DWQXO
GNUQQ
GUQSH
M2O
MBDVC
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQQKQ
PQUKI
PRINS
Q9U
7X8
5PM
DOA
DOI 10.3390/ph14111203
DatabaseName CrossRef
ProQuest Central (Corporate)
ProQuest Central (purchase pre-March 2016)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Research Library
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
ProQuest Central Essentials
ProQuest Central
ProQuest One Community College
ProQuest Central Korea
ProQuest Central Student
ProQuest Research Library
ProQuest Research Library
Research Library (Corporate)
ProQuest Central Premium
ProQuest One Academic
Publicly Available Content Database
ProQuest One Academic Middle East (New)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
ProQuest Central Basic
MEDLINE - Academic
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle CrossRef
Publicly Available Content Database
Research Library Prep
ProQuest Central Student
ProQuest One Academic Middle East (New)
ProQuest Central Basic
ProQuest Central Essentials
ProQuest One Academic Eastern Edition
ProQuest Central (Alumni Edition)
ProQuest One Community College
Research Library (Alumni Edition)
ProQuest Central China
ProQuest Central
ProQuest One Academic UKI Edition
ProQuest Central Korea
ProQuest Research Library
ProQuest Central (New)
ProQuest One Academic
ProQuest One Academic (New)
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
CrossRef
Publicly Available Content Database

Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Pharmacy, Therapeutics, & Pharmacology
EISSN 1424-8247
ExternalDocumentID oai_doaj_org_article_e38a230d4a6e432db33b44876d801431
PMC8622848
10_3390_ph14111203
GroupedDBID ---
2WC
53G
5VS
8G5
AADQD
AAFWJ
AAYXX
ABDBF
ABUWG
ACGFO
ACIHN
ACUHS
ADBBV
AEAQA
AFKRA
AFPKN
AFZYC
ALMA_UNASSIGNED_HOLDINGS
AOIJS
AZQEC
BAWUL
BCNDV
BENPR
BPHCQ
CCPQU
CITATION
DIK
DWQXO
EBD
ESX
GNUQQ
GROUPED_DOAJ
GUQSH
GX1
HH5
HYE
IAO
IHR
ITC
KQ8
M2O
M48
MK0
MODMG
M~E
OK1
P2P
PGMZT
PHGZM
PHGZT
PIMPY
PQQKQ
PROAC
RPM
TUS
3V.
7XB
8FK
MBDVC
PKEHL
PQEST
PQUKI
PRINS
Q9U
7X8
5PM
PUEGO
ID FETCH-LOGICAL-c515t-4b6453544e6e2a594a038f83a515dc8f230b0eff8e50ed735288bd883ae4ec03
IEDL.DBID M48
ISSN 1424-8247
IngestDate Wed Aug 27 01:15:45 EDT 2025
Thu Aug 21 18:08:13 EDT 2025
Thu Jul 10 23:12:39 EDT 2025
Mon Jun 30 14:49:04 EDT 2025
Tue Jul 01 04:13:22 EDT 2025
Thu Apr 24 23:13:04 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 11
Language English
License https://creativecommons.org/licenses/by/4.0
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c515t-4b6453544e6e2a594a038f83a515dc8f230b0eff8e50ed735288bd883ae4ec03
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
ObjectType-Review-3
content type line 23
ORCID 0000-0002-5997-1456
OpenAccessLink https://doaj.org/article/e38a230d4a6e432db33b44876d801431
PMID 34832985
PQID 2602146357
PQPubID 2032350
ParticipantIDs doaj_primary_oai_doaj_org_article_e38a230d4a6e432db33b44876d801431
pubmedcentral_primary_oai_pubmedcentral_nih_gov_8622848
proquest_miscellaneous_2604008788
proquest_journals_2602146357
crossref_primary_10_3390_ph14111203
crossref_citationtrail_10_3390_ph14111203
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 20211122
PublicationDateYYYYMMDD 2021-11-22
PublicationDate_xml – month: 11
  year: 2021
  text: 20211122
  day: 22
PublicationDecade 2020
PublicationPlace Basel
PublicationPlace_xml – name: Basel
PublicationTitle Pharmaceuticals (Basel, Switzerland)
PublicationYear 2021
Publisher MDPI AG
MDPI
Publisher_xml – name: MDPI AG
– name: MDPI
References Parrill (ref_60) 2008; 16
Desroy (ref_87) 2017; 60
ref_12
ref_96
ref_95
Jethwa (ref_25) 2016; 129
Stefan (ref_1) 2006; 2
Li (ref_69) 2020; 203
Bourgeois (ref_30) 2020; 5
Gerokonstantis (ref_72) 2020; 28
Iwaki (ref_67) 2020; 11
Albers (ref_63) 2010; 107
Nojiri (ref_27) 2019; 66
Fukui (ref_39) 2020; 150
Brinkmann (ref_54) 2008; 266
ref_26
Thomson (ref_97) 2021; 31
