Pierisin, Cytotoxic and Apoptosis-Inducing DNA ADP-Ribosylating Protein in Cabbage Butterfly
Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological f...
Saved in:
Published in | Toxins Vol. 16; no. 6; p. 270 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
MDPI AG
14.06.2024
MDPI |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological function revealed that pierisin-1 binds to cell surface glycosphingolipids on the C-terminal side, is taken up into the cell, and is cleaved to N- and C-terminal portions, where the N-terminal portion mono-ADP-ribosylates the guanine base of DNA in the presence of NAD to induce cellular genetic mutation and apoptosis. Unlike other ADP-ribosyltransferases, pieisin-1 was first found to exhibit DNA mono-ADP-ribosylating activity and show anti-cancer activity in vitro and in vivo against various cancer cell lines. Pierisin-1 was most abundantly produced during the transition from the final larval stage to the pupal stage of the cabbage butterfly, and this production was regulated by ecdysteroid hormones. This suggests that pierisn-1 might play a pivotal role in the process of metamorphosis. Moreover, pierisin-1 could contribute as a defense factor against parasitization and microbial infections in the cabbage butterfly. Pierisin-like proteins in butterflies were shown to be present not only among the subtribe Pierina but also among the subtribes Aporiina and Appiadina, and pierisin-2, -3, and -4 were identified in these butterflies. Furthermore, DNA ADP-ribosylating activities were found in six different edible clams. Understanding of the biological nature of pierisin-1 with DNA mono-ADP-ribosylating activity could open up exciting avenues for research and potential therapeutic applications, making it a subject of great interest in the field of molecular biology and biotechnology. |
---|---|
AbstractList | Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological function revealed that pierisin-1 binds to cell surface glycosphingolipids on the C-terminal side, is taken up into the cell, and is cleaved to N- and C-terminal portions, where the N-terminal portion mono-ADP-ribosylates the guanine base of DNA in the presence of NAD to induce cellular genetic mutation and apoptosis. Unlike other ADP-ribosyltransferases, pieisin-1 was first found to exhibit DNA mono-ADP-ribosylating activity and show anti-cancer activity in vitro and in vivo against various cancer cell lines. Pierisin-1 was most abundantly produced during the transition from the final larval stage to the pupal stage of the cabbage butterfly, and this production was regulated by ecdysteroid hormones. This suggests that pierisn-1 might play a pivotal role in the process of metamorphosis. Moreover, pierisin-1 could contribute as a defense factor against parasitization and microbial infections in the cabbage butterfly. Pierisin-like proteins in butterflies were shown to be present not only among the subtribe Pierina but also among the subtribes Aporiina and Appiadina, and pierisin-2, -3, and -4 were identified in these butterflies. Furthermore, DNA ADP-ribosylating activities were found in six different edible clams. Understanding of the biological nature of pierisin-1 with DNA mono-ADP-ribosylating activity could open up exciting avenues for research and potential therapeutic applications, making it a subject of great interest in the field of molecular biology and biotechnology. Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological function revealed that pierisin-1 binds to cell surface glycosphingolipids on the C-terminal side, is taken up into the cell, and is cleaved to N- and C-terminal portions, where the N-terminal portion mono-ADP-ribosylates the guanine base of DNA in the presence of NAD to induce cellular genetic mutation and apoptosis. Unlike other ADP-ribosyltransferases, pieisin-1 was first found to exhibit DNA mono-ADP-ribosylating activity and show anti-cancer activity in vitro and in vivo against various cancer cell lines. Pierisin-1 was most abundantly produced during the transition from the final larval stage to the pupal stage of the cabbage butterfly, and this production was regulated by ecdysteroid hormones. This suggests that pierisn-1 might play a pivotal role in the process of metamorphosis. Moreover, pierisin-1 could contribute as a defense factor against parasitization and microbial infections in the cabbage butterfly. Pierisin-like proteins in butterflies were shown to be present not only among the subtribe Pierina but also among the subtribes Aporiina and Appiadina, and pierisin-2, -3, and -4 were identified in these butterflies. Furthermore, DNA ADP-ribosylating activities were found in six different edible clams. Understanding of the biological nature of pierisin-1 with DNA mono-ADP-ribosylating activity could open up exciting avenues for research and potential therapeutic applications, making it a subject of great interest in the field of molecular biology and biotechnology.Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological function revealed that pierisin-1 binds to cell surface glycosphingolipids on the C-terminal side, is taken up into the cell, and is cleaved to N- and C-terminal portions, where the N-terminal portion mono-ADP-ribosylates the guanine base of DNA in the presence of NAD to induce cellular genetic mutation and apoptosis. Unlike other ADP-ribosyltransferases, pieisin-1 was first found to exhibit DNA mono-ADP-ribosylating activity and show anti-cancer activity in vitro and in vivo against various cancer cell lines. Pierisin-1 was most abundantly produced during the transition from the final larval stage to the pupal stage of the cabbage butterfly, and this production was regulated by ecdysteroid hormones. This suggests that pierisn-1 might play a pivotal role in the process of metamorphosis. Moreover, pierisin-1 could contribute as a defense factor against parasitization and microbial infections in the cabbage butterfly. Pierisin-like proteins in butterflies were shown to be present not only among the subtribe Pierina but also among the subtribes Aporiina and Appiadina, and pierisin-2, -3, and -4 were identified in these butterflies. Furthermore, DNA ADP-ribosylating activities were found in six different edible clams. Understanding of the biological nature of pierisin-1 with DNA mono-ADP-ribosylating activity could open up exciting avenues for research and potential therapeutic applications, making it a subject of great interest in the field of molecular biology and biotechnology. Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological function revealed that pierisin-1 binds to cell surface glycosphingolipids on the C-terminal side, is taken up into the cell, and is cleaved to N- and C-terminal portions, where the N-terminal portion mono-ADP-ribosylates the guanine base of DNA in the presence of NAD to induce cellular genetic mutation and apoptosis. Unlike other ADP-ribosyltransferases, pieisin-1 was first found to exhibit DNA mono-ADP-ribosylating activity and show anti-cancer activity in vitro and in vivo against various cancer cell lines. Pierisin-1 was most abundantly produced during the transition from the final larval stage to the pupal stage of the cabbage butterfly, and this production was regulated by ecdysteroid hormones. This suggests that pierisn-1 might play a pivotal role in the process of metamorphosis. Moreover, pierisin-1 could contribute as a defense factor against parasitization and microbial infections in the cabbage butterfly. Pierisin-like proteins in butterflies were shown to be present not only among the subtribe Pierina but also among the subtribes Aporiina and Appiadina, and pierisin-2, -3, and -4 were identified in these butterflies. Furthermore, DNA ADP-ribosylating activities were found in six different edible clams. Understanding of the biological nature of pierisin-1 with DNA mono-ADP-ribosylating activity could open up exciting avenues for research and potential therapeutic applications, making it a subject of great interest in the field of molecular biology and biotechnology. Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer cell lines. This 98-kDa protein consists of the N-terminal region (27 kDa) and C-terminal region (71 kDa), and analysis of their biological function revealed that pierisin-1 binds to cell surface glycosphingolipids on the C-terminal side, is taken up into the cell, and is cleaved to N- and C-terminal portions, where the N-terminal portion mono-ADP-ribosylates the guanine base of DNA in the presence of NAD to induce cellular genetic mutation and apoptosis. Unlike other ADP-ribosyltransferases, pieisin-1 was first found to exhibit DNA mono-ADP-ribosylating activity and show anti-cancer activity in vitro and in vivo against various cancer cell lines. Pierisin-1 was most abundantly produced during the transition from the final larval stage to the pupal stage of the cabbage butterfly, and this production was regulated by ecdysteroid hormones. This suggests that pierisn-1 might play a pivotal role in the process of metamorphosis. Moreover, pierisin-1 could contribute as a defense factor against parasitization and microbial infections in the cabbage butterfly. Pierisin-like proteins in butterflies were shown to be present not only among the subtribe Pierina but also among the subtribes Aporiina and Appiadina, and pierisin-2, -3, and -4 were identified in these butterflies. Furthermore, DNA ADP-ribosylating activities were found in six different edible clams. Understanding of the biological nature of pierisin-1 with DNA mono-ADP-ribosylating activity could open up exciting avenues for research and potential therapeutic applications, making it a subject of great interest in the field of molecular biology and biotechnology. |
Audience | Academic |
Author | Azusa Takahashi-Nakaguchi Masafumi Yamamoto Yukari Totsuka Keiji Wakabayashi Yu Horiuchi |
AuthorAffiliation | 1 Medical Mycology Research Center, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8673, Japan 2 Aquatic Food Research Laboratory, Central Research Institute, Tokyo Innovation Center, Nissui Corporation, 1-32-3 Shichikoku, Hachioji City 192-0991, Japan 3 Central Institute for Experimental Medicine and Life Science, 3-25-12 Tonomachi, Kawasaki-ku, Kawasaki 210-0821, Japan 4 Department of Environmental Health Sciences, Hoshi University, 2-4-41 Ebara, Shinagawa-ku, Tokyo 142-8501, Japan 5 Graduate Division of Nutritional and Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan |
AuthorAffiliation_xml | – name: 3 Central Institute for Experimental Medicine and Life Science, 3-25-12 Tonomachi, Kawasaki-ku, Kawasaki 210-0821, Japan – name: 5 Graduate Division of Nutritional and Environmental Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan – name: 2 Aquatic Food Research Laboratory, Central Research Institute, Tokyo Innovation Center, Nissui Corporation, 1-32-3 Shichikoku, Hachioji City 192-0991, Japan – name: 1 Medical Mycology Research Center, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8673, Japan – name: 4 Department of Environmental Health Sciences, Hoshi University, 2-4-41 Ebara, Shinagawa-ku, Tokyo 142-8501, Japan |
Author_xml | – sequence: 1 fullname: Takahashi-Nakaguchi, Azusa – sequence: 2 fullname: Horiuchi, Yu – sequence: 3 fullname: Yamamoto, Masafumi – sequence: 4 fullname: Totsuka, Yukari – sequence: 5 fullname: Wakabayashi, Keiji |
BackLink | https://cir.nii.ac.jp/crid/1871147691550400256$$DView record in CiNii https://www.ncbi.nlm.nih.gov/pubmed/38922164$$D View this record in MEDLINE/PubMed |
BookMark | eNp1kstvEzEQhy1UREvolSNaCQ4c2OL37p5QSHlUqiACjkiWXxtcbexgexH57_EmfQWBbNnW-DffzNjzGBz54C0ATxE8I6SDr3P47XxCHHKIG_gAnGDY4Jpzho7unY_BaUpOQcoI4oSRR-CYtB3GiNMT8H3pbHTJ-VfVYpvDRNSV9Kaab8Imh-RSfeHNqJ1fVeef5tX8fFl_cSqk7SDzZFzGkK3zVZkLqZRc2ertmLON_bB9Ah72ckj29Hqfga_v331bfKwvP3-4WMwva81pk2vJGJKEG8KwwbzrDUdc9g3CJUlFcd8YbYhmreZ93yptFGSGKNhwxiFVZAYu9lQT5JXYRLeWcSuCdGJnCHElZMxOD1Z0imrGNYMtbCgkpm1bSlXDIGPcUDWx3uxZm1GtrdHW5yiHA-jhjXc_xCr8Eghh2MHCnIGX14QYfo42ZbF2SdthkN6GMQlSvgV3HO-kz_-SXoUx-vJSOxVv264jd6qVLBU434cSWE9QMW-6jjMCESqqs3-oyjB27XRpm94V-4HDs_uV3pZ40xpFQPcCHUNK0fZCu1z-PEyFu0EgKKYmFIdNeJfIrdsN-b8OL_YO3rkSYlpR2yBEG94hxsqbQsw4-QOs5Oa2 |
