The first report on transcriptome analysis of the venom gland of Iranian scorpion, Hemiscorpius lepturus

Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The prevalence and severity of scorpionism is high and health services are not able to control it. Scorpionism in Iran especially in the southern regio...

Full description

Saved in:
Bibliographic Details
Published inToxicon (Oxford) Vol. 125; pp. 123 - 130
Main Authors Kazemi-Lomedasht, Fatemeh, Khalaj, Vahid, Bagheri, Kamran Pooshang, Behdani, Mahdi, Shahbazzadeh, Delavar
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.01.2017
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The prevalence and severity of scorpionism is high and health services are not able to control it. Scorpionism in Iran especially in the southern regions (Khuzestan, Sistan and Baluchestan, Hormozgan, Ilam) is one of the main health challenges. Due to the medical and health importance of scorpionism, the focus of various studies has been on the identification of H. lepturus venom components. Nevertheless, until now, only a few percent of H. lepturus venom components have been identified and there is no complete information about the venom components of H. lepturus. The current study reports transcriptome analysis of the venom gland of H. lepturus scorpion. Illumina Next Generation Sequencing results identified venom components of H. lepturus. When compared with other scorpion's venom, the venom of H. lepturus consists of mixtures of peptides, proteins and enzymes such as; phospholipases, metalloproteases, hyaluronidases, potassium channel toxins, calcium channel toxins, antimicrobial peptides (AMPs), venom proteins, venom toxins, allergens, La1-like peptides, proteases and scorpine-like peptides. Comparison of identified components of H. lepturus venom was carried out with venom components of reported scorpions and various identities and similarities between them were observed. With transcriptome analysis of H. lepturus venom unique sequences, coding venom components were investigated. Moreover, our study confirmed transcript expression of previously reported peptides; Hemitoxin, Hemicalcin and Hemilipin. The gene sequences of venom components were investigated employing transcriptome analysis of venom gland of H. lepturus. In summary, new bioactive molecules identified in this study, provide basis for venomics studies of scorpions of Hemiscorpiidae family and promises development of novel biotherapeutics. [Display omitted] •The current study reports transcriptome analysis of the venom gland of H. lepturus scorpion using Illumina next generation sequencing.•Illumina Next Generation Sequencing results identified venom components of H. lepturus.•New bioactive molecules identified in this study, provide basis for venomics studies of scorpions of Hemiscorpiidae family and promises development of novel biotherapeutics.
AbstractList Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The prevalence and severity of scorpionism is high and health services are not able to control it. Scorpionism in Iran especially in the southern regions (Khuzestan, Sistan and Baluchestan, Hormozgan, Ilam) is one of the main health challenges. Due to the medical and health importance of scorpionism, the focus of various studies has been on the identification of H. lepturus venom components. Nevertheless, until now, only a few percent of H. lepturus venom components have been identified and there is no complete information about the venom components of H. lepturus. The current study reports transcriptome analysis of the venom gland of H. lepturus scorpion. Illumina Next Generation Sequencing results identified venom components of H. lepturus. When compared with other scorpion's venom, the venom of H. lepturus consists of mixtures of peptides, proteins and enzymes such as; phospholipases, metalloproteases, hyaluronidases, potassium channel toxins, calcium channel toxins, antimicrobial peptides (AMPs), venom proteins, venom toxins, allergens, La1-like peptides, proteases and scorpine-like peptides. Comparison of identified components of H. lepturus venom was carried out with venom components of reported scorpions and various identities and similarities between them were observed. With transcriptome analysis of H. lepturus venom unique sequences, coding venom components were investigated. Moreover, our study confirmed transcript expression of previously reported peptides; Hemitoxin, Hemicalcin and Hemilipin. The gene sequences of venom components were investigated employing transcriptome analysis of venom gland of H. lepturus. In summary, new bioactive molecules identified in this study, provide basis for venomics studies of scorpions of Hemiscorpiidae family and promises development of novel biotherapeutics.
Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The prevalence and severity of scorpionism is high and health services are not able to control it. Scorpionism in Iran especially in the southern regions (Khuzestan, Sistan and Baluchestan, Hormozgan, Ilam) is one of the main health challenges. Due to the medical and health importance of scorpionism, the focus of various studies has been on the identification of H. lepturus venom components. Nevertheless, until now, only a few percent of H. lepturus venom components have been identified and there is no complete information about the venom components of H. lepturus. The current study reports transcriptome analysis of the venom gland of H. lepturus scorpion. Illumina Next Generation Sequencing results identified venom components of H. lepturus. When compared with other scorpion's venom, the venom of H. lepturus consists of mixtures of peptides, proteins and enzymes such as; phospholipases, metalloproteases, hyaluronidases, potassium channel toxins, calcium channel toxins, antimicrobial peptides (AMPs), venom proteins, venom toxins, allergens, La1-like peptides, proteases and scorpine-like peptides. Comparison of identified components of H. lepturus venom was carried out with venom components of reported scorpions and various identities and similarities between them were observed. With transcriptome analysis of H. lepturus venom unique sequences, coding venom components were investigated. Moreover, our study confirmed transcript expression of previously reported peptides; Hemitoxin, Hemicalcin and Hemilipin. The gene sequences of venom components were investigated employing transcriptome analysis of venom gland of H. lepturus. In summary, new bioactive molecules identified in this study, provide basis for venomics studies of scorpions of Hemiscorpiidae family and promises development of novel biotherapeutics.
Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The prevalence and severity of scorpionism is high and health services are not able to control it. Scorpionism in Iran especially in the southern regions (Khuzestan, Sistan and Baluchestan, Hormozgan, Ilam) is one of the main health challenges. Due to the medical and health importance of scorpionism, the focus of various studies has been on the identification of H. lepturus venom components. Nevertheless, until now, only a few percent of H. lepturus venom components have been identified and there is no complete information about the venom components of H. lepturus. The current study reports transcriptome analysis of the venom gland of H. lepturus scorpion. Illumina Next Generation Sequencing results identified venom components of H. lepturus. When compared with other scorpion's venom, the venom of H. lepturus consists of mixtures of peptides, proteins and enzymes such as; phospholipases, metalloproteases, hyaluronidases, potassium channel toxins, calcium channel toxins, antimicrobial peptides (AMPs), venom proteins, venom toxins, allergens, La1-like peptides, proteases and scorpine-like peptides. Comparison of identified components of H. lepturus venom was carried out with venom components of reported scorpions and various identities and similarities between them were observed. With transcriptome analysis of H. lepturus venom unique sequences, coding venom components were investigated. Moreover, our study confirmed transcript expression of previously reported peptides; Hemitoxin, Hemicalcin and Hemilipin. The gene sequences of venom components were investigated employing transcriptome analysis of venom gland of H. lepturus. In summary, new bioactive molecules identified in this study, provide basis for venomics studies of scorpions of Hemiscorpiidae family and promises development of novel biotherapeutics. [Display omitted] •The current study reports transcriptome analysis of the venom gland of H. lepturus scorpion using Illumina next generation sequencing.•Illumina Next Generation Sequencing results identified venom components of H. lepturus.•New bioactive molecules identified in this study, provide basis for venomics studies of scorpions of Hemiscorpiidae family and promises development of novel biotherapeutics.