Clair (ref_46) 2005; 4
Jiang (ref_56) 2011; 21
Stracke (ref_2) 1992; 267
Matralis (ref_3) 2019; 39
Albers (ref_64) 2011; 54
Hashimoto (ref_20) 2011; 151
Fells (ref_78) 2014; 281
Balupuri (ref_76) 2017; 27
Sakai (ref_35) 2019; 9
Bain (ref_82) 2016; 360
Lei (ref_91) 2020; 63
Magkrioti (ref_41) 2019; 104
Fish (ref_24) 2018; 293
Jinno (ref_33) 2021; 112
Leblanc (ref_18) 2014; 124
Albers (ref_62) 2010; 53
Stein (ref_81) 2015; 88
Joncour (ref_86) 2017; 60
Ruurs (ref_40) 2006; 26
Virag (ref_47) 2003; 63
East (ref_58) 2010; 20
Fisher (ref_55) 2014; 5
Fells (ref_77) 2013; 84
Shah (ref_84) 2016; 26
Perrakis (ref_16) 2014; 55
Rahman (ref_31) 2020; 8
Houben (ref_15) 2013; 288
ref_53
Kuttruff (ref_70) 2017; 8
Rancoule (ref_75) 2014; 96
Benesch (ref_10) 2016; 30
Pantsar (ref_85) 2017; 107
Altman (ref_52) 2010; 9
Banerjee (ref_80) 2020; 103
Jia (ref_93) 2020; 28
Durgam (ref_49) 2006; 16
Gududuru (ref_50) 2006; 16
Zhao (ref_34) 2019; 164
Moolenaar (ref_7) 2007; 46
Keune (ref_23) 2016; 7
Hoeglund (ref_61) 2010; 53
Nakamura (ref_5) 2007; 367
ref_66
Nie (ref_29) 2020; 8
Durgam (ref_48) 2005; 48
Miller (ref_83) 2017; 60
Wu (ref_19) 2014; 28
Jansen (ref_17) 2005; 118
Jasinska (ref_6) 1999; 340
Jing (ref_89) 2018; 26
Kremer (ref_11) 2010; 139
Nishimasu (ref_22) 2011; 18
ref_36
Jones (ref_71) 2016; 7
Kawaguchi (ref_94) 2020; 63
ref_32
Gierse (ref_74) 2010; 334
Tokumura (ref_4) 2002; 277
Herr (ref_38) 2020; 57
Tager (ref_8) 2008; 14
ref_37
Lei (ref_92) 2020; 201
Galperin (ref_43) 2001; 45
Jiang (ref_90) 2019; 187
Gupte (ref_51) 2010; 20
Kawaguchi (ref_65) 2013; 8
Gijsbers (ref_44) 2001; 276
Barbayianni (ref_13) 2015; 58
Gupte (ref_57) 2011; 6
Banerjee (ref_79) 2017; 60
Nikolaou (ref_68) 2018; 61
Igarashi (ref_28) 2021; 11
Balupuri (ref_73) 2018; 148
Hausmann (ref_21) 2011; 18
ref_42
Clair (ref_45) 2003; 63
Albers (ref_14) 2012; 112
Saunders (ref_59) 2008; 7
Keune (ref_88) 2017; 60
Kaffe (ref_9) 2017; 65
References_xml – volume: 57
  start-page: 372
  year: 2020
  ident: ref_38
  article-title: Pleotropic Roles of Autotaxin in the Nervous System Present Opportunities for the Development of Novel Therapeutics for Neurological Diseases
  publication-title: Mol. Neurobiol.
  doi: 10.1007/s12035-019-01719-1
– volume: 96
  start-page: 140
  year: 2014
  ident: ref_75
  article-title: Involvement of autotaxin/lysophosphatidic acid signaling in obesity and impaired glucose homeostasis
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2013.04.010
– volume: 60
  start-page: 7371
  year: 2017
  ident: ref_86
  article-title: Discovery, Structure–Activity Relationship, and Binding Mode of an Imidazo[1,2-a]pyridine Series of Autotaxin Inhibitors
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.7b00647
– volume: 16
  start-page: 1784
  year: 2008
  ident: ref_60
  article-title: Virtual screening approaches for the identification of non-lipid autotaxin inhibitors
  publication-title: Bioorg. Med. Chem.
  doi: 10.1016/j.bmc.2007.11.018
– volume: 53
  start-page: 1056
  year: 2010
  ident: ref_61
  article-title: Optimization of a Pipemidic Acid Autotaxin Inhibitor
  publication-title: J. Med. Chem.
  doi: 10.1021/jm9012328
– volume: 30
  start-page: 272
  year: 2016
  ident: ref_10
  article-title: Recent advances in targeting the autotaxin-lysophosphatidate-lipid phosphate phosphatase axis in vivo
  publication-title: J. Biomed. Res.
  doi: 10.7555/JBR.30.20150058
– volume: 5
  start-page: 888
  year: 2020
  ident: ref_30
  article-title: Interaction of Autotaxin with Lipoprotein(a) in Patients with Calcific Aortic Valve Stenosis
  publication-title: JACC Basic Transl. Sci.
  doi: 10.1016/j.jacbts.2020.06.012
– volume: 11
  start-page: 1335
  year: 2020
  ident: ref_67
  article-title: ONO-8430506: A Novel Autotaxin Inhibitor That Enhances the Antitumor Effect of Paclitaxel in a Breast Cancer Model
  publication-title: ACS Med. Chem. Lett.