CitedBy_id | crossref_primary_10_3390_toxins16080331 |
Cites_doi | 10.1016/j.ijbiomac.2016.01.072 10.1128/AEM.68.10.4894-4899.2002 10.1016/j.cub.2019.10.009 10.4161/auto.4908 10.1073/pnas.0712221105 10.1111/j.1742-4658.2011.08182.x 10.1098/rstb.2019.0065 10.2165/00139709-200322010-00006 10.1016/j.cois.2020.09.004 10.1126/science.1072221 10.1073/pnas.1703449114 10.1128/jb.173.9.2776-2785.1991 10.1073/pnas.051628898 10.1074/jbc.M212114200 10.2183/pjab.83.175 10.1073/pnas.221444598 10.1074/jbc.M114.589846 10.1038/s41586-021-03825-4 10.1016/S0021-9258(19)35408-0 10.1007/s10709-011-9626-5 10.2183/pjab.73.192 10.3390/toxins13020151 10.1016/S0304-3835(98)00346-2 10.1016/S0021-9258(18)71671-2 10.1126/science.1095833 10.1016/j.chom.2019.01.014 10.1111/j.1432-1033.1990.tb19448.x 10.1038/287250a0 10.1016/0006-291X(65)90855-7 10.1111/1744-7917.13208 10.1016/0014-5793(89)80279-0 10.1016/j.molcel.2023.06.013 10.1146/annurev.nutr.19.1.485 10.1074/jbc.270.28.16775 10.1016/j.cois.2020.09.015 10.3390/toxins13010040 10.12688/f1000research.9765.1 10.1042/BSR20193405 10.1074/jbc.AC118.004412 10.1128/CMR.8.1.34 10.1074/jbc.273.45.29506 10.1016/S0006-291X(02)00815-X 10.3390/toxins15050304 10.1016/j.jinsphys.2013.08.014 10.3390/biology13030137 10.1073/pnas.0606140103 10.1021/tx034052o 10.1016/j.bbrc.2004.08.132 10.1128/jb.175.8.2314-2320.1993 10.1073/pnas.87.1.308 10.1021/bi971806n 10.1074/jbc.M401939200 10.1016/S0006-291X(02)02011-9 10.1016/j.toxicon.2012.11.019 10.1111/j.1349-7006.1996.tb03141.x 10.2174/1871520619666181127113848 10.1016/j.cbpb.2004.07.010 10.1016/S0021-9258(18)93347-8 10.1111/j.1365-2958.2006.05401.x 10.1007/82_2014_416 10.1016/j.jinsphys.2010.11.006 10.1042/BSR20203727 10.1128/iai.58.10.3173-3177.1990 10.1073/pnas.96.19.10608 10.1038/322390a0 10.1128/aem.56.12.3772-3778.1990 10.2183/pjab.78.305 10.1046/j.1432-1327.2000.01640.x 10.1093/jb/mvh062 10.2131/jts.31.123 10.1074/jbc.M117.776641 10.3389/fmolb.2022.944774 10.1093/genetics/125.2.275 10.1038/sj.cdd.4400767 10.1016/j.ygeno.2019.08.017 10.1016/j.molbiopara.2016.05.012 10.1016/S0006-291X(88)80849-0 10.1016/0165-1218(90)90100-G 10.1016/j.cbpb.2009.07.007 10.1021/bi035907z 10.1126/science.7878463 10.2307/3901826 10.1371/journal.pone.0060539 10.3389/fmicb.2019.03045 10.1111/j.1349-7006.1998.tb03297.x 10.1074/jbc.M108463200 10.1080/09687680410001663267 |
ContentType | Journal Article |
Copyright | COPYRIGHT 2024 MDPI AG 2024 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. 2024 by the authors. 2024 |
Copyright_xml | – notice: COPYRIGHT 2024 MDPI AG – notice: 2024 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: 2024 by the authors. 2024 |
DBID | RYH AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7T7 7U7 7X7 7XB 88E 8FD 8FE 8FH 8FI 8FJ 8FK ABUWG AEUYN AFKRA ATCPS AZQEC BBNVY BENPR BHPHI C1K CCPQU DWQXO FR3 FYUFA GHDGH GNUQQ HCIFZ K9. LK8 M0S M1P M7P P64 PATMY PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS PYCSY 7X8 5PM DOA |
DOI | 10.3390/toxins16060270 |
DatabaseName | CiNii Complete CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Industrial and Applied Microbiology Abstracts (Microbiology A) Toxicology Abstracts ProQuest Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Technology Research Database ProQuest SciTech Collection ProQuest Natural Science Journals ProQuest Hospital Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest One Sustainability (subscription) ProQuest Central UK/Ireland Agricultural & Environmental Science Collection ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection Environmental Sciences and Pollution Management ProQuest One ProQuest Central Engineering Research Database Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) Biological Sciences