Author Khalaj, Vahid
Shahbazzadeh, Delavar
Bagheri, Kamran Pooshang
Kazemi-Lomedasht, Fatemeh
Behdani, Mahdi
Author_xml – sequence: 1
  givenname: Fatemeh
  surname: Kazemi-Lomedasht
  fullname: Kazemi-Lomedasht, Fatemeh
  organization: Venom & Biotherapeutics Molecules Laboratory, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran
– sequence: 2
  givenname: Vahid
  surname: Khalaj
  fullname: Khalaj, Vahid
  organization: Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran
– sequence: 3
  givenname: Kamran Pooshang
  surname: Bagheri
  fullname: Bagheri, Kamran Pooshang
  organization: Venom & Biotherapeutics Molecules Laboratory, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran
– sequence: 4
  givenname: Mahdi
  surname: Behdani
  fullname: Behdani, Mahdi
  email: Behdani@pasteur.ac.ir
  organization: Venom & Biotherapeutics Molecules Laboratory, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran
– sequence: 5
  givenname: Delavar
  surname: Shahbazzadeh
  fullname: Shahbazzadeh, Delavar
  email: shahbazzadeh@pasteur.ac.ir
  organization: Venom & Biotherapeutics Molecules Laboratory, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran
BackLink https://www.ncbi.nlm.nih.gov/pubmed/27914888$$D View this record in MEDLINE/PubMed
BookMark eNqFkcFu1DAQhi1URLeFRwD5yIGkHsfJ2uKAUAW0UiUu5Ww5zoR6ldjBdqr27fFqFw697Mka6_tHo_-7IGc-eCTkPbAaGHRXuzqHJ2eDr3kZa4Cad_CKbEBuVdVAy87IhjEBFSv4OblIaccYa6Tq3pBzvlUgpJQb8nD_gHR0MWUacQkx0-BpjsYnG92Sw4zUeDM9J5doGGku9CP6MNPfk_HD_uu2wM54mmyIiwv-E73B2R2mNdEJl7zGNb0lr0czJXx3fC_Jr-_f7q9vqrufP26vv95VVnQiV20vOtkOtm2YVbbvhehHiSMA52PTWGs6lEKMYBWYXplGMeDM9mIwyvJxYM0l-XjYu8TwZ8WU9f4YnMq5GNakOUCnQPLtaRSk6BjfAlcF_XBE137GQS_RzSY-639FFqA9ADaGlCKO_xFgei9M7_RRmN4L0wC6CCu5zy9y1mWTS49FgptOpr8c0lgafXQYdbIOvcXBRbRZD8Gd2PAXMPK2rg
CitedBy_id crossref_primary_10_1016_j_toxicon_2017_05_002
crossref_primary_10_1186_s40409_018_0145_z
crossref_primary_10_1016_j_toxicon_2020_12_017
crossref_primary_10_1186_s12860_020_00328_4
crossref_primary_10_1016_j_toxicon_2018_07_018
crossref_primary_10_3390_toxins10060249
crossref_primary_10_1016_j_bbagen_2018_08_019
crossref_primary_10_1016_j_peptides_2021_170643
crossref_primary_10_1016_j_toxicon_2024_108109
crossref_primary_10_1016_j_toxicon_2021_09_001
crossref_primary_10_3390_toxins11110637
crossref_primary_10_1016_j_toxicon_2020_05_003
crossref_primary_10_1007_s12639_019_01113_7
crossref_primary_10_1007_s10989_017_9625_1
crossref_primary_10_1016_j_toxicon_2020_04_003
crossref_primary_10_1016_j_toxicon_2017_12_051
crossref_primary_10_2174_0126661217183829231108105708
crossref_primary_10_1186_s13578_017_0187_x
crossref_primary_10_1590_1678_9199_jvatitd_2021_0002
crossref_primary_10_29328_journal_abb_1001025
crossref_primary_10_1016_j_toxicon_2020_12_007
crossref_primary_10_5812_jjhs_102586
crossref_primary_10_3390_toxins13020154
crossref_primary_10_1016_j_toxicon_2018_07_007
crossref_primary_10_1371_journal_pntd_0009880
crossref_primary_10_2174_2666121701666211124151529
crossref_primary_10_3390_molecules25071673
crossref_primary_10_3390_molecules24142670
crossref_primary_10_1080_15569543_2021_2018613
crossref_primary_10_1007_s10989_023_10543_0
crossref_primary_10_1016_j_toxicon_2020_02_021
crossref_primary_10_1016_j_toxicon_2017_12_042
crossref_primary_10_1016_j_toxicon_2017_09_010
crossref_primary_10_1016_j_toxicon_2020_05_010
crossref_primary_10_3389_fphar_2024_1464648
crossref_primary_10_1016_j_toxicon_2022_04_015
crossref_primary_10_29328_journal_abb_1001014
crossref_primary_10_2174_0109298665321842240819073453
Cites_doi 10.1016/j.toxicon.2015.08.022
10.1016/j.molimm.2014.09.018
10.1016/j.peptides.2013.10.021
10.1038/nmeth.3213
10.1046/j.1432-1327.1999.00625.x
10.1016/j.jprot.2013.06.007
10.1016/j.peptides.2003.12.003
10.1016/j.toxicon.2016.03.014
10.1016/j.toxicon.2004.03.022
10.1016/S0167-0115(03)00146-0
10.1021/bi0349930
10.1111/j.1755-0998.2011.02990.x
10.1186/1471-2164-10-290
10.1073/pnas.1214062110
10.1186/1471-2164-8-119
10.1016/j.peptides.2004.12.002
10.1002/pmic.200900763
10.1016/j.toxicon.2014.11.233
10.1016/j.peptides.2012.03.016
10.1016/j.toxicon.2011.02.001
10.1111/j.1742-4658.2008.06607.x
10.1096/fj.13-247478
10.1016/j.toxicon.2013.08.064
10.1002/pmic.200500525
10.1371/journal.pone.0043331
10.1002/pmic.201100409
10.1186/1471-2164-13-362
10.1371/journal.pone.0117188
10.1186/1471-2164-11-452
10.1016/j.jprot.2014.04.033
10.1016/j.jprot.2011.11.029
10.1016/j.toxicon.2013.10.006
10.1016/j.toxicon.2016.06.002
10.1016/j.toxicon.2009.04.010
10.1016/j.toxicon.2010.05.008
10.1016/j.biochi.2009.05.005
10.1371/journal.pone.0127883
10.1021/pr400875s
10.1016/j.actatropica.2008.05.021
10.1016/j.toxicon.2009.11.010
10.1016/j.toxicon.2012.11.017
10.1016/S0014-5793(99)01392-7
10.1007/s00018-007-7370-x
10.1016/j.toxicon.2011.05.016
10.1042/BJ20061404
10.1016/j.toxicon.2013.03.010
10.1007/978-94-007-6416-3_29
10.1016/j.jchromb.2003.09.002
10.1016/j.toxicon.2012.10.012
10.1016/j.toxicon.2013.03.012
10.1159/000358060
ContentType Journal Article
Copyright 2016 Elsevier Ltd
Copyright © 2016 Elsevier Ltd. All rights reserved.
Copyright_xml – notice: 2016 Elsevier Ltd
– notice: Copyright © 2016 Elsevier Ltd. All rights reserved.
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7S9
L.6
DOI 10.1016/j.toxicon.2016.11.261
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList AGRICOLA
MEDLINE
MEDLINE - Academic

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 Anatomy & Physiology
Pharmacy, Therapeutics, & Pharmacology
EISSN 1879-3150
EndPage 130
ExternalDocumentID 27914888
10_1016_j_toxicon_2016_11_261
S0041010116306055
Genre Journal Article
GeographicLocations Iran
Iraq
Yemen
GeographicLocations_xml – name: Iran
– name: Iraq
– name: Yemen
GroupedDBID ---
--K
--M
-~X
.GJ
.~1
0R~
123
1B1
1RT
1~.
1~5
29Q
4.4
41~
457
4G.
