Amyloid aggregation and secondary structure changes of liver cystatin: Acidic denaturation and TFE induced studies

A cysteine proteinase inhibitor has been purified by affinity chromatography from the liver of buffalo. Liver cystatin is subjected to incubation at low pH with co-solvent TFE, where we have studied the effect on the conformation, activity and tendency to form aggregates or fibrils. ANS fluorescence...

Full description

Saved in:
Bibliographic Details
Published inJournal of biomolecular structure & dynamics Vol. 40; no. 23; pp. 12506 - 12515
Main Authors Mir, Faisal Mustafa, Bano, Bilqees
Format Journal Article
LanguageEnglish
Published England Taylor & Francis 01.01.2022
Subjects
aggregation
amyloid
Amyloid - chemistry
CD spectroscopy
Circular Dichroism
Cystatin
Cystatins - chemistry
FTIR
Liver
Protein Structure, Secondary
Solvents
Cystatin
aggregation
amyloid
FTIR
CD spectroscopy
Online AccessGet full text

Cover

Abstract A cysteine proteinase inhibitor has been purified by affinity chromatography from the liver of buffalo. Liver cystatin is subjected to incubation at low pH with co-solvent TFE, where we have studied the effect on the conformation, activity and tendency to form aggregates or fibrils. ANS fluorescence was used to study conformational changes. The fibril formation and aggregation was studied using ThT assay, CD, FTIR and fluorescence spectroscopy. At pH 3.0 there was no fibril formation though aggregates were formed but in presence of TFE fibrils appeared. At pH 2.0 and 1.0, TFE induced rapid fibril formation compared to only acid induced state as assessed by Thioflavin T (ThT) fluorescence.TFE stabilized each of the three acid induced intermediates at predenaturational concentrations (20%) and accelerated fibril formation. Solvent conditions had a profound effect on the tendency of liver cystatin to produce fibrils and aggregation. Communicated by Ramaswamy H. Sarma
AbstractList A cysteine proteinase inhibitor has been purified by affinity chromatography from the liver of buffalo. Liver cystatin is subjected to incubation at low pH with co-solvent TFE, where we have studied the effect on the conformation, activity and tendency to form aggregates or fibrils. ANS fluorescence was used to study conformational changes. The fibril formation and aggregation was studied using ThT assay, CD, FTIR and fluorescence spectroscopy. At pH 3.0 there was no fibril formation though aggregates were formed but in presence of TFE fibrils appeared. At pH 2.0 and 1.0, TFE induced rapid fibril formation compared to only acid induced state as assessed by Thioflavin T (ThT) fluorescence.TFE stabilized each of the three acid induced intermediates at predenaturational concentrations (20%) and accelerated fibril formation. Solvent conditions had a profound effect on the tendency of liver cystatin to produce fibrils and aggregation. Communicated by Ramaswamy H. Sarma
A cysteine proteinase inhibitor has been purified by affinity chromatography from the liver of buffalo. Liver cystatin is subjected to incubation at low pH with co-solvent TFE, where we have studied the effect on the conformation, activity and tendency to form aggregates or fibrils. ANS fluorescence was used to study conformational changes. The fibril formation and aggregation was studied using ThT assay, CD, FTIR and fluorescence spectroscopy. At pH 3.0 there was no fibril formation though aggregates were formed but in presence of TFE fibrils appeared. At pH 2.0 and 1.0, TFE induced rapid fibril formation compared to only acid induced state as assessed by Thioflavin T (ThT) fluorescence.TFE stabilized each of the three acid induced intermediates at predenaturational concentrations (20%) and accelerated fibril formation. Solvent conditions had a profound effect on the tendency of liver cystatin to produce fibrils and aggregation.Communicated by Ramaswamy H. Sarma.