ProQuest Health & Medical Collection Medical Database Biological Science Database Biotechnology and BioEngineering Abstracts Environmental Science Database ProQuest Central Premium ProQuest One Academic Publicly Available Content Database (subscription) ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China Environmental Science Collection MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Publicly Available Content Database ProQuest Central Student Technology Research Database ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest Central ProQuest One Applied & Life Sciences ProQuest One Sustainability ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Health & Medical Research Collection Agricultural & Environmental Science Collection Biological Science Collection Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (New) ProQuest Medical Library (Alumni) ProQuest Biological Science Collection Toxicology Abstracts ProQuest One Academic Eastern Edition ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest SciTech Collection ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts Environmental Science Collection ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition Environmental Science Database Engineering Research Database ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
DatabaseTitleList | Publicly Available Content Database MEDLINE - Academic MEDLINE CrossRef |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 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: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Medicine Anatomy & Physiology |
EISSN | 2072-6651 |
ExternalDocumentID | oai_doaj_org_article_9b4c56c50807403d88844b750556d4bb PMC11209040 A799653011 38922164 10_3390_toxins16060270 |
Genre | Research Support, Non-U.S. Gov't Journal Article Review |
GeographicLocations | Japan |
GeographicLocations_xml | – name: Japan |
GrantInformation_xml | – fundername: Shionogi (Japan) grantid: SHIONOGI INFECTIOUS DISEASE RESEARCH PROMOTION FOUNDATION – fundername: Takeda (Japan) grantid: Takeda Science Foundation – fundername: Shionogi Infectious Disease Research Promotion Foundation – fundername: Takeda Science Foundation |
GroupedDBID | --- 2XV 53G 5VS 7X7 7XC 88E 8FE 8FH 8FI 8FJ A8Z AADQD AAHBH ABDBF ABUWG ACGFO ACPRK ACUHS ADBBV AEGXH AENEX AEUYN AFKRA AFRAH AFZYC AIAGR ALIPV ALMA_UNASSIGNED_HOLDINGS AOIJS ATCPS BAWUL BBNVY BCNDV BENPR BHPHI BPHCQ BVXVI CCPQU DIK E3Z EBD EMOBN ESX F5P FYUFA GROUPED_DOAJ GX1 HCIFZ HH5 HMCUK HYE IAO IHR ITC KQ8 LK8 M1P M48 M7P MODMG M~E OK1 PATMY PGMZT PHGZM PHGZT PIMPY PQQKQ PROAC PSQYO PYCSY RNS RPM RYH SV3 TR2 TUS UKHRP AAYXX CITATION CGR CUY CVF ECM EIF NPM PJZUB PPXIY PQGLB PMFND 3V. 7T7 7U7 7XB 8FD 8FK AZQEC C1K DWQXO FR3 GNUQQ K9. P64 PKEHL PQEST PQUKI PRINS 7X8 5PM PUEGO |
ID | FETCH-LOGICAL-c647t-a551a36d352d269fd616af712922b42f7dcd3c58c6ff8bcdb05d3b0765604b3 |
IEDL.DBID | M48 |
ISSN | 2072-6651 |
IngestDate | Wed Aug 27 01:07:55 EDT 2025 Thu Aug 21 18:32:19 EDT 2025 Fri Jul 11 15:39:09 EDT 2025 Fri Jul 25 10:24:20 EDT 2025 Tue Jun 17 22:08:45 EDT 2025 Tue Jun 10 21:04:41 EDT 2025 Mon Jul 21 05:57:59 EDT 2025 Thu Apr 24 23:11:16 EDT 2025 Tue Jul 01 02:02:02 EDT 2025 Fri Jun 27 01:04:40 EDT 2025 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 6 |
Keywords | DNA ADP-ribosylation Pierisin-1 Pieris rapae |
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-c647t-a551a36d352d269fd616af712922b42f7dcd3c58c6ff8bcdb05d3b0765604b3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23 |
ORCID | 0000-0002-6652-4654 |
OpenAccessLink | http://journals.scholarsportal.info/openUrl.xqy?doi=10.3390/toxins16060270 |
PMID | 38922164 |
PQID | 3072688993 |
PQPubID | 2032321 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_9b4c56c50807403d88844b750556d4bb pubmedcentral_primary_oai_pubmedcentral_nih_gov_11209040 proquest_miscellaneous_3072296240 proquest_journals_3072688993 gale_infotracmisc_A799653011 gale_infotracacademiconefile_A799653011 pubmed_primary_38922164 crossref_citationtrail_10_3390_toxins16060270 crossref_primary_10_3390_toxins16060270 nii_cinii_1871147691550400256 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 20240614 |