53G
5RE
5VS
7-5
71M
8P~
9JM
AABNK
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AATCM
AAXUO
ABFNM
ABFRF
ABFYP
ABGSF
ABJNI
ABLST
ABMAC
ABUDA
ABXDB
ABYKQ
ABZDS
ACDAQ
ACGFO
ACGFS
ACIUM
ACRLP
ADBBV
ADEZE
ADMUD
ADUVX
AEBSH
AEFWE
AEHWI
AEKER
AENEX
AFKWA
AFTJW
AFXIZ
AGHFR
AGRDE
AGUBO
AGYEJ
AHEUO
AHHHB
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
AKIFW
ALCLG
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLECG
BLXMC
C45
CS3
DOVZS
DU5
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
F5P
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HMT
HVGLF
HZ~
IHE
J1W
KCYFY
KOM
M34
M41
MO0
N9A
O-L
O9-
OAUVE
OGGZJ
OVD
OZT
P-8
P-9
P2P
PC.
Q38
R2-
RIG
ROL
RPZ
SCC
SDF
SDG
SDP
SES
SEW
SPCBC
SPT
SSJ
SSP
SSU
SSZ
T5K
TEORI
TWZ
WUQ
XOL
Y6R
ZGI
ZXP
~02
~G-
~KM
AAHBH
AATTM
AAXKI
AAYWO
AAYXX
ABWVN
ACRPL
ACVFH
ADCNI
ADNMO
AEIPS
AEUPX
AFJKZ
AFPUW
AGCQF
AGQPQ
AGRNS
AIGII
AIIUN
AKBMS
AKRWK
AKYEP
ANKPU
APXCP
BNPGV
CITATION
SSH
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7S9
L.6
ID FETCH-LOGICAL-c464t-5b4685dc530c9cbb44bf8ef1122f33cca6e844f1c91ab9a390120cb4da9c2fd03
IEDL.DBID .~1
ISSN 0041-0101
IngestDate Fri Jul 11 08:23:19 EDT 2025
Fri Jul 11 04:03:46 EDT 2025
Wed Feb 19 02:41:24 EST 2025
Thu Apr 24 22:56:01 EDT 2025
Tue Jul 01 01:46:19 EDT 2025
Fri Feb 23 02:29:31 EST 2024
IsPeerReviewed true
IsScholarly true
Keywords Hemiscorpius lepturus
Transcriptome analysis
Iranian scorpion
RNAseq
Language English
License Copyright © 2016 Elsevier Ltd. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c464t-5b4685dc530c9cbb44bf8ef1122f33cca6e844f1c91ab9a390120cb4da9c2fd03
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 27914888
PQID 1846027129
PQPubID 23479
PageCount 8
ParticipantIDs proquest_miscellaneous_2116918270
proquest_miscellaneous_1846027129
pubmed_primary_27914888
crossref_primary_10_1016_j_toxicon_2016_11_261
crossref_citationtrail_10_1016_j_toxicon_2016_11_261
elsevier_sciencedirect_doi_10_1016_j_toxicon_2016_11_261
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate January 2017
2017-01-00
2017-Jan
20170101
PublicationDateYYYYMMDD 2017-01-01
PublicationDate_xml – month: 01
  year: 2017
  text: January 2017
PublicationDecade 2010
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle Toxicon (Oxford)
PublicationTitleAlternate Toxicon
PublicationYear 2017
Publisher Elsevier Ltd
Publisher_xml – name: Elsevier Ltd
References Conde, Zamudio, Becerril, Possani (bib16) 1999; 460
de la Vega, Schwartz, Possani (bib18) 2010; 56
González-Morales, Pedraza-Escalona, Diego-Garcia, Restano-Cassulini, Batista, del Carmen Gutiérrez, Possani (bib23) 2014; 111
Srairi-Abid, Shahbazzadeh, Chatti, Mlayah-Bellalouna, Mejdoub, Borchani, Benkhalifa, Akbari, El Ayeb (bib50) 2008; 275
Chen, Walker, Zhou, Shaw (bib14) 2005; 26
Higa, das Dores Noronha, López-Lozano (bib27) 2014
Borchani, Sassi, Shahbazzadeh, Strub, Tounsi-Guetteti, Boubaker, Akbari, Van Dorsselaer, El Ayeb (bib11) 2011; 58
Ma, He, Zhao, Wu, Li, Cao (bib33) 2012; 75
Abdel-Rahman, Quintero-Hernández, Possani (bib2) 2016
Yang, Yan, Roy, Xu, Poisson, Zhang (bib54) 2015; 12
Rouault, Bollinger, Lazdunski, Gelb, Lambeau (bib43) 2003; 42
Smith, Vetter, Lewis, Peigneur, Tytgat, Lam, Gallant, Beard, Alewood, Dulhunty (bib49) 2013; 110
Machado, Estrela, Nascimento, Melo, Torres-Rêgo, Lima, Rocha, Carvalho, Silva, Fernandes-Pedrosa (bib36) 2016; 119
Harrison, Abdel-Rahman, Strong, Tawfik, Miller (bib25) 2016; 117
Chen, Folan, Kwok, O'Kane, Bjourson, Shaw (bib13) 2003; 115
Almaaytah, Zhou, Wang, Chen, Walker, Shaw (bib4) 2012; 35
Abdel-Rahman, Quintero-Hernandez, Possani (bib1) 2013; 74
Ma, Zhao, He, Li, Liu, Wu, Cao, Li (bib34) 2009; 10
Angeloni, Wagemaker, Jetten, Op den Camp, Janssen-Megens, Francoijs, Stunnenberg, Ouborg (bib7) 2011; 11
Xia, Ma, Xue, Wang, Tao, Zhao, Zhang, Liu, Lu (bib53) 2013; 76
Incamnoi, Patramanon, Thammasirirak, Chaveerach, Uawonggul, Sukprasert, Rungsa, Daduang, Daduang (bib28) 2013; 61
World Health Organization, W (bib52) 2010
Díaz-García, Ruiz-Fuentes, Yglesias-Rivera, Rodríguez-Sánchez, Garlobo, Martinez, Castro (bib20) 2015; 6
Schwartz, Diego-Garcia, de la Vega, Possani (bib45) 2007; 8
Luna-Ramírez, Quintero-Hernández, Vargas-Jaimes, Batista, Winkel, Possani (bib32) 2013; 63
Batista, D'Suze, Gómez-Lagunas, Zamudio, Encarnación, Sevcik, Possani (bib8) 2006; 6
Ortiz, Gurrola, Schwartz, Possani (bib38) 2015; 93
Zobel-Thropp, Correa, Garb, Binford (bib57) 2013; 13
He, Zhao, Di, Li, Xu, Hong, Wu, Zhao, Li, Cao (bib26) 2013; 89
Possani, Becerril, Delepierre, Tytgat (bib39) 1999; 264
Jridi, Catacchio, Majdoub, Shahbazeddah, El Ayeb, Frassanito, Ribatti, Vacca, Borchani (bib29) 2015; 105
Zeng, Wang, Zhu, Zhu, Li (bib56) 2004; 25
Ruiming, Yibao, Yawen, Zhiyong, Yingliang, Zhijian, Wenxin (bib44) 2010; 11
Borchani, Sassi, Gharsa, Safra, Shahbazzadeh, Lasfar, El Ayeb (bib10) 2013; 68
Alvarenga, Mendes, Magalhaes, Siqueira, Dantas, Barroca, Horta, Kalapothakis (bib6) 2012
Luna-Ramírez, Quintero-Hernández, Juárez-González, Possani (bib31) 2015; 10