Author Bano, Bilqees
Mir, Faisal Mustafa
Author_xml – sequence: 1
  givenname: Faisal Mustafa
  surname: Mir
  fullname: Mir, Faisal Mustafa
  organization: School of Biotechnology and Graduate school of Biochemistry, Yeungnum University
– sequence: 2
  givenname: Bilqees
  surname: Bano
  fullname: Bano, Bilqees
  organization: Department of Biochemistry, faculty of Life Sciences, A.M.U
BackLink https://www.ncbi.nlm.nih.gov/pubmed/34488562$$D View this record in MEDLINE/PubMed
BookMark eNp9kMtOHDEQRS0EguHxCUReZtOT8qsfWWWEIImElA2sLbddPTjqtondHTR_H49mSHZZ1ebce1XnkpyGGJCQWwZrBi18gkZ0jAFfc-BszbqGqVqdkBVToq2AK3lKVnum2kMX5DLnn1BI1rBzciGkbFtV8xVJm2k3Ru-o2W4Tbs3sY6AmOJrRxuBM2tE8p8XOS0JqX0zYYqZxoKP_jYnaXZ5LJHymG-udt9RhMAX9V_P0cE99cIvFUjkvzmO-JmeDGTPeHO8VeX64f7r7Vj3--Pr9bvNYWcHkXNV1b7rWupZJgWglb_quUdDUtRJWYg39gICSGWUc8J6D64RUbWulsD0DEFfk46H3NcVfC-ZZTz5bHEcTMC5Zc9VAkdN1rKDqgNoUc0446Nfkp_K8ZqD3uvW7br3XrY-6S-7DcWLpJ3R_U-9-C_DlAPgwxDSZt5hGp2dTnKchmWB91uL_G38Ay6WRWg
Cites_doi 10.1002/pro.5560040813
10.1006/jmbi.1994.0015
10.1016/S0022-2836(65)80111-5
10.1002/(SICI)1097-0134(19980815)32:3<296::AID-PROT5>3.0.CO;2-G
10.1016/S0014-5793(00)01888-3
10.1016/S0021-9258(19)50385-4
10.1046/j.1432-1033.2002.03112.x
10.1007/s00441-017-2706-9
10.1038/nsb1096-868
10.1021/bi00207a018
10.1523/JNEUROSCI.3672-12.2013
10.1021/bi00039a051
10.1021/bi9604587
10.1016/S0167-4838(01)00295-3
10.1073/pnas.88.10.4176
10.1038/7616
10.1177/37.8.2666510
10.1016/j.biochi.2010.05.012
10.1126/science.181.4096.223
10.1002/(SICI)1097-0134(19990801)36:2<205::AID-PROT6>3.0.CO;2-4
10.1038/35065514
10.1038/358302a0
10.2174/1389203720666190214152439
10.1016/S0959-4388(98)80090-1
10.1016/j.semcdb.2003.12.008
10.1016/j.bbapap.2007.06.008
10.1016/S0959-440X(99)00049-4
10.1006/jsbi.2000.4221
10.1016/s0076-6879(99)09020-5
10.1126/sageke.2005.38.pe28
10.1146/annurev-pathol-020712-163913
10.1146/annurev.bi.60.070191.004051
10.1006/jmbi.2001.4970
10.1021/bi00091a037
10.1021/acs.accounts.7b00554
10.1016/S0006-3495(03)74550-0
10.1006/jmbi.2001.4858
10.1146/annurev.biochem.66.1.385
10.1038/s41586-020-1984-7
10.1016/j.ijbiomac.2014.07.027
10.1146/annurev-biochem-061516-044518
10.1002/(SICI)1097-0134(20000515)39:3<204::AID-PROT20>3.0.CO;2-8
10.1021/bi952501g
10.1074/jbc.271.3.1314
10.1074/jbc.M010907200
10.1016/S0006-291X(86)80519-8
10.1006/jmbi.1996.0412
10.1006/jmbi.1995.0652
10.1042/bj2360312
10.1038/s41593-018-0235-9
ContentType Journal Article
Copyright 2021 Informa UK Limited, trading as Taylor & Francis Group 2021