PublicationDateYYYYMMDD | 2024-06-14 |
PublicationDate_xml | – month: 6 year: 2024 text: 20240614 day: 14 |
PublicationDecade | 2020 |
PublicationPlace | Switzerland |
PublicationPlace_xml | – name: Switzerland – name: Basel |
PublicationTitle | Toxins |
PublicationTitleAlternate | Toxins (Basel) |
PublicationYear | 2024 |
Publisher | MDPI AG MDPI |
Publisher_xml | – name: MDPI AG – name: MDPI |
References | Parikh (ref_11) 2004; 43 Heidelberger (ref_30) 1973; 33 Schirmer (ref_7) 2002; 277 Hirst (ref_13) 2004; 21 ref_56 Cupples (ref_33) 1990; 125 Steller (ref_64) 1995; 267 Vandekerckhove (ref_23) 1988; 263 Yu (ref_31) 2002; 297 Matsumoto (ref_49) 2007; 83 Yoshida (ref_82) 2018; 293 Watanabe (ref_16) 2001; 98 Sugimura (ref_38) 2002; 296 Kono (ref_48) 1997; 73 Kanazawa (ref_40) 2002; 78 Lord (ref_46) 2003; 22 Thanabalu (ref_5) 1991; 173 ref_69 Weigt (ref_22) 1989; 246 Aktories (ref_19) 1988; 156 ref_67 Haggerty (ref_34) 1990; 242 Kanazawa (ref_17) 2001; 98 Siegall (ref_42) 1989; 264 Honjo (ref_9) 1968; 243 Grishin (ref_66) 2016; 5 Kortright (ref_88) 2019; 25 Rusconi (ref_62) 2000; 7 Ling (ref_26) 1998; 37 Watanabe (ref_15) 1999; 96 Schuller (ref_77) 2023; 83 Niu (ref_70) 2024; 31 Subbarayan (ref_54) 2016; 87 Srinivasan (ref_65) 2020; 112 Tsuzuki (ref_14) 1990; 58 Carpusca (ref_4) 2006; 62 Koyama (ref_2) 1996; 87 Fraser (ref_27) 2004; 279 Watanabe (ref_3) 1998; 89 ref_72 Jones (ref_35) 1990; 56 Adelberg (ref_29) 1965; 18 Kono (ref_39) 1999; 137 Smith (ref_89) 1926; 9 Thanabalu (ref_8) 1993; 175 ref_79 Watanabe (ref_52) 2004; 323 Tatsuta (ref_32) 1990; 50 Yamamoto (ref_58) 2011; 139 Kanazawa (ref_28) 2002; 296 Scott (ref_71) 2013; 59 ref_73 Lee (ref_63) 2021; 43 Pan (ref_60) 2021; 43 Watanabe (ref_37) 2004; 135 Mauss (ref_21) 1990; 194 Watanabe (ref_25) 2003; 278 Watanabe (ref_57) 2004; 139 Nakano (ref_75) 2013; 63 ref_83 Krueger (ref_84) 1995; 8 Kessel (ref_10) 1980; 287 ref_81 ref_80 Allen (ref_86) 2004; 303 Debinski (ref_45) 1995; 270 Weldon (ref_44) 2011; 278 Barth (ref_24) 1998; 273 Nakano (ref_74) 2006; 103 Okazaki (ref_85) 1999; 19 ref_47 Schirmer (ref_6) 2002; 68 Aktories (ref_20) 1986; 322 Totsuka (ref_36) 2003; 16 Matsumoto (ref_50) 2008; 105 Schuller (ref_76) 2021; 596 Yamamoto (ref_53) 2009; 154 ref_87 Oda (ref_18) 2017; 292 Terenius (ref_68) 2011; 57 Krska (ref_78) 2015; 290 Chaudhary (ref_43) 1990; 87 Watanabe (ref_51) 2000; 267 Tettamanti (ref_61) 2007; 3 Sarathbabu (ref_55) 2018; 19 Truman (ref_59) 2019; 29 Otsuki (ref_90) 2017; 114 Ochiai (ref_1) 1985; 76 Avila (ref_12) 2016; 207 Shiga (ref_41) 2006; 31 |
References_xml | – volume: 87 start-page: 16 year: 2016 ident: ref_54 article-title: Characterization and Cytotoxic Activity of Apoptosis-Inducing Pierisin-5 Protein from White Cabbage Butterfly publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2016.01.072 – volume: 68 start-page: 4894 year: 2002 ident: ref_6 article-title: Inactivation of the Elongation Factor Tu by Mosquitocidal Toxin-Catalyzed Mono-ADP-Ribosylation publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.68.10.4894-4899.2002 – volume: 29 start-page: R1252 year: 2019 ident: ref_59 article-title: The Evolution of Insect Metamorphosis publication-title: Curr. Biol. doi: 10.1016/j.cub.2019.10.009 – volume: 3 start-page: 630 year: 2007 ident: ref_61 article-title: Erratum: Lepidopteran Larval Midgut during Prepupal Instar: Digestion or Self-Digestion? publication-title: Autophagy doi: 10.4161/auto.4908 – volume: 105 start-page: 2516 year: 2008 ident: ref_50 article-title: Distribution of Cytotoxic and DNA ADP-Ribosylating Activity in Crude Extracts from Butterflies among the Family Pieridae publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0712221105 – volume: 278 start-page: 4683 year: 2011 ident: ref_44 article-title: A Guide to Taming a Toxin—Recombinant