Morgenstern, Rohde, King, Tal, Sher, Zlotkin (bib37) 2011; 57
Diego-García, Peigneur, Clynen, Marien, Czech, Schoofs, Tytgat (bib22) 2012; 12
Van Vaerenbergh, De Smet, Rafei-Shamsabadi, Blank, Spillner, Ebo, Devreese, Jakob, de Graaf (bib51) 2015; 63
Rendón-Anaya, Delaye, Possani, Herrera-Estrella (bib41) 2012; 7
D'Suze, Schwartz, García-Gómez, Sevcik, Possani (bib17) 2009; 91
Batista, del Pozo, Zamudio, Contreras, Becerril, Wanke, Possani (bib9) 2004; 803
Bouzid, Klopp, Verdenaud, Ducancel, Vétillard (bib12) 2013; 70
Seyedian, Pipelzadeh, Jalali, Kim, Lee, Kang, Cha, Sohn, Jung, Rahmani (bib46) 2010; 56
Ma, Zhao, Zhao, Zhang, He, Wu, Cao, Guo, Li (bib35) 2010; 10
Almaaytah, Albalas (bib3) 2014; 51
Silva, Camargos, Maranhão, Silva-Pereira, Silva, Possani, Schwartz (bib48) 2009; 54
Yardehnavi, Behdani, Bagheri, Mahmoodzadeh, Khanahmad, Shahbazzadeh, Habibi-Anbouhi, Ghassabeh, Muyldermans (bib55) 2014; 28
Almeida, Scortecci, Kobashi, Agnez-Lima, Medeiros, Silva-Junior, de LM Junqueira-de-Azevedo, de F Fernandes-Pedrosa (bib5) 2012; 13
Quintero-Hernández, Ramírez-Carreto, Romero-Gutiérrez, Valdez-Velázquez, Becerril, Possani, Ortiz (bib40) 2015; 10
Kastin (bib30) 2013
Chippaux, Goyffon (bib15) 2008; 107
Diego-García, Abdel-Mottaleb, Schwartz, de la Vega, Tytgat, Possani (bib21) 2008; 65
Hanen, Nacim, Nabil, Youssef (bib24) 2011
de la Vega, Possani (bib19) 2004; 43
Rodríguez-Pérez, Monsalve, Galán, Perez-Pinar, Umpierrez, Lluch-Bernal, Polo, Caballero (bib42) 2014; 163
Shahbazzadeh, Srairi-Abid, Feng, Ram, Borchani, Ronjat, Akbari, Pessah, De Waard, El Ayeb (bib47) 2007; 404
Chen (10.1016/j.toxicon.2016.11.261_bib13) 2003; 115
Diego-García (10.1016/j.toxicon.2016.11.261_bib22) 2012; 12
Xia (10.1016/j.toxicon.2016.11.261_bib53) 2013; 76
Abdel-Rahman (10.1016/j.toxicon.2016.11.261_bib1) 2013; 74
Smith (10.1016/j.toxicon.2016.11.261_bib49) 2013; 110
Batista (10.1016/j.toxicon.2016.11.261_bib9) 2004; 803
Rodríguez-Pérez (10.1016/j.toxicon.2016.11.261_bib42) 2014; 163
Rendón-Anaya (10.1016/j.toxicon.2016.11.261_bib41) 2012; 7
Chippaux (10.1016/j.toxicon.2016.11.261_bib15) 2008; 107
Yardehnavi (10.1016/j.toxicon.2016.11.261_bib55) 2014; 28
World Health Organization, W (10.1016/j.toxicon.2016.11.261_bib52) 2010
Jridi (10.1016/j.toxicon.2016.11.261_bib29) 2015; 105
Quintero-Hernández (10.1016/j.toxicon.2016.11.261_bib40) 2015; 10
Luna-Ramírez (10.1016/j.toxicon.2016.11.261_bib32) 2013; 63
Ortiz (10.1016/j.toxicon.2016.11.261_bib38) 2015; 93
de la Vega (10.1016/j.toxicon.2016.11.261_bib19) 2004; 43
Srairi-Abid (10.1016/j.toxicon.2016.11.261_bib50) 2008; 275
González-Morales (10.1016/j.toxicon.2016.11.261_bib23) 2014; 111
Ma (10.1016/j.toxicon.2016.11.261_bib35) 2010; 10
Schwartz (10.1016/j.toxicon.2016.11.261_bib45) 2007; 8
Kastin (10.1016/j.toxicon.2016.11.261_bib30) 2013
Almeida (10.1016/j.toxicon.2016.11.261_bib5) 2012; 13
Ma (10.1016/j.toxicon.2016.11.261_bib33) 2012; 75
Hanen (10.1016/j.toxicon.2016.11.261_bib24) 2011
Borchani (10.1016/j.toxicon.2016.11.261_bib10) 2013; 68
Higa (10.1016/j.toxicon.2016.11.261_bib27) 2014
D'Suze (10.1016/j.toxicon.2016.11.261_bib17) 2009; 91
Díaz-García (10.1016/j.toxicon.2016.11.261_bib20) 2015; 6
Ma (10.1016/j.toxicon.2016.11.261_bib34) 2009; 10
Abdel-Rahman (10.1016/j.toxicon.2016.11.261_bib2) 2016
Van Vaerenbergh (10.1016/j.toxicon.2016.11.261_bib51) 2015; 63
Bouzid (10.1016/j.toxicon.2016.11.261_bib12) 2013; 70
He (10.1016/j.toxicon.2016.11.261_bib26) 2013; 89
Incamnoi (10.1016/j.toxicon.2016.11.261_bib28) 2013; 61
Yang (10.1016/j.toxicon.2016.11.261_bib54) 2015; 12
Zeng (10.1016/j.toxicon.2016.11.261_bib56) 2004; 25
Shahbazzadeh (10.1016/j.toxicon.2016.11.261_bib47) 2007; 404
Almaaytah (10.1016/j.toxicon.2016.11.261_bib3) 2014; 51
Rouault (10.1016/j.toxicon.2016.11.261_bib43) 2003; 42
Harrison (10.1016/j.toxicon.2016.11.261_bib25) 2016; 117
Possani (10.1016/j.toxicon.2016.11.261_bib39) 1999; 264
de la Vega (10.1016/j.toxicon.2016.11.261_bib18) 2010; 56
Alvarenga (10.1016/j.toxicon.2016.11.261_bib6) 2012
Borchani (10.1016/j.toxicon.2016.11.261_bib11) 2011; 58
Morgenstern (10.1016/j.toxicon.2016.11.261_bib37) 2011; 57
Chen (10.1016/j.toxicon.2016.11.261_bib14) 2005; 26
Conde (10.1016/j.toxicon.2016.11.261_bib16) 1999; 460
Seyedian (10.1016/j.toxicon.2016.11.261_bib46) 2010; 56
Almaaytah (10.1016/j.toxicon.2016.11.261_bib4) 2012; 35
Zobel-Thropp (10.1016/j.toxicon.2016.11.261_bib57) 2013; 13
Angeloni (10.1016/j.toxicon.2016.11.261_bib7) 2011; 11
Diego-García (10.1016/j.toxicon.2016.11.261_bib21) 2008; 65
Ruiming (10.1016/j.toxicon.2016.11.261_bib44) 2010; 11
Luna-Ramírez (10.1016/j.toxicon.2016.11.261_bib31) 2015; 10
Batista (10.1016/j.toxicon.2016.11.261_bib8) 2006; 6
Silva (10.1016/j.toxicon.2016.11.261_bib48) 2009; 54
Machado (10.1016/j.toxicon.2016.11.261_bib36) 2016; 119
28192687 - Toxicon. 2017 Mar 15;128:60
References_xml – volume: 107
  start-page: 71
  year: 2008
  end-page: 79
  ident: bib15
  article-title: Epidemiology of scorpionism: a global appraisal
  publication-title: Acta Trop.