  doi: 10.1021/acsmedchemlett.0c00200
– volume: 276
  start-page: 1361
  year: 2001
  ident: ref_44
  article-title: Structural and Catalytic Similarities between Nucleotide Pyrophosphatases/Phosphodiesterases and Alkaline Phosphatases
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M007552200
– volume: 60
  start-page: 3580
  year: 2017
  ident: ref_87
  article-title: Discovery of 2-[[2-Ethyl-6-[4-[2-(3-hydroxyazetidin-1-yl)-2-oxoethyl]piperazin-1-yl]-8-methylimidazo[1,2-a]pyridin-3-yl]methylamino]-4-(4-fluorophenyl)thiazole-5-carbonitrile (GLPG1690), a First-in-Class Autotaxin Inhibitor Undergoing Clinical Evaluation for the Treatment of Idiopathic Pulmonary Fibrosis
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.7b00032
– volume: 201
  start-page: 112456
  year: 2020
  ident: ref_92
  article-title: Structure guided design of potent indole-based ATX inhibitors bearing hydrazone moiety with tumor suppression effects
  publication-title: Eur. J. Med. Chem.
  doi: 10.1016/j.ejmech.2020.112456
– volume: 8
  start-page: 240
  year: 2020
  ident: ref_29
  article-title: Autotaxin: An Early Warning Biomarker for Acute-on-chronic Liver Failure
  publication-title: J. Clin. Transl. Hepatol.
  doi: 10.14218/JCTH.2020.00045
– volume: 277
  start-page: 39436
  year: 2002
  ident: ref_4
  article-title: Identification of Human Plasma Lysophospholipase D, a Lysophosphatidic Acid-producing Enzyme, as Autotaxin, a Multifunctional Phosphodiesterase
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M205623200
– ident: ref_12
  doi: 10.3390/nu10040399
– volume: 293
  start-page: 14312
  year: 2018
  ident: ref_24
  article-title: Lysophosphatidic acid produced by autotaxin acts as an allosteric modulator of its catalytic efficiency
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.RA118.004450
– volume: 21
  start-page: 5098
  year: 2011
  ident: ref_56
  article-title: Aromatic phosphonates inhibit the lysophospholipase D activity of autotaxin
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2011.03.068
– volume: 203
  start-page: 112614
  year: 2020
  ident: ref_69
  article-title: Design and synthesis of Leukotriene A4 hydrolase inhibitors to alleviate idiopathic pulmonary fibrosis and acute lung injury
  publication-title: Eur. J. Med. Chem.
  doi: 10.1016/j.ejmech.2020.112614
– volume: 18
  start-page: 198
  year: 2011
  ident: ref_21
  article-title: Structural basis of substrate discrimination and integrin binding by autotaxin
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1980
– volume: 53
  start-page: 4958
  year: 2010
  ident: ref_62
  article-title: Discovery and Optimization of Boronic Acid Based Inhibitors of Autotaxin
  publication-title: J. Med. Chem.
  doi: 10.1021/jm1005012
– volume: 148
  start-page: 397
  year: 2018
  ident: ref_73
  article-title: Discovery and optimization of ATX inhibitors via modeling, synthesis and biological evaluation
  publication-title: Eur. J. Med. Chem.
  doi: 10.1016/j.ejmech.2018.02.049
– volume: 103
  start-page: 104188
  year: 2020
  ident: ref_80
  article-title: Molecular modelling guided design, synthesis and QSAR analysis of new small molecule non-lipid autotaxin inhibitors
  publication-title: Bioorg. Chem.
  doi: 10.1016/j.bioorg.2020.104188
– volume: 20
  start-page: 7132
  year: 2010
  ident: ref_58
  article-title: Synthesis and structure–activity relationships of tyrosine-based inhibitors of autotaxin (ATX)
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2010.09.030
– volume: 187
  start-page: 111904
  year: 2019
  ident: ref_90
  article-title: Optimization and evaluation of novel tetrahydropyrido[4,3-d]pyrimidine derivatives as ATX inhibitors for cardiac and hepatic fibrosis
  publication-title: Eur. J. Med. Chem.
  doi: 10.1016/j.ejmech.2019.111904
– volume: 14
  start-page: 45
  year: 2008
  ident: ref_8
  article-title: The lysophosphatidic acid receptor LPA1 links pulmonary fibrosis to lung injury by mediating fibroblast recruitment and vascular leak
  publication-title: Nat. Med.
  doi: 10.1038/nm1685
– volume: 118
  start-page: 3081
  year: 2005
  ident: ref_17
  article-title: Proteolytic maturation and activation of autotaxin (NPP2), a secreted metastasis-enhancing lysophospholipase D
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.02438
– volume: 28
  start-page: 115795
  year: 2020
  ident: ref_93
  article-title: Structure-based linker exploration: Discovery of 1-ethyl-1H-indole analogs as novel ATX inhibitors
  publication-title: Bioorg. Med. Chem.
  doi: 10.1016/j.bmc.2020.115795
– volume: 9
  start-page: 7414
  year: 2019
  ident: ref_35
  article-title: The involvement of autotaxin in renal interstitial fibrosis through regulation of fibroblast functions and induction of vascular leakage
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-019-43576-x
– volume: 39
  start-page: 976
  year: 2019
  ident: ref_3
  article-title: Development and therapeutic potential of autotaxin small molecule inhibitors: From bench to advanced clinical trials
  publication-title: Med. Res. Rev.