Copyright_xml – notice: 2021 Informa UK Limited, trading as Taylor & Francis Group 2021
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
DOI 10.1080/07391102.2021.1971565
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
DatabaseTitleList
MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1538-0254
EndPage 12515
ExternalDocumentID 10_1080_07391102_2021_1971565
34488562
1971565
Genre Research Articles
Journal Article
GroupedDBID ---
-~X
.QJ
0BK
0R~
30N
4.4
5GY
AAAVI
AAENE
AAJMT
AALDU
AAMIU
AAPUL
AAQRR
ABBKH
ABCCY
ABFIM
ABJVF
ABLIJ
ABPEM
ABQHQ
ABTAI
ABXUL
ACGFS
ACTIO
ADCVX
ADGTB
AEGYZ
AEISY
AENEX
AEOZL
AEPSL
AEYOC
AFOLD
AFWLO
AGDLA
AGMYJ
AHDLD
AIJEM
AIRXU
AKBVH
AKOOK
ALMA_UNASSIGNED_HOLDINGS
ALQZU
AQRUH
AVBZW
BLEHA
CCCUG
DGEBU
DKSSO
EBS
E~A
E~B
F5P
FUNRP
FVPDL
GTTXZ
H13
HZ~
H~P
IPNFZ
J.P
KYCEM
LJTGL
M4Z
NX0
O9-
P2P
RIG
RNANH
ROSJB
RTWRZ
S-T
SJN
SNACF
TEI
TFL
TFT
TFW
TQWBC
TTHFI
UT5
V1K
ZGOLN
~KM
~S~
07X
53G
AAGME
AAHBH
AAOAP
ABFMO
ABJNI
ABPAQ
ABTAA
ABXYU
ACBBU
ACDHJ
ACQMU
ACZPZ
ADGTR
ADOPC
AFDYB
AFFVI
AHDZW
AI.
AMATQ
APNXG
AURDB
AWYRJ
BFWEY
C0.
CGR
CUY
CVF
CWRZV
DLOXE
ECM
EIF
EJD
EMOBN
HGUVV
JEPSP
NPM
NUSFT
OWHGL
PCLFJ
S70
TBQAZ
TDBHL
TUROJ
VH1
AAYXX
CITATION
7X8
ID FETCH-LOGICAL-c314t-66ba98cd8143eec427b975076653c4e60bfe0e41a5ad02b20d934588c43cb1003
ISSN 0739-1102
IngestDate Fri Aug 16 21:48:34 EDT 2024
Fri Aug 23 01:17:14 EDT 2024
Wed Oct 16 00:40:13 EDT 2024
Tue Jun 13 19:15:44 EDT 2023
IsPeerReviewed true
IsScholarly true
Issue 23
Keywords Cystatin
aggregation
amyloid
FTIR
CD spectroscopy
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c314t-66ba98cd8143eec427b975076653c4e60bfe0e41a5ad02b20d934588c43cb1003
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 34488562
PQID 2570110991
PQPubID 23479
PageCount 10
ParticipantIDs informaworld_taylorfrancis_310_1080_07391102_2021_1971565
proquest_miscellaneous_2570110991
crossref_primary_10_1080_07391102_2021_1971565
pubmed_primary_34488562
PublicationCentury 2000
PublicationDate 2022-01-01
PublicationDateYYYYMMDD 2022-01-01
PublicationDate_xml – month: 01
  year: 2022
  text: 2022-01-01
  day: 01
PublicationDecade 2020
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle Journal of biomolecular structure & dynamics
PublicationTitleAlternate J Biomol Struct Dyn
PublicationYear 2022
Publisher Taylor & Francis
Publisher_xml – name: Taylor & Francis
References CIT0030
CIT0032
CIT0031
CIT0034
CIT0036
CIT0035
Turk B. (CIT0043) 1997; 378
CIT0038
CIT0037