– volume: 76
  start-page: 234
  year: 2013
  end-page: 238
  ident: bib53
  article-title: Cloning and molecular characterization of BumaMPs1, a novel metalloproteinases from the venom of scorpion Buthus martensi Karsch
  publication-title: Toxicon
– volume: 68
  start-page: 30
  year: 2013
  end-page: 39
  ident: bib10
  article-title: The pathological effects of Heminecrolysin, a dermonecrotic toxin from Hemiscorpius lepturus scorpion venom are mediated through its lysophospholipase D activity
  publication-title: Toxicon
– volume: 51
  start-page: 35
  year: 2014
  end-page: 45
  ident: bib3
  article-title: Scorpion venom peptides with no disulfide bridges: a review
  publication-title: Peptides
– volume: 70
  start-page: 70
  year: 2013
  end-page: 81
  ident: bib12
  article-title: Profiling the venom gland transcriptome of Tetramorium bicarinatum (Hymenoptera: Formicidae): the first transcriptome analysis of an ant species
  publication-title: Toxicon
– year: 2013
  ident: bib30
  article-title: Handbook of Biologically Active Peptides
– volume: 13
  start-page: 1
  year: 2012
  ident: bib5
  article-title: Profiling the resting venom gland of the scorpion Tityus stigmurus through a transcriptomic survey
  publication-title: BMC Genom.
– volume: 61
  start-page: 62
  year: 2013
  end-page: 71
  ident: bib28
  article-title: Heteromtoxin (HmTx), a novel heterodimeric phospholipase A 2 from Heterometrus laoticus scorpion venom
  publication-title: Toxicon
– volume: 13
  start-page: 817
  year: 2013
  end-page: 835
  ident: bib57
  article-title: Spit and venom from Scytodes spiders: a diverse and distinct cocktail
  publication-title: J. Proteome Res.
– year: 2011
  ident: bib24
  article-title: A New Chymotrypsin-like Serine Protease Involved in Dietary Protein Digestion in a Primitive Animal, Scorpio Maurus: Purification and Biochemical Characterization
– volume: 105
  start-page: 34
  year: 2015
  end-page: 44
  ident: bib29
  article-title: Hemilipin, a novel Hemiscorpius lepturus venom heterodimeric phospholipase A2, which inhibits angiogenesis in vitro and in vivo
  publication-title: Toxicon
– volume: 117
  start-page: 30
  year: 2016
  end-page: 36
  ident: bib25
  article-title: Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus
  publication-title: Toxicon
– volume: 111
  start-page: 224
  year: 2014
  end-page: 237
  ident: bib23
  article-title: Proteomic characterization of the venom and transcriptomic analysis of the venomous gland from the Mexican centipede Scolopendra viridis
  publication-title: J. Proteom.
– volume: 28
  start-page: 4004
  year: 2014
  end-page: 4014
  ident: bib55
  article-title: A camelid antibody candidate for development of a therapeutic agent against Hemiscorpius lepturus envenomation
  publication-title: FASEB J.
– start-page: 134
  year: 2010
  ident: bib52
  article-title: WHO Guidelines for the Production, Control and Regulation of Snake Antivenom Immunoglobulins
– volume: 43
  start-page: 865
  year: 2004
  end-page: 875
  ident: bib19
  article-title: Current views on scorpion toxins specific for K+-channels
  publication-title: Toxicon
– volume: 110
  start-page: 8906
  year: 2013
  end-page: 8911
  ident: bib49
  article-title: Multiple actions of φ-LITX-Lw1a on ryanodine receptors reveal a functional link between scorpion DDH and ICK toxins
  publication-title: Proc. Natl. Acad. Sci.
– volume: 275
  start-page: 4641
  year: 2008
  end-page: 4650
  ident: bib50
  article-title: Hemitoxin, the first potassium channel toxin from the venom of the Iranian scorpion Hemiscorpius lepturus
  publication-title: FeBS J.
– volume: 54
  start-page: 252
  year: 2009
  end-page: 261
  ident: bib48
  article-title: Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum
  publication-title: Toxicon
– year: 2012
  ident: bib6
  article-title: Transcriptome Analysis of the Tityus Serrulatus Scorpion Venom Gland
– volume: 460
  start-page: 447
  year: 1999
  end-page: 450
  ident: bib16
  article-title: Phospholipin, a novel heterodimeric phospholipase A2 from Pandinus imperator scorpion venom
  publication-title: FEBS Lett.
– volume: 63
  start-page: 44
  year: 2013
  end-page: 54
  ident: bib32
  article-title: Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity
  publication-title: Toxicon
– volume: 65
  start-page: 187
  year: 2008
  end-page: 200
  ident: bib21
  article-title: Cytolytic and K+ channel blocking activities of β-KTx and scorpine-like peptides purified from scorpion venoms
  publication-title: Cell. Mol. Life Sci.
– volume: 119
  start-page: 362
  year: 2016
  end-page: 370
  ident: bib36
  article-title: Characterization of TistH, a multifunctional peptide from the scorpion Tityus stigmurus: structure, cytotoxicity and antimicrobial activity
  publication-title: Toxicon
– volume: 404
  start-page: 89
  year: 2007
  end-page: 96
  ident: bib47
  article-title: Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels
  publication-title: Biochem. J.
– volume: 11
  start-page: 1
  year: 2010
  ident: bib44
  article-title: Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components
  publication-title: BMC Genom.
– volume: 12
  start-page: 7
  year: 2015
  end-page: 8
  ident: bib54
  article-title: The I-TASSER Suite: protein structure and function prediction
  publication-title: Nat. Methods
– volume: 35
  start-page: 291
  year: 2012
  end-page: 299
  ident: bib4
  article-title: Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog
  publication-title: Peptides
– volume: 264
  start-page: 287
  year: 1999
  end-page: 300
  ident: bib39
  article-title: Scorpion toxins specific for Na+-channels
  publication-title: Eur. J. Biochem.
– volume: 11
  start-page: 662
  year: 2011
  end-page: 674
  ident: bib7
  article-title: De novo transcriptome characterization and development of genomic tools for Scabiosa columbaria L. using next-generation sequencing techniques
  publication-title: Mol. Ecol. Resour.
– volume: 10
  start-page: 2471
  year: 2010
  end-page: 2485
  ident: bib35
  article-title: Molecular diversity of toxic components from the scorpion Heterometrus petersii venom revealed by proteomic and transcriptome analysis
  publication-title: Proteomics
– volume: 163
  start-page: 179
  year: 2014
  end-page: 184
  ident: bib42
  article-title: Cross-reactivity between Anisakis spp. and wasp venom allergens
  publication-title: Int. Archives Allergy Immunol.
– volume: 803
  start-page: 55
  year: 2004
  end-page: 66
  ident: bib9
  article-title: Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and the role of prolines on mass spectrometry analysis of toxins
  publication-title: J. Chromatogr. B
– volume: 7
  start-page: e43331
  year: 2012
  ident: bib41
  article-title: Global transcriptome analysis of the scorpion Centruroides noxius: new toxin families and evolutionary insights from an ancestral scorpion species
  publication-title: PloS one
– volume: 6
  start-page: 11
  year: 2015
  ident: bib20
  article-title: Enzymatic analysis of venom from Cuban scorpion Rhopalurus junceus
  publication-title: J. Venom Res.
– volume: 93
  start-page: 125
  year: 2015
  end-page: 135
  ident: bib38
  article-title: Scorpion venom components as potential candidates for drug development
  publication-title: Toxicon
– volume: 56
  start-page: 1155
  year: 2010
  end-page: 1161
  ident: bib18
  article-title: Mining on scorpion venom biodiversity
  publication-title: Toxicon
– volume: 75
  start-page: 1563
  year: 2012
  end-page: 1576
  ident: bib33
  article-title: Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: implication for proteome evolution of scorpion venom arsenal
  publication-title: J. Proteom.
– volume: 57
  start-page: 695
  year: 2011
  end-page: 703
  ident: bib37
  article-title: The tale of a resting gland: transcriptome of a replete venom gland from the scorpion Hottentotta judaicus
  publication-title: Toxicon
– volume: 63
  start-page: 449
  year: 2015
  end-page: 455
  ident: bib51
  article-title: IgE recognition of chimeric isoforms of the honeybee (Apis mellifera) venom allergen Api m 10 evaluated by protein array technology
  publication-title: Mol. Immunol.