  doi: 10.1002/med.21551
– volume: 66
  start-page: 409
  year: 2019
  ident: ref_27
  article-title: Serum autotaxin levels are associated with Graves’ disease
  publication-title: Endocr. J.
  doi: 10.1507/endocrj.EJ18-0451
– volume: 7
  start-page: 857
  year: 2016
  ident: ref_71
  article-title: Novel Autotaxin Inhibitors for the Treatment of Osteoarthritis Pain: Lead Optimization via Structure-Based Drug Design
  publication-title: ACS Med. Chem. Lett.
  doi: 10.1021/acsmedchemlett.6b00207
– volume: 48
  start-page: 4919
  year: 2005
  ident: ref_48
  article-title: Synthesis, Structure−Activity Relationships, and Biological Evaluation of Fatty Alcohol Phosphates as Lysophosphatidic Acid Receptor Ligands, Activators of PPARγ, and Inhibitors of Autotaxin
  publication-title: J. Med. Chem.
  doi: 10.1021/jm049609r
– ident: ref_37
  doi: 10.1371/journal.pone.0226050
– volume: 26
  start-page: 5403
  year: 2016
  ident: ref_84
  article-title: Discovery of potent inhibitors of the lysophospholipase autotaxin
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2016.10.036
– volume: 60
  start-page: 2006
  year: 2017
  ident: ref_88
  article-title: Rational Design of Autotaxin Inhibitors by Structural Evolution of Endogenous Modulators
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.6b01743
– volume: 164
  start-page: 74
  year: 2019
  ident: ref_34
  article-title: Targeting the autotaxin-Lysophosphatidic acid receptor axis in cardiovascular diseases
  publication-title: Biochem. Pharmacol.
  doi: 10.1016/j.bcp.2019.03.035
– ident: ref_96
  doi: 10.3390/molecules24152808
– ident: ref_53
  doi: 10.1371/journal.pone.0070941
– volume: 7
  start-page: 1
  year: 2016
  ident: ref_23
  article-title: Steroid binding to Autotaxin links bile salts and lysophosphatidic acid signalling
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms11248
– volume: 112
  start-page: 668
  year: 2021
  ident: ref_33
  article-title: Autotaxin in ascites promotes peritoneal dissemination in pancreatic cancer
  publication-title: Cancer Sci.
  doi: 10.1111/cas.14689
– volume: 340
  start-page: 677
  year: 1999
  ident: ref_6
  article-title: Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters
  publication-title: Biochem. J.
  doi: 10.1042/bj3400677
– volume: 18
  start-page: 205
  year: 2011
  ident: ref_22
  article-title: Crystal structure of autotaxin and insight into GPCR activation by lipid mediators
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1998
– ident: ref_66
  doi: 10.3390/molecules24193419
– volume: 58
  start-page: 76
  year: 2015
  ident: ref_13
  article-title: Autotaxin, a secreted lysophospholipase D, as a promising therapeutic target in chronic inflammation and cancer
  publication-title: Prog. Lipid Res.
  doi: 10.1016/j.plipres.2015.02.001
– ident: ref_32
  doi: 10.3390/ijms21165938
– volume: 26
  start-page: 5015
  year: 2006
  ident: ref_40
  article-title: Autotaxin, a Secreted Lysophospholipase D, Is Essential for Blood Vessel Formation during Development
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.02419-05
– volume: 8
  start-page: 1713
  year: 2013
  ident: ref_65
  article-title: Screening and X-ray Crystal Structure-based Optimization of Autotaxin (ENPP2) Inhibitors, Using a Newly Developed Fluorescence Probe
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb400150c
– volume: 139
  start-page: 1008
  year: 2010
  ident: ref_11
  article-title: Lysophosphatidic Acid Is a Potential Mediator of Cholestatic Pruritus
  publication-title: Gastroenterology
  doi: 10.1053/j.gastro.2010.05.009
– volume: 288
  start-page: 510
  year: 2013
  ident: ref_15
  article-title: The polybasic insertion in autotaxin α confers specific binding to heparin and cell surface heparan sulfate proteoglycans
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M112.358416
– volume: 60
  start-page: 1309
  year: 2017
  ident: ref_79
  article-title: Highly Potent Non-Carboxylic Acid Autotaxin Inhibitors Reduce Melanoma Metastasis and Chemotherapeutic Resistance of Breast Cancer Stem Cells
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.6b01270
– volume: 63
  start-page: 7326
  year: 2020
  ident: ref_91
  article-title: Discovery of Novel Indole-Based Allosteric Highly Potent ATX Inhibitors with Great In Vivo Efficacy in a Mouse Lung Fibrosis Model
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.0c00506
– volume: 88
  start-page: 982
  year: 2015
  ident: ref_81
  article-title: Structural Basis for Inhibition of Human Autotaxin by Four Potent Compounds with Distinct Modes of Binding
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.115.100404
– volume: 27
  start-page: 4156
  year: 2017
  ident: ref_76
  article-title: Design, synthesis, docking and biological evaluation of 4-phenyl-thiazole derivatives as autotaxin (ATX) inhibitors
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2017.07.022
– volume: 267
  start-page: 2524
  year: 1992
  ident: ref_2
  article-title: Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)45911-X
– volume: 16
  start-page: 451
  year: 2006
  ident: ref_50
  article-title: Identification of Darmstoff analogs as selective agonists and antagonists of lysophosphatidic acid receptors
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2005.08.096
– ident: ref_36
  doi: 10.3390/cancers11111626
– volume: 11
  start-page: 1408
  year: 2021
  ident: ref_28
  article-title: Aqueous autotaxin and TGF-βs are promising diagnostic biomarkers for distinguishing open-angle glaucoma subtypes
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-021-81048-3
– volume: 45
  start-page: 318
  year: 2001
  ident: ref_43
  article-title: Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes
  publication-title: Proteins Struct. Funct. Bioinform.