CIT0039
CIT0041
CIT0040
CIT0042
CIT0001
CIT0045
CIT0044
Lashuel H. A. (CIT0028) 2005; 2005
CIT0003
CIT0047
CIT0046
CIT0005
CIT0049
CIT0004
CIT0048
CIT0007
CIT0006
CIT0009
CIT0008
CIT0050
CIT0052
CIT0051
CIT0010
CIT0053
CIT0012
CIT0011
Barrett A. J. (CIT0002) 1986; 45
CIT0014
Raso S. W. (CIT0033) 2000
CIT0013
CIT0016
CIT0015
CIT0018
CIT0017
CIT0019
CIT0021
CIT0020
CIT0023
CIT0022
CIT0025
CIT0024
CIT0027
CIT0026
CIT0029
References_xml – ident: CIT0011
  doi: 10.1002/pro.5560040813
– ident: CIT0037
  doi: 10.1006/jmbi.1994.0015
– ident: CIT0042
  doi: 10.1016/S0022-2836(65)80111-5
– ident: CIT0052
  doi: 10.1002/(SICI)1097-0134(19980815)32:3<296::AID-PROT5>3.0.CO;2-G
– ident: CIT0019
  doi: 10.1016/S0014-5793(00)01888-3
– ident: CIT0048
  doi: 10.1016/S0021-9258(19)50385-4
– ident: CIT0021
  doi: 10.1046/j.1432-1033.2002.03112.x
– ident: CIT0040
  doi: 10.1007/s00441-017-2706-9
– ident: CIT0015
  doi: 10.1038/nsb1096-868
– ident: CIT0013
  doi: 10.1021/bi00207a018
– ident: CIT0005
  doi: 10.1523/JNEUROSCI.3672-12.2013
– ident: CIT0030
  doi: 10.1021/bi00039a051
– ident: CIT0007
  doi: 10.1021/bi9604587
– ident: CIT0049
  doi: 10.1016/S0167-4838(01)00295-3
– ident: CIT0041
  doi: 10.1073/pnas.88.10.4176
– ident: CIT0004
  doi: 10.1038/7616
– ident: CIT0025
  doi: 10.1177/37.8.2666510
– ident: CIT0050
  doi: 10.1016/j.biochi.2010.05.012
– ident: CIT0001
  doi: 10.1126/science.181.4096.223
– volume: 45
  start-page: 1363
  issue: 11
  year: 1986
  ident: CIT0002
  publication-title: Biomedica Biochimica Acta
  contributor:
    fullname: Barrett A. J.
– ident: CIT0051
  doi: 10.1002/(SICI)1097-0134(19990801)36:2<205::AID-PROT6>3.0.CO;2-4
– ident: CIT0012
  doi: 10.1038/35065514
– ident: CIT0032
  doi: 10.1038/358302a0
– ident: CIT0045
  doi: 10.2174/1389203720666190214152439
– ident: CIT0014
  doi: 10.1016/S0959-4388(98)80090-1
– start-page: 406
  volume-title: Frontiers in molecular biology series
  year: 2000
  ident: CIT0033
  contributor:
    fullname: Raso S. W.
– ident: CIT0009
  doi: 10.1016/j.semcdb.2003.12.008
– ident: CIT0018
  doi: 10.1016/j.bbapap.2007.06.008
– ident: CIT0034
  doi: 10.1016/S0959-440X(99)00049-4
– ident: CIT0038
  doi: 10.1006/jsbi.2000.4221
– ident: CIT0029
  doi: 10.1016/s0076-6879(99)09020-5
– volume: 2005
  start-page: pe28
  issue: 38
  year: 2005
  ident: CIT0028
  publication-title: Science of Aging Knowledge Environment: SAGE KE
  doi: 10.1126/sageke.2005.38.pe28
  contributor:
    fullname: Lashuel H. A.