– volume: 12
  start-page: 313
  year: 2012
  end-page: 328
  ident: bib22
  article-title: Molecular diversity of the telson and venom components from Pandinus cavimanus (Scorpionidae Latreille 1802): transcriptome, venomics and function
  publication-title: Proteomics
– volume: 58
  start-page: 130
  year: 2011
  end-page: 139
  ident: bib11
  article-title: Heminecrolysin, the first hemolytic dermonecrotic toxin purified from scorpion venom
  publication-title: Toxicon
– volume: 26
  start-page: 731
  year: 2005
  end-page: 736
  ident: bib14
  article-title: Molecular cloning of a novel putative potassium channel-blocking neurotoxin from the venom of the North African scorpion, Androctonus amoreuxi
  publication-title: Peptides
– volume: 10
  start-page: e0117188
  year: 2015
  ident: bib40
  article-title: Transcriptome analysis of scorpion species belonging to the Vaejovis genus
  publication-title: PloS one
– volume: 6
  start-page: 3718
  year: 2006
  end-page: 3727
  ident: bib8
  article-title: Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins
  publication-title: Proteomics
– volume: 115
  start-page: 115
  year: 2003
  end-page: 121
  ident: bib13
  article-title: Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom
  publication-title: Regul. Pept.
– volume: 91
  start-page: 1010
  year: 2009
  end-page: 1019
  ident: bib17
  article-title: Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans
  publication-title: Biochimie
– volume: 89
  start-page: 1
  year: 2013
  end-page: 14
  ident: bib26
  article-title: Molecular diversity of Chaerilidae venom peptides reveals the dynamic evolution of scorpion venom components from Buthidae to non-Buthidae
  publication-title: J. Proteom.
– volume: 10
  start-page: 290
  year: 2009
  ident: bib34
  article-title: Transcriptome analysis of the venom gland of the scorpion Scorpiops jendeki: implication for the evolution of the scorpion venom arsenal
  publication-title: BMC Genom.
– volume: 74
  start-page: 193
  year: 2013
  end-page: 207
  ident: bib1
  article-title: Venom proteomic and venomous glands transcriptomic analysis of the Egyptian scorpion Scorpio maurus palmatus (Arachnida: Scorpionidae)
  publication-title: Toxicon
– volume: 25
  start-page: 143
  year: 2004
  end-page: 150
  ident: bib56
  article-title: Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch
  publication-title: Peptides
– start-page: 1
  year: 2014
  ident: bib27
  article-title: Degradation of Aα and Bβ chains from bovine fibrinogen by serine proteases of the Amazonian scorpion Brotheas amazonicus
  publication-title: BMC Proc. Biomed. Cent.
– volume: 8
  start-page: 1
  year: 2007
  ident: bib45
  article-title: Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones)
  publication-title: BMC Genom.
– volume: 56
  start-page: 521
  year: 2010
  end-page: 525
  ident: bib46
  article-title: Enzymatic analysis of Hemiscorpius lepturus scorpion venom using zymography and venom-specific antivenin
  publication-title: Toxicon
– start-page: 105
  year: 2016
  end-page: 124
  ident: bib2
  article-title: Scorpion venom gland transcriptomics and proteomics: an overview
  publication-title: Venom Genom. Proteom.
– volume: 10
  start-page: e0127883
  year: 2015
  ident: bib31
  article-title: Whole transcriptome of the venom gland from Urodacus yaschenkoi scorpion
  publication-title: PloS one
– volume: 42
  start-page: 11494
  year: 2003
  end-page: 11503
  ident: bib43
  article-title: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity
  publication-title: Biochemistry
– volume: 105
  start-page: 34
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib29
  article-title: Hemilipin, a novel Hemiscorpius lepturus venom heterodimeric phospholipase A2, which inhibits angiogenesis in vitro and in vivo
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2015.08.022
– year: 2012
  ident: 10.1016/j.toxicon.2016.11.261_bib6
– volume: 63
  start-page: 449
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib51
  article-title: IgE recognition of chimeric isoforms of the honeybee (Apis mellifera) venom allergen Api m 10 evaluated by protein array technology
  publication-title: Mol. Immunol.
  doi: 10.1016/j.molimm.2014.09.018
– volume: 51
  start-page: 35
  year: 2014
  ident: 10.1016/j.toxicon.2016.11.261_bib3
  article-title: Scorpion venom peptides with no disulfide bridges: a review
  publication-title: Peptides
  doi: 10.1016/j.peptides.2013.10.021
– volume: 12
  start-page: 7
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib54
  article-title: The I-TASSER Suite: protein structure and function prediction
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.3213
– volume: 264
  start-page: 287
  year: 1999
  ident: 10.1016/j.toxicon.2016.11.261_bib39
  article-title: Scorpion toxins specific for Na+-channels
  publication-title: Eur. J. Biochem.
  doi: 10.1046/j.1432-1327.1999.00625.x
– volume: 89
  start-page: 1
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib26
  article-title: Molecular diversity of Chaerilidae venom peptides reveals the dynamic evolution of scorpion venom components from Buthidae to non-Buthidae
  publication-title: J. Proteom.
  doi: 10.1016/j.jprot.2013.06.007
– volume: 25
  start-page: 143
  year: 2004
  ident: 10.1016/j.toxicon.2016.11.261_bib56
  article-title: Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch
  publication-title: Peptides
  doi: 10.1016/j.peptides.2003.12.003
– volume: 117
  start-page: 30
  year: 2016
  ident: 10.1016/j.toxicon.2016.11.261_bib25
  article-title: Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2016.03.014
– volume: 43
  start-page: 865
  year: 2004
  ident: 10.1016/j.toxicon.2016.11.261_bib19
  article-title: Current views on scorpion toxins specific for K+-channels
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2004.03.022
– volume: 115
  start-page: 115
  year: 2003
  ident: 10.1016/j.toxicon.2016.11.261_bib13
  article-title: Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins and parallel cloning of their respective cDNAs from a single sample of venom
  publication-title: Regul. Pept.
  doi: 10.1016/S0167-0115(03)00146-0
– volume: 42
  start-page: 11494
  year: 2003
  ident: 10.1016/j.toxicon.2016.11.261_bib43
  article-title: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity
  publication-title: Biochemistry
  doi: 10.1021/bi0349930
– volume: 11
  start-page: 662
  year: 2011
  ident: 10.1016/j.toxicon.2016.11.261_bib7
  article-title: De novo transcriptome characterization and development of genomic tools for Scabiosa columbaria L. using next-generation sequencing techniques
  publication-title: Mol. Ecol. Resour.
  doi: 10.1111/j.1755-0998.2011.02990.x
– start-page: 1
  year: 2014
  ident: 10.1016/j.toxicon.2016.11.261_bib27
  article-title: Degradation of Aα and Bβ chains from bovine fibrinogen by serine proteases of the Amazonian scorpion Brotheas amazonicus
  publication-title: BMC Proc. Biomed. Cent.