  doi: 10.1002/prot.1152
– volume: 9
  start-page: 1
  year: 2010
  ident: ref_52
  article-title: Targeting melanoma growth and viability reveals dualistic functionality of the phosphonothionate analogue of carba cyclic phosphatidic acid
  publication-title: Mol. Cancer
  doi: 10.1186/1476-4598-9-140
– volume: 28
  start-page: 861
  year: 2014
  ident: ref_19
  article-title: Integrin-mediated cell surface recruitment of autotaxin promotes persistent directional cell migration
  publication-title: FASEB J.
  doi: 10.1096/fj.13-232868
– volume: 63
  start-page: 1032
  year: 2003
  ident: ref_47
  article-title: Fatty Alcohol Phosphates are Subtype-Selective Agonists and Antagonists of Lysophosphatidic Acid Receptors
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.63.5.1032
– volume: 84
  start-page: 415
  year: 2013
  ident: ref_77
  article-title: Hits of a High-Throughput Screen Identify the Hydrophobic Pocket of Autotaxin/Lysophospholipase D As an Inhibitory Surface
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.113.087080
– volume: 6
  start-page: 922
  year: 2011
  ident: ref_57
  article-title: Benzyl and Naphthalene Methylphosphonic Acid Inhibitors of Autotaxin with Anti-invasive and Anti-metastatic Activity
  publication-title: ChemMedChem
  doi: 10.1002/cmdc.201000425
– volume: 334
  start-page: 310
  year: 2010
  ident: ref_74
  article-title: A Novel Autotaxin Inhibitor Reduces Lysophosphatidic Acid Levels in Plasma and the Site of Inflammation
  publication-title: J. Pharmacol. Exp. Ther.
  doi: 10.1124/jpet.110.165845
– ident: ref_42
  doi: 10.1371/journal.pone.0143083
– volume: 281
  start-page: 1017
  year: 2014
  ident: ref_78
  article-title: Targeting the hydrophobic pocket of autotaxin with virtual screening of inhibitors identifies a common aromatic sulfonamide structural motif
  publication-title: FEBS J.
  doi: 10.1111/febs.12674
– volume: 150
  start-page: 106471
  year: 2020
  ident: ref_39
  article-title: Distinct contributions of two choline-producing enzymatic activities to lysophosphatidic acid production in human amniotic fluid from pregnant women in the second trimester and after parturition
  publication-title: Prostaglandins Other Lipid Mediat.
  doi: 10.1016/j.prostaglandins.2020.106471
– volume: 20
  start-page: 7525
  year: 2010
  ident: ref_51
  article-title: Synthesis and pharmacological evaluation of the stereoisomers of 3-carba cyclic-phosphatidic acid
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2010.09.115
– volume: 63
  start-page: 3188
  year: 2020
  ident: ref_94
  article-title: Identification of Potent In Vivo Autotaxin Inhibitors that Bind to Both Hydrophobic Pockets and Channels in the Catalytic Domain
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.9b01967
– volume: 31
  start-page: 127663
  year: 2021
  ident: ref_97
  article-title: Development of autotaxin inhibitors: A series of tetrazole cinnamides
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2020.127663
– volume: 107
  start-page: 7257
  year: 2010
  ident: ref_63
  article-title: Boronic acid-based inhibitor of autotaxin reveals rapid turnover of LPA in the circulation
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1001529107
– volume: 129
  start-page: 3948
  year: 2016
  ident: ref_25
  article-title: Exosomes bind autotaxin and act as a physiological delivery mechanism to stimulate LPA receptor signalling in cells
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.184424
– volume: 55
  start-page: 1010
  year: 2014
  ident: ref_16
  article-title: Autotaxin: Structure-function and signaling
  publication-title: J. Lipid Res.
  doi: 10.1194/jlr.R046391
– volume: 8
  start-page: 1252
  year: 2017
  ident: ref_70
  article-title: Discovery of BI-2545: A Novel Autotaxin Inhibitor That Significantly Reduces LPA Levels in Vivo
  publication-title: ACS Med. Chem. Lett.
  doi: 10.1021/acsmedchemlett.7b00312
– volume: 124
  start-page: 3141
  year: 2014
  ident: ref_18
  article-title: Interaction of platelet-derived autotaxin with tumor integrin αVβ3 controls metastasis of breast cancer cells to bone
  publication-title: Blood
  doi: 10.1182/blood-2014-04-568683
– volume: 2
  start-page: 361
  year: 2006
  ident: ref_1
  article-title: Modulation of purinergic signaling by NPP-type ectophosphodiesterases
  publication-title: Purinergic Signal.