– ident: CIT0046
  doi: 10.1146/annurev-pathol-020712-163913
– ident: CIT0008
  doi: 10.1146/annurev.bi.60.070191.004051
– ident: CIT0024
  doi: 10.1006/jmbi.2001.4970
– ident: CIT0031
  doi: 10.1021/bi00091a037
– ident: CIT0026
  doi: 10.1021/acs.accounts.7b00554
– ident: CIT0023
  doi: 10.1016/S0006-3495(03)74550-0
– ident: CIT0053
  doi: 10.1006/jmbi.2001.4858
– ident: CIT0016
  doi: 10.1146/annurev.biochem.66.1.385
– ident: CIT0036
  doi: 10.1038/s41586-020-1984-7
– ident: CIT0022
  doi: 10.1016/j.ijbiomac.2014.07.027
– ident: CIT0017
  doi: 10.1146/annurev-biochem-061516-044518
– volume: 378
  start-page: 141
  issue: 3
  year: 1997
  ident: CIT0043
  publication-title: Biological Chemistry
  contributor:
    fullname: Turk B.
– ident: CIT0006
  doi: 10.1002/(SICI)1097-0134(20000515)39:3<204::AID-PROT20>3.0.CO;2-8
– ident: CIT0027
  doi: 10.1021/bi952501g
– ident: CIT0010
  doi: 10.1074/jbc.271.3.1314
– ident: CIT0044
  doi: 10.1074/jbc.M010907200
– ident: CIT0020
  doi: 10.1016/S0006-291X(86)80519-8
– ident: CIT0035
  doi: 10.1006/jmbi.1996.0412
– ident: CIT0047
  doi: 10.1006/jmbi.1995.0652
– ident: CIT0003
  doi: 10.1042/bj2360312
– ident: CIT0039
  doi: 10.1038/s41593-018-0235-9
SSID ssj0021171
Score 2.3438706
Snippet A cysteine proteinase inhibitor has been purified by affinity chromatography from the liver of buffalo. Liver cystatin is subjected to incubation at low pH...
SourceID proquest
crossref
pubmed
informaworld
SourceType Aggregation Database
Index Database
Publisher
StartPage 12506
SubjectTerms aggregation
amyloid
Amyloid - chemistry
CD spectroscopy
Circular Dichroism
Cystatin
Cystatins - chemistry
FTIR
Liver
Protein Structure, Secondary
Solvents
Title Amyloid aggregation and secondary structure changes of liver cystatin: Acidic denaturation and TFE induced studies
URI https://www.tandfonline.com/doi/abs/10.1080/07391102.2021.1971565
https://www.ncbi.nlm.nih.gov/pubmed/34488562
https://search.proquest.com/docview/2570110991
Volume 40
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lj9MwELZgERIXxJvykpG4RaliO3YabgW1WqHdckml3qzEdleRdlug3cPy65mx86ooYuGSVpHiVv6-jGfs-WYI-WATVXFlZGzhI06l4XGpIOZxLMnXiRWm8lsD5wt1uky_rOSqT8j06pJ9NTY_j-pK_gdVuAe4okr2H5DtBoUb8B3whSsgDNdbYTy9gnC7tlF5AVHzRYDSb4RjlGsxHy6Uh8VDgqDw9Ykbl5iLEZkbFBPVPrNjampbmwhsENb57Acq5rMIgvZrTBLYDTIOf_dmUcbfdtod_CoSy4am953zfl57lszLeofCYFRwrfttgdL3Ao8-1ZffnTvYlOB8sCnhekOKSvuhpQ2FmRpGcTGwm-BmJWqwCKPbJY9a-CYlMhNgpb2SjrMxyzMIQ2W_pLXH-Iuver48O9PFbFXcJfd4lktM-xTJogvKGctYq-zCmuvHBj7wWQ4q2v45LvH-SfGIPGygoNPAksfkjts8IfdDq9Gbp-RHwxU64AoFiGnHFdqhRhuu0O2aeq7QlisfaWAKHTLFDwNMoQ1TaMOUZ2Q5nxWfT-Om30ZsBEv3sVJVmU-MnYAP7ZxJeVbl4FBmSklhUqeSau0Sl7JSljbhFU9sLlDobFJ4pRksD8_JyWa7cS8JFTCLE1gaSqmy1Eo3ETYpXcWlBZcfIuwRGbczqr-FsiqatdVqGwg0QqAbCEYkH8673vv9rHVoPqPFX55934KkwXjiiVi5cdvrncYWjlhyN2cj8iKg1_0dkcLaBtHBq1s8_Zo86N-CN-QE8HJvwVndV-88234B1PaTdg