– volume: 10
  start-page: 290
  year: 2009
  ident: 10.1016/j.toxicon.2016.11.261_bib34
  article-title: Transcriptome analysis of the venom gland of the scorpion Scorpiops jendeki: implication for the evolution of the scorpion venom arsenal
  publication-title: BMC Genom.
  doi: 10.1186/1471-2164-10-290
– volume: 110
  start-page: 8906
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib49
  article-title: Multiple actions of φ-LITX-Lw1a on ryanodine receptors reveal a functional link between scorpion DDH and ICK toxins
  publication-title: Proc. Natl. Acad. Sci.
  doi: 10.1073/pnas.1214062110
– volume: 8
  start-page: 1
  year: 2007
  ident: 10.1016/j.toxicon.2016.11.261_bib45
  article-title: Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones)
  publication-title: BMC Genom.
  doi: 10.1186/1471-2164-8-119
– volume: 26
  start-page: 731
  year: 2005
  ident: 10.1016/j.toxicon.2016.11.261_bib14
  article-title: Molecular cloning of a novel putative potassium channel-blocking neurotoxin from the venom of the North African scorpion, Androctonus amoreuxi
  publication-title: Peptides
  doi: 10.1016/j.peptides.2004.12.002
– volume: 10
  start-page: 2471
  year: 2010
  ident: 10.1016/j.toxicon.2016.11.261_bib35
  article-title: Molecular diversity of toxic components from the scorpion Heterometrus petersii venom revealed by proteomic and transcriptome analysis
  publication-title: Proteomics
  doi: 10.1002/pmic.200900763
– volume: 93
  start-page: 125
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib38
  article-title: Scorpion venom components as potential candidates for drug development
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2014.11.233
– volume: 35
  start-page: 291
  year: 2012
  ident: 10.1016/j.toxicon.2016.11.261_bib4
  article-title: Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog
  publication-title: Peptides
  doi: 10.1016/j.peptides.2012.03.016
– volume: 57
  start-page: 695
  year: 2011
  ident: 10.1016/j.toxicon.2016.11.261_bib37
  article-title: The tale of a resting gland: transcriptome of a replete venom gland from the scorpion Hottentotta judaicus
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2011.02.001
– volume: 275
  start-page: 4641
  year: 2008
  ident: 10.1016/j.toxicon.2016.11.261_bib50
  article-title: Hemitoxin, the first potassium channel toxin from the venom of the Iranian scorpion Hemiscorpius lepturus
  publication-title: FeBS J.
  doi: 10.1111/j.1742-4658.2008.06607.x
– volume: 28
  start-page: 4004
  year: 2014
  ident: 10.1016/j.toxicon.2016.11.261_bib55
  article-title: A camelid antibody candidate for development of a therapeutic agent against Hemiscorpius lepturus envenomation
  publication-title: FASEB J.
  doi: 10.1096/fj.13-247478
– volume: 74
  start-page: 193
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib1
  article-title: Venom proteomic and venomous glands transcriptomic analysis of the Egyptian scorpion Scorpio maurus palmatus (Arachnida: Scorpionidae)
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2013.08.064
– volume: 6
  start-page: 3718
  year: 2006
  ident: 10.1016/j.toxicon.2016.11.261_bib8
  article-title: Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins
  publication-title: Proteomics
  doi: 10.1002/pmic.200500525
– volume: 7
  start-page: e43331
  year: 2012
  ident: 10.1016/j.toxicon.2016.11.261_bib41
  article-title: Global transcriptome analysis of the scorpion Centruroides noxius: new toxin families and evolutionary insights from an ancestral scorpion species
  publication-title: PloS one
  doi: 10.1371/journal.pone.0043331
– year: 2011
  ident: 10.1016/j.toxicon.2016.11.261_bib24
– volume: 12
  start-page: 313
  year: 2012
  ident: 10.1016/j.toxicon.2016.11.261_bib22
  article-title: Molecular diversity of the telson and venom components from Pandinus cavimanus (Scorpionidae Latreille 1802): transcriptome, venomics and function
  publication-title: Proteomics
  doi: 10.1002/pmic.201100409
– volume: 13
  start-page: 1
  year: 2012
  ident: 10.1016/j.toxicon.2016.11.261_bib5
  article-title: Profiling the resting venom gland of the scorpion Tityus stigmurus through a transcriptomic survey
  publication-title: BMC Genom.
  doi: 10.1186/1471-2164-13-362
– volume: 10
  start-page: e0117188
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib40
  article-title: Transcriptome analysis of scorpion species belonging to the Vaejovis genus
  publication-title: PloS one
  doi: 10.1371/journal.pone.0117188
– volume: 11
  start-page: 1
  year: 2010
  ident: 10.1016/j.toxicon.2016.11.261_bib44
  article-title: Comparative venom gland transcriptome analysis of the scorpion Lychas mucronatus reveals intraspecific toxic gene diversity and new venomous components
  publication-title: BMC Genom.
  doi: 10.1186/1471-2164-11-452
– volume: 111
  start-page: 224
  year: 2014
  ident: 10.1016/j.toxicon.2016.11.261_bib23
  article-title: Proteomic characterization of the venom and transcriptomic analysis of the venomous gland from the Mexican centipede Scolopendra viridis
  publication-title: J. Proteom.
  doi: 10.1016/j.jprot.2014.04.033
– volume: 75
  start-page: 1563
  year: 2012
  ident: 10.1016/j.toxicon.2016.11.261_bib33
  article-title: Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: implication for proteome evolution of scorpion venom arsenal
  publication-title: J. Proteom.
  doi: 10.1016/j.jprot.2011.11.029
– volume: 76
  start-page: 234
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib53
  article-title: Cloning and molecular characterization of BumaMPs1, a novel metalloproteinases from the venom of scorpion Buthus martensi Karsch
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2013.10.006
– volume: 119
  start-page: 362
  year: 2016
  ident: 10.1016/j.toxicon.2016.11.261_bib36
  article-title: Characterization of TistH, a multifunctional peptide from the scorpion Tityus stigmurus: structure, cytotoxicity and antimicrobial activity
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2016.06.002
– volume: 54
  start-page: 252
  year: 2009
  ident: 10.1016/j.toxicon.2016.11.261_bib48
  article-title: Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2009.04.010
– volume: 56
  start-page: 521
  year: 2010
  ident: 10.1016/j.toxicon.2016.11.261_bib46
  article-title: Enzymatic analysis of Hemiscorpius lepturus scorpion venom using zymography and venom-specific antivenin
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2010.05.008
– volume: 91
  start-page: 1010
  year: 2009
  ident: 10.1016/j.toxicon.2016.11.261_bib17
  article-title: Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2009.05.005
– volume: 10
  start-page: e0127883
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib31
  article-title: Whole transcriptome of the venom gland from Urodacus yaschenkoi scorpion
  publication-title: PloS one
  doi: 10.1371/journal.pone.0127883
– volume: 13
  start-page: 817
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib57
  article-title: Spit and venom from Scytodes spiders: a diverse and distinct cocktail
  publication-title: J. Proteome Res.
  doi: 10.1021/pr400875s
– start-page: 134
  year: 2010
  ident: 10.1016/j.toxicon.2016.11.261_bib52
– volume: 107
  start-page: 71
  year: 2008
  ident: 10.1016/j.toxicon.2016.11.261_bib15
  article-title: Epidemiology of scorpionism: a global appraisal
  publication-title: Acta Trop.
  doi: 10.1016/j.actatropica.2008.05.021
– volume: 56
  start-page: 1155
  year: 2010
  ident: 10.1016/j.toxicon.2016.11.261_bib18
  article-title: Mining on scorpion venom biodiversity
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2009.11.010
– volume: 63
  start-page: 44
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib32
  article-title: Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2012.11.017
– volume: 460
  start-page: 447
  year: 1999
  ident: 10.1016/j.toxicon.2016.11.261_bib16
  article-title: Phospholipin, a novel heterodimeric phospholipase A2 from Pandinus imperator scorpion venom
  publication-title: FEBS Lett.