  doi: 10.1007/s11302-005-5303-4
– volume: 26
  start-page: 1784
  year: 2018
  ident: ref_89
  article-title: Discovery and optimization of tetrahydropyrido[4,3-d]pyrimidine derivatives as novel ATX and EGFR dual inhibitors
  publication-title: Bioorg. Med. Chem.
  doi: 10.1016/j.bmc.2018.02.023
– volume: 367
  start-page: 20
  year: 2007
  ident: ref_5
  article-title: Suppression of lysophosphatidic acid and lysophosphatidylcholine formation in the plasma in vitro: Proposal of a plasma sample preparation method for laboratory testing of these lipids
  publication-title: Anal. Biochem.
  doi: 10.1016/j.ab.2007.05.004
– volume: 7
  start-page: 3352
  year: 2008
  ident: ref_59
  article-title: Identification of small-molecule inhibitors of autotaxin that inhibit melanoma cell migration and invasion
  publication-title: Mol. Cancer Ther.
  doi: 10.1158/1535-7163.MCT-08-0463
– volume: 266
  start-page: 203
  year: 2008
  ident: ref_54
  article-title: Anticancer activity of FTY720: Phosphorylated FTY720 inhibits autotaxin, a metastasis-enhancing and angiogenic lysophospholipase D
  publication-title: Cancer Lett.
  doi: 10.1016/j.canlet.2008.02.052
– volume: 54
  start-page: 4619
  year: 2011
  ident: ref_64
  article-title: Structure-Based Design of Novel Boronic Acid-Based Inhibitors of Autotaxin
  publication-title: J. Med. Chem.
  doi: 10.1021/jm200310q
– volume: 28
  start-page: 115216
  year: 2020
  ident: ref_72
  article-title: Synthesis of novel 2-pyrrolidinone and pyrrolidine derivatives and study of their inhibitory activity against autotaxin enzyme
  publication-title: Bioorg. Med. Chem.
  doi: 10.1016/j.bmc.2019.115216
– volume: 63
  start-page: 5446
  year: 2003
  ident: ref_45
  article-title: Autotaxin hydrolyzes sphingosylphosphorylcholine to produce the regulator of migration, sphingosine-1-phosphate
  publication-title: Cancer Res.
– volume: 8
  start-page: e10328
  year: 2020
  ident: ref_31
  article-title: Deregulation of lysophosphatidic acid metabolism in oral cancer promotes cell migration via the up-regulation of COX-2
  publication-title: PeerJ
  doi: 10.7717/peerj.10328
– volume: 61
  start-page: 3697
  year: 2018
  ident: ref_68
  article-title: Hydroxamic Acids Constitute a Novel Class of Autotaxin Inhibitors that Exhibit in Vivo Efficacy in a Pulmonary Fibrosis Model
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.8b00232
– volume: 65
  start-page: 1369
  year: 2017
  ident: ref_9
  article-title: Hepatocyte autotaxin expression promotes liver fibrosis and cancer
  publication-title: Hepatology
  doi: 10.1002/hep.28973
– ident: ref_26
  doi: 10.1186/s12876-021-01635-6
– volume: 5
  start-page: 34
  year: 2014
  ident: ref_55
  article-title: Dendrimer Conjugate of [4-(Tetradecanoylamino)benzyl]phosphonic Acid (S32826) as an Autotaxin Inhibitor
  publication-title: ACS Med. Chem. Lett.
  doi: 10.1021/ml4003106
– volume: 46
  start-page: 145
  year: 2007
  ident: ref_7
  article-title: Regulation and biological activities of the autotaxin-LPA axis
  publication-title: Prog. Lipid Res.
  doi: 10.1016/j.plipres.2007.02.001
– volume: 60
  start-page: 722
  year: 2017
  ident: ref_83
  article-title: Structure–Activity Relationships of Small Molecule Autotaxin Inhibitors with a Discrete Binding Mode
  publication-title: J. Med. Chem.
  doi: 10.1021/acs.jmedchem.6b01597
– volume: 151
  start-page: 89
  year: 2011
  ident: ref_20
  article-title: Identification and biochemical characterization of a novel autotaxin isoform, ATX, with a four-amino acid deletion
  publication-title: J. Biochem.
  doi: 10.1093/jb/mvr126
– ident: ref_95
  doi: 10.3390/molecules25051107
– volume: 4
  start-page: 1
  year: 2005
  ident: ref_46
  article-title: L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine, autotaxin
  publication-title: Lipids Health Dis.
  doi: 10.1186/1476-511X-4-5
– volume: 360
  start-page: 1
  year: 2016
  ident: ref_82
  article-title: Selective Inhibition of Autotaxin Is Efficacious in Mouse Models of Liver Fibrosis
  publication-title: J. Pharmacol. Exp. Ther.
  doi: 10.1124/jpet.116.237156
– volume: 112
  start-page: 2593
  year: 2012
  ident: ref_14
  article-title: Chemical Evolution of Autotaxin Inhibitors
  publication-title: Chem. Rev.