link.rule.ids 315,786,790,27955,27956,60239,61028
linkProvider Taylor & Francis
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9swDCa2DsN62bPrsqcG7OpUsi0l3i0YGmRbk1MC9Cbo5cDo6hR5HLJfP9KKu2ZAsENPPkmyREriR_EjAb54rmyqnEw8fpJcujQxCjFPELwouc-cbVwD44kazfIfl_LyDheGwioJQ5cxUURzVtPmJmd0GxJ3Rq9LeG0RjyoVXVH0EITIh_BIEVOTaBx8cgu6hGhAFzVJqE3L4jnUzd79tJe99LAN2txFw2fg2lnEEJSr7mZtu-73Pwke7zfN5_B0Z6qyQdStF_Ag1C_hcSxeuX0Fy8E1gv3KMzNHzD5vJMxwMLYijO3NcstictrNMrDIL16xRcl-USQIc1uiMlX1VzZwla8cw_OPcoz-7WY6PGdV7VH1sMsY7XgCs-H59Nso2VVwSFwm8nWilDVF3_k-WmUhuDzt2QJNlJ5SMnN5UNyWgYdcGGk8T23KfZERddblqCQCD5zXcFQv6vAGWIZrgWidG6l6uZehn3lugk2lRyMSMVsHuq3c9E1M1KFFm_90t5CaFlLvFrIDxV3p6nXjISljOROd_aft51YVNG5HemMxdVhsVpqKAlIS10J04DTqyO3vZAiF-2hvvr3HyJ_gyWg6vtAX3yc_38FxSmSMxiH0Ho5QpuEDmkhr-7HZA38ACaIB3w
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LT9wwEB61VK24UFpe2xZqpF6z2Ens3fS2allBH6seQOJm-RUU0WbRPg7Lr2cmTihUQj1wysl27Bl75rNnvgH45LmyqXIy8fhJcunSxCjEPEHwouQ-c7a5Gvg5USfn-bcL2UUTztuwSsLQZSSKaM5q2tzXvuwi4o7ocQmtFqVRpaIvigFiEPkcXigylpTFwSd3mEuIBnNRk4TadEk8j3XzwDw9IC993AVtTNH4NdhuEjEC5aq_XNi-u_mH3_FJs9yEjdZRZaOoWW_gWajfwstYunK1BbPRH4T6lWfmEhH7ZSNfhmOxOSFsb2YrFqlpl7PAYnbxnE1L9pviQJhbUSJTVX9mI1f5yjE8_Yhh9G83Z-NjVtUeFQ-7jLGO23A-Pj77cpK09RsSl4l8kShlTTF0fog-WQguTwe2QAdloJTMXB4Ut2XgIRdGGs9Tm3JfZJQ463JUEYHHzQ6s1dM67AHLcC0Qq3Mj1SD3Mgwzz02wqfToQiJi60G_E5u-jjQdWnTsp-1CalpI3S5kD4r7wtWL5n6kjMVMdPaftoedJmjcjPTCYuowXc41lQQkCtdC9GA3qsjd72QIhIfobb57wsgf4dWvr2P943Ty_T2sp5SJ0dwGfYA1FGnYR_9oYQ-aHXAL7W0AjA
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=Amyloid+aggregation+and+secondary+structure+changes+of+liver+cystatin%3A+Acidic+denaturation+and+TFE+induced+studies&rft.jtitle=Journal+of+biomolecular+structure+%26+dynamics&rft.au=Mir%2C+Faisal+Mustafa&rft.au=Bano%2C+Bilqees&rft.date=2022-01-01&rft.eissn=1538-0254&rft.volume=40&rft.issue=23&rft.spage=12506&rft.epage=12515&rft_id=info:doi/10.1080%2F07391102.2021.1971565&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0739-1102&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0739-1102&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0739-1102&client=summon