  doi: 10.1016/S0014-5793(99)01392-7
– volume: 65
  start-page: 187
  year: 2008
  ident: 10.1016/j.toxicon.2016.11.261_bib21
  article-title: Cytolytic and K+ channel blocking activities of β-KTx and scorpine-like peptides purified from scorpion venoms
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-007-7370-x
– volume: 58
  start-page: 130
  year: 2011
  ident: 10.1016/j.toxicon.2016.11.261_bib11
  article-title: Heminecrolysin, the first hemolytic dermonecrotic toxin purified from scorpion venom
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2011.05.016
– volume: 404
  start-page: 89
  year: 2007
  ident: 10.1016/j.toxicon.2016.11.261_bib47
  article-title: Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels
  publication-title: Biochem. J.
  doi: 10.1042/BJ20061404
– volume: 70
  start-page: 70
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib12
  article-title: Profiling the venom gland transcriptome of Tetramorium bicarinatum (Hymenoptera: Formicidae): the first transcriptome analysis of an ant species
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2013.03.010
– start-page: 105
  year: 2016
  ident: 10.1016/j.toxicon.2016.11.261_bib2
  article-title: Scorpion venom gland transcriptomics and proteomics: an overview
  publication-title: Venom Genom. Proteom.
  doi: 10.1007/978-94-007-6416-3_29
– volume: 803
  start-page: 55
  year: 2004
  ident: 10.1016/j.toxicon.2016.11.261_bib9
  article-title: Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and the role of prolines on mass spectrometry analysis of toxins
  publication-title: J. Chromatogr. B
  doi: 10.1016/j.jchromb.2003.09.002
– year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib30
– volume: 6
  start-page: 11
  year: 2015
  ident: 10.1016/j.toxicon.2016.11.261_bib20
  article-title: Enzymatic analysis of venom from Cuban scorpion Rhopalurus junceus
  publication-title: J. Venom Res.
– volume: 61
  start-page: 62
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib28
  article-title: Heteromtoxin (HmTx), a novel heterodimeric phospholipase A 2 from Heterometrus laoticus scorpion venom
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2012.10.012
– volume: 68
  start-page: 30
  year: 2013
  ident: 10.1016/j.toxicon.2016.11.261_bib10
  article-title: The pathological effects of Heminecrolysin, a dermonecrotic toxin from Hemiscorpius lepturus scorpion venom are mediated through its lysophospholipase D activity
  publication-title: Toxicon
  doi: 10.1016/j.toxicon.2013.03.012
– volume: 163
  start-page: 179
  year: 2014
  ident: 10.1016/j.toxicon.2016.11.261_bib42
  article-title: Cross-reactivity between Anisakis spp. and wasp venom allergens
  publication-title: Int. Archives Allergy Immunol.
  doi: 10.1159/000358060
– reference: 28192687 - Toxicon. 2017 Mar 15;128:60
SSID ssj0003896
Score 2.3622355
Snippet Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The...
Hemiscorpius lepturus scorpion is one of the most venomous members of the Hemiscorpiidae family. H. lepturus is distributed in Iran, Iraq and Yemen. The...
SourceID proquest
pubmed
crossref
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 123
SubjectTerms allergens
Animals
antimicrobial peptides
Arthropod Proteins - chemistry
bioactive compounds
calcium channels
Computational Biology
Gene Expression Profiling
health services
Hemiscorpius lepturus
High-Throughput Nucleotide Sequencing
Iran
Iranian scorpion
Iraq
metalloproteinases
nucleotide sequences
phospholipases
potassium channels
RNAseq
Scorpion Venoms - chemistry
Scorpiones
Scorpions - metabolism
Sequence Analysis, RNA
toxins
Transcriptome
Transcriptome analysis
transcriptomics
venoms
Yemen
Title The first report on transcriptome analysis of the venom gland of Iranian scorpion, Hemiscorpius lepturus
URI https://dx.doi.org/10.1016/j.toxicon.2016.11.261
https://www.ncbi.nlm.nih.gov/pubmed/27914888
https://www.proquest.com/docview/1846027129
https://www.proquest.com/docview/2116918270
Volume 125
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Na9swFBelu_RSunZb0y9UGD3FiT-eZekYykrasdJDC70JS5ZoSmOH2oHlsr99T7KdsEMo7GhbAqH3_N7vJ70PQr6niCIMsxCYTKQBIKINuDBJYIVh6LBzkfquJb_u2fQJ7p7T5x1y3efCuLDKzva3Nt1b6-7NuNvN8WI2czm-ELkKaYgoQgTlLtEcIHNaPvqzCfNAh8zaW2ZHm8Nok8Uzfh011e-Zo53oBRkaj1HMom3-aRv-9H7o5oDsdwCSTto1fiY7pjwkR5MSyfN8Ra-oD-n0Z-WH5OqhLUy9GtLHTZ5VPfTD1iWrV0fkBT9TO0MkSNtLBFqVtHFuzBuVam5o3lUvoZWlCBopGslqTn0HEPfqFgejptEa2ewCZT2kU9dJzj8ta_pmFujblvUX8nTz4_F6GnQ9GAINDJogVcB4Wug0CbXQSgEoy41FlBbbJEHxM8MBbKRFlCuRuxOUONQKilzo2BZh8pXsllVpjgkFbZSIQ6ELUJDoTGVcpbxQUZGYIsqjAYF-56XuCpS7Phlvso9Ee5WdwKQTGJIXiQIbkNF62qKt0PHRBN6LVf6jahK9yEdTL3s1kG4PXYBaaaplLZEoM2T4iJ62j0GuzQTyuSwckG-tDq1XHGcCiSnnJ_-_uFOyFzvM4c-Hzshu874054iYGnXhf4kL8mly-3N6_xdn2BhG
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Na9swFH906WG7jK3dR_bRajB6ihN_SLJ1DKXFWduwQwq9CUuWaUpjh9mB5b_fk2yn7BAKPdqWQOg9v_f7Se8D4CdDFGF4QT0TC-ZRRLReIkzkFcJwdNiZYK5ryc2cp7f01x27O4DzPhfGhlV2tr-16c5ad28m3W5O1sulzfGlga2QhojCR1DOXsGhrU7FBnA4nV2l851BRp_M24tmy5z94CmRZ_Iwbqq_S8s80RFytB_jkAf7XNQ-COpc0eU7eNthSDJtl_keDkx5BMfTEvnzakvOiIvqdMflR3D2u61NvR2RxVOqVT1yw3ZVq7fHcI-fSbFEMEjaewRSlaSxnszZlWplSNYVMCFVQRA3ErST1Yq4JiD21QwHo7KRGgntGsU9IqltJueeNjV5NGt0b5v6A9xeXizOU69rw-BpymnjMUV5wnLNIl8LrRSlqkhMgUAtLKIINYCbhNIi0CLIlMjsIUroa0XzTOiwyP3oIwzKqjSfgVBtlAh9oXOqaKRjFSeKJbkK8sjkQRYMgfY7L3VXo9y2yniUfTDag-wEJq3AkL9IFNgQxrtp67ZIx3MTkl6s8j9tk-hInpv6o1cDaffQxqiVptrUErkyR5KPAGr_GKTbXCCli_0hfGp1aLfiMBbITZPky8sXdwqv08XNtbyeza--wpvQQhB3XPQNBs2fjfmOAKpRJ90P8g_o3Br3
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=The+first+report+on+transcriptome+analysis+of+the+venom+gland+of+Iranian+scorpion%2C+Hemiscorpius+lepturus&rft.jtitle=Toxicon+%28Oxford%29&rft.au=Kazemi-Lomedasht%2C+Fatemeh&rft.au=Khalaj%2C+Vahid&rft.au=Bagheri%2C+Kamran+Pooshang&rft.au=Behdani%2C+Mahdi&rft.date=2017-01-01&rft.eissn=1879-3150&rft.volume=125&rft.spage=123&rft.epage=130&rft_id=info:doi/10.1016%2Fj.toxicon.2016.11.261&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0041-0101&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0041-0101&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0041-0101&client=summon