  doi: 10.1021/cr2003213
– volume: 16
  start-page: 633
  year: 2006
  ident: ref_49
  article-title: Synthesis and pharmacological evaluation of second-generation phosphatidic acid derivatives as lysophosphatidic acid receptor ligands
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2005.10.031
– volume: 107
  start-page: 97
  year: 2017
  ident: ref_85
  article-title: Design, synthesis, and biological evaluation of 2,4-dihydropyrano[2,3-c]pyrazole derivatives as autotaxin inhibitors
  publication-title: Eur. J. Pharm. Sci.
  doi: 10.1016/j.ejps.2017.07.002
– volume: 104
  start-page: 102327
  year: 2019
  ident: ref_41
  article-title: Autotaxin and chronic inflammatory diseases
  publication-title: J. Autoimmun.
  doi: 10.1016/j.jaut.2019.102327
SSID ssj0057141
Score 2.3761413
SecondaryResourceType review_article
Snippet Autotaxin (ATX) is the only enzyme of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP2) family with lysophospholipase D (lysoPLD) activity, which...
SourceID doaj
pubmedcentral
proquest
crossref
SourceType Open Website
Open Access Repository
Aggregation Database
Enrichment Source
Index Database
StartPage 1203
SubjectTerms Amino acids
autotaxin
Binding sites
Cancer
Cell growth
development
Disease
inhibitor
Lipids
lysophosphatidic acid
Melanoma
Metabolism
Motility
Nervous system
Physiology
Pruritus
Review
structure design
Zinc
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1LS8QwEA7iyYv4xPoiogiC1TaPNh59ooLiYQVvJY8JuyDdRbug_95J230UBC8e28wh_SbpzEcm3xByZEWe-IxDzB2DWBgPsU6tjI3jOk2sEqY-inl6zu5fxeObfJtr9RVqwhp54Aa4c-BKY5rshM5AcOYM5wYpRZ65oHtS36BmGPMmZKr5B8s8FWkjRsqR1J-P-viMmcWkNVYbfmqV_k5q2S2MnIs0dytkuU0R6WUztVWyAOUaOX5pNKa_T2lvdmXq85Qe05eZ-vT3Ojm7qWsyqC4dnasIokNPL8fVsNJfg5I-lP2BGYRGOxukd3fbu76P26YIscXUo0I4MyG5FAIyYFpeCJ1w5RXXOOqs8oiVScB7BTIBlwfxFmWcQgMQYBO-SRbLYQlbhDLkWnmqM55KLaxHGyGtUACMG66Uj8jJBKrCtoLhoW_Fe4HEIcBazGCNyOHUdtTIZPxqdRUQn1oEaev6BTq8aB1e_OXwiOxO_FW0--2zQFYWOpRzmUfkYDqMOyUcf-gShuPaRgQFPqUiknf83JlQd6Qc9GvNbSR-GMjV9n98wQ5ZYqEyJk1jxnbJYvUxhj1MbSqzX6_iH3mT9nU
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Central
  dbid: BENPR
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1La9wwEBZpcumltE1L3KZFISFQiBPLkmzlFPIkKTQsZQu5GT1G3YVib7NeaP59R155N4bSo60B26OZ0Yw0_j5CDqwoM19wSLnLIRXGQ6qZlalxXLPMKmG6o5hv98XtD_H1QT7EDbd5bKvsY2IXqF1jwx75CebdgYOay_Js9jsNrFHhdDVSaLwgWxiCFVr41sX1_eh7H4tlyQRbgpJyLO5PZhO8xgyjp8iKy1CH1j9IMYcNks9WnJvX5FVMFen5cm7fkA2o35LD0RJr-umIjte_Ts2P6CEdrVGon7bJ8VXXm0F17eizziDaeHq-aJtW_5nW9K6eTM00EO68I-Ob6_HlbRrJEVKLKUiLai2E5FIIKCDX8lTojCuvuMZRZ5XH0sJk4L0CmYErA4iLMk6hAAiwGX9PNuumhh1Cc6y5SqYLzqQW1qOMkFYogJwbrpRPyJdeVZWNwOGBv-JXhQVEUGu1VmtC9leysyVcxj-lLoLGVxIB4rq70Tz-rKLHVMCVxo9wQhcgeO4M5wZrybJwAfCGs4Ts9vNVRb-bV2srScjeahg9JhyD6BqaRScjAhKfUgkpB_M8eKHhSD2ddNjbWADigq4-_P_hH8nLPPS-MJbm-S7ZbB8X8AmTl9Z8jhb6F5G88HM
  priority: 102
  providerName: ProQuest
Title Design and Development of Autotaxin Inhibitors
URI https://www.proquest.com/docview/2602146357
https://www.proquest.com/docview/2604008788
https://pubmed.ncbi.nlm.nih.gov/PMC8622848
https://doaj.org/article/e38a230d4a6e432db33b44876d801431
Volume 14
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1La9wwEBYhufRS-qRuk0WlJVCIU1sPSz2UkrQJaSFhKRvIzegx6i4EO914IfvvM7K9u3HJoVdrDNZIw8xnjb6PkI9OqCwUHFLuGaTCBkhN7mRqPTd55rSw7VHM-UVxdil-XcmrLbLS7-wdePsotIt6Upfz68O7v8tvGPBfI-JEyP75ZpoLDFkWST93MCOpKOFwLtanCVJ1CpbxUleqmVAdTek_7w4SU8vfPyg6hy2TD3LQ6TPytC8e6VG32s_JFlQvyP64Y59eHtDJ5jLV7QHdp-MNL_XyJTn80XZrUFN5-qBXiNaBHi2aujF3s4r-rKYzO4sSPK_I5PRk8v0s7eUSUodFSYOOLoTkUggogBn5RZiM66C5wVHvdECwYTMIQYPMwKtI66Kt12gAAlzGX5Ptqq7gDaEMUZjKTcFzaYQLaCOkExqAccu1Dgn5tHJV6Xoq8ahocV0ipIhuLTduTciHte1NR6DxqNVx9PjaIpJetw_q-Z-yj6ESuDY4CS9MAYIzbzm3iC5V4SMFDs8Tsrtar3K1kUrEa1G7nEuVkPfrYYyheDBiKqgXrY2I3HxaJ0QN1nnwQcORajZt2bgREmKK12__a57vyBMWm2LyPGVsl2w38wXsYVXT2BHZOT65GP8etX8FRu0Gvge8YvcO
linkProvider Scholars Portal
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEB6V9AAXxFMYCiwCKiHVrb0Pe3tAqKWtEtpGEQpSb9a-TCIhOzSJID-K_8isH0ktIW492juy17Mzu994Z78BeGd4GuUJcyGz1IVc5y5UsRGhtkzFkZFcV1sxl8Ok_41_uRJXW_CnPQvj0yrbObGaqG1p_D_yA8TdvgY1E-mn2c_QV43yu6ttCY3aLM7d6heGbPOPgxMc3_eUnp2OP_fDpqpAaHDtXmB_Ei6Y4NwljipxyFXEZC6ZwlZrZI6YXEcuz6UTkbOpZz-R2koUcNyZiOFj78A2Z4gUerB9fDocfW2nfpHGPK45UBk7jA5mE7xGQNNW5GpWvao4QAfRdvMxbyxwZw_gfoNMyVFtSg9hyxWPYHdUU1uv9sh4c1Jrvkd2yWhDer16DPsnVSoIUYUlNxKRSJmTo-WiXKjf04IMislUT319nycwvg2tPYVeURbuGRCKIV4aq4TFQnGTowwXhkvnKNNMyjyAD62qMtPwlPtyGT8yjFe8WrONWgN4u5ad1ewc_5Q69hpfS3hG7epGef09axw0c0wq_AjLVeI4o1YzpjF0TRPr-XVYHMBOO15Z4-bzbGOUAbxZN6OD-l0XVbhyWclwT_wnZQBpZ5w7Heq2FNNJRfWN8SbiB_n8_y9_DXf748uL7GIwPH8B96hPu4njkNId6C2ul-4l4qaFftVYK4Hslv3jLzfcLGU
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3db9MwED-NTkK8ID5FYIARMAlp2RLbSbwHhDa6amVQVahIe4v8SSuhpKypoH8a_x3nfLSrhHjbY-JT4pzv7Lv4_PsBvNE8i1zKbMgMtSFXzoYy1kmoDJNxpAVX9VbMl1F6_o1_ukwud-BPdxbGl1V2c2I9UZtS-3_kRxh3ew5qhgm8a8sixv3Bh_nP0DNI-Z3Wjk6jMZELu_qF6dvi_bCPY_2W0sHZ5ON52DIMhBrX8Qr7lvKEJZzb1FKZHHMZMeEEk9hqtHAYn6vIOidsElmTeSQUoYxAAcutjhg-9hbsZv70aA92T89G46_dMpBkMY8bPFTGjqOj-RSvMbjp2LnaFbAmCtiKbrdrM68tdoN7cLeNUslJY1b3YccWD2B_3MBcrw7IZHNqa3FA9sl4A4C9egiH_boshMjCkGtFSaR05GRZlZX8PSvIsJjO1Mxz_TyCyU1o7TH0irKwT4BQTPeyWKYsTiTXDmV4ormwljLFhHABvOtUlesWs9xTZ_zIMXfxas03ag3g9Vp23iB1_FPq1Gt8LeHRtesb5dX3vHXW3DIh8SMMl6nljBrFmMI0NkuNx9phcQB73Xjlrcsv8o2BBvBq3YzO6ndgZGHLZS3DPQigEAFkW-O81aHtlmI2rWG_MffEWEI8_f_LX8Jt9Iv883B08QzuUF-BE8chpXvQq66W9jmGUJV60RorgfyG3eMvHE8wow
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Design+and+Development+of+Autotaxin+Inhibitors&rft.jtitle=Pharmaceuticals+%28Basel%2C+Switzerland%29&rft.au=Jia%2C+Yi&rft.au=Li%2C+Yan&rft.au=Xu%2C+Xu-Dong&rft.au=Tian%2C+Yu&rft.date=2021-11-22&rft.issn=1424-8247&rft.eissn=1424-8247&rft.volume=14&rft.issue=11&rft.spage=1203&rft_id=info:doi/10.3390%2Fph14111203&rft.externalDBID=n%2Fa&rft.externalDocID=10_3390_ph14111203
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1424-8247&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1424-8247&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1424-8247&client=summon