Immunotoxins Constructed from Pseudomonas Exotoxin A for the Treatment of Cancer publication-title: FEBS J. doi: 10.1111/j.1742-4658.2011.08182.x – ident: ref_56 doi: 10.1098/rstb.2019.0065 – volume: 22 start-page: 53 year: 2003 ident: ref_46 article-title: Ricin: Mechanisms of Cytotoxicity publication-title: Toxicol. Rev. doi: 10.2165/00139709-200322010-00006 – volume: 43 start-page: 11 year: 2021 ident: ref_60 article-title: Control of the Insect Metamorphic Transition by Ecdysteroid Production and Secretion publication-title: Curr. Opin. Insect Sci. doi: 10.1016/j.cois.2020.09.004 – volume: 297 start-page: 5579 year: 2002 ident: ref_31 article-title: Mediation of Poly(ADP-Ribose) Polymerase-1—Dependent Cell Death by Apoptosis-Inducing Factor publication-title: Science doi: 10.1126/science.1072221 – volume: 114 start-page: 6740 year: 2017 ident: ref_90 article-title: Bioengineered Silkworms with Butterfly Cytotoxinmodified Silk Glands Produce Sericin Cocoons with a Utility for a New Biomaterial publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1703449114 – volume: 173 start-page: 2776 year: 1991 ident: ref_5 article-title: Cloning, Sequencing, and Expression of a Gene Encoding a 100-Kilodalton Mosquitocidal Toxin from Bacillus sphaericus SSII-1 publication-title: J. Bacteriol. doi: 10.1128/jb.173.9.2776-2785.1991 – volume: 98 start-page: 2226 year: 2001 ident: ref_17 article-title: Distinct Roles for the N- and C-Terminal Regions in the Cytotoxicity of Pierisin-1, a Putative ADP-Ribosylating Toxin from Cabbage Butterfly, against Mammalian Cells publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.051628898 – volume: 278 start-page: 9972 year: 2003 ident: ref_25 article-title: Identification of Glycosphingolipid Receptors for Pierisin-1, a Guanine-Specific ADP-Ribosylating Toxin from the Cabbage Butterfly publication-title: J. Biol. Chem. doi: 10.1074/jbc.M212114200 – volume: 83 start-page: 175 year: 2007 ident: ref_49 article-title: Persistence of Pierisin-1 Activities in the Adult Cabbage White Butterfly, Pieris rapae, during Storage after Killing publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. doi: 10.2183/pjab.83.175 – volume: 98 start-page: 12414 year: 2001 ident: ref_16 article-title: Mono(ADP-Ribosyl)Ation of 2’-Deoxyguanosine Residue in DNA by an Apoptosis-Inducing Protein Pierisin-1 from Cabbage Butterfly publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.221444598 – volume: 290 start-page: 1639 year: 2015 ident: ref_78 article-title: C3larvin Toxin, an ADP-Ribosyltransferase from Paenibacillus larvae publication-title: J. Biol. Chem. doi: 10.1074/jbc.M114.589846 – volume: 596 start-page: 597 year: 2021 ident: ref_76 article-title: Molecular Basis for DarT ADP-Ribosylation of a DNA Base publication-title: Nature doi: 10.1038/s41586-021-03825-4 – volume: 263 start-page: 696 year: 1988 ident: ref_23 article-title: Botulinum C2 Toxin ADP-Ribosylates Cytoplasmic β/γ-Actin in Arginine 177 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)35408-0 – volume: 139 start-page: 1251 year: 2011 ident: ref_58 article-title: Nucleotide Sequence and Chromosomal Localization of the Gene for Pierisin-1, a DNA ADP-Ribosylating Protein, in the Cabbage Butterfly Pieris rapae publication-title: Genetica doi: 10.1007/s10709-011-9626-5 – volume: 73 start-page: 192 year: 1997 ident: ref_48 article-title: Anti-Cancer Substance in Pieris brassicae publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. doi: 10.2183/pjab.73.192 – ident: ref_79 doi: 10.3390/toxins13020151 – volume: 137 start-page: 75 year: 1999 ident: ref_39 article-title: Cytotoxic Activity of Pierisin, from the Cabbage Butterfly, Pieris rapae, in Various Human Cancer Cell Lines publication-title: Cancer Lett. doi: 10.1016/S0304-3835(98)00346-2 – volume: 264 start-page: 14256 year: 1989 ident: ref_42 article-title: Functional Analysis of Domains II, Ib, and III of Pseudomonas Exotoxin publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)71671-2 – volume: 303 start-page: 1818 year: 2004 ident: ref_86 article-title: Drug Delivery Systems: Entering the Mainstream publication-title: Science doi: 10.1126/science.1095833 – volume: 25 start-page: 219 year: 2019 ident: ref_88 article-title: Phage Therapy: A Renewed Approach to Combat Antibiotic-Resistant Bacteria publication-title: Cell Host Microbe doi: 10.1016/j.chom.2019.01.014 – volume: 194 start-page: 237 year: 1990 ident: ref_21 article-title: ADP-ribosylation of Actin Isoforms by Clostridium botulinum C2 Toxin and Clostridium Perfringens Iota Toxin publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1990.tb19448.x – volume: 287 start-page: 250 year: 1980 ident: ref_10 article-title: Archaebacterial Elongation Factor Is ADP-Ribosylated by Diphtheria Toxin publication-title: Nature doi: 10.1038/287250a0 – volume: 18 start-page: 788 year: 1965 ident: ref_29 article-title: Optimal Conditions for Mutagenesis by N-Methyl-N’-Nitro-N-Nitrosoguanidine in Escherichia coli K12 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(65)90855-7 – volume: 31 start-page: 2 year: 2024 ident: ref_70 article-title: RNA Interference in Insects: The Link between Antiviral Defense and Pest Control publication-title: Insect Sci. doi: 10.1111/1744-7917.13208 – volume: 246 start-page: 181 year: 1989 ident: ref_22 article-title: Nonmuscle Actin ADP-Ribosylated by Botulinum C2 Toxin Caps Actin Filaments publication-title: FEBS Lett. doi: 10.1016/0014-5793(89)80279-0 – volume: 83 start-page: 2303 year: 2023 ident: ref_77 article-title: Molecular basis for the reversible ADP-ribosylation of guanosine bases publication-title: Mol. Cell doi: 10.1016/j.molcel.2023.06.013 – volume: 19 start-page: 485 year: 1999 ident: ref_85 article-title: Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases publication-title: Annu. Rev. Nutr. doi: 10.1146/annurev.nutr.19.1.485 – volume: 270 start-page: 16775 year: 1995 ident: ref_45 article-title: A Novel Chimeric Protein Composed of Interleukin 13 and Pseudomonas Exotoxin Is Highly Cytotoxic to Human Carcinoma Cells Expressing Receptors for Interleukin 13 and Interleukin 4 publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.28.16775 – volume: 43 start-page: 39 year: 2021 ident: ref_63 article-title: Programmed Cell Death Reshapes the Central Nervous System during Metamorphosis in Insects publication-title: Curr. Opin. Insect Sci. doi: 10.1016/j.cois.2020.09.015 – ident: ref_83 doi: 10.3390/toxins13010040 – volume: 5 start-page: 2631 year: 2016 ident: ref_66 article-title: Complete Genome of Pieris rapae, a Resilient Alien, a Cabbage Pest, and a Source of Anti-Cancer Proteins publication-title: F1000Research doi: 10.12688/f1000research.9765.1 – ident: ref_80 doi: 10.1042/BSR20193405 – volume: 293 start-page: 13768 year: 2018 ident: ref_82 article-title: Substrate N2 Atom Recognition Mechanism in Pierisin Family DNA-Targeting, Guanine-Specific ADP-Ribosyltransferase ScARP publication-title: J. Biol. Chem. doi: 10.1074/jbc.AC118.004412 – volume: 8 start-page: 34 year: 1995 ident: ref_84 article-title: The family of bacterial ADP-ribosylating exotoxins publication-title: Clin. Microbiol. Rev. doi: 10.1128/CMR.8.1.34 – volume: 273 start-page: 29506 year: 1998 ident: ref_24 article-title: Characterization of the Catalytic Site of the ADP-Ribosyltransferase Clostridium botulinum C2 Toxin by Site-Directed Mutagenesis publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.45.29506 – volume: 296 start-page: 20 year: 2002 ident: ref_28 article-title: Bcl-2 Blocks Apoptosis Caused by Pierisin-1, a Guanine-Specific ADP-Ribosylating Toxin from the Cabbage Butterfly publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(02)00815-X – ident: ref_47 doi: 10.3390/toxins15050304 – volume: 59 start-page: 1212 year: 2013 ident: ref_71 article-title: Towards the Elements of Successful Insect RNAi publication-title: J. Insect Physiol. doi: 10.1016/j.jinsphys.2013.08.014 – ident: ref_69 doi: 10.3390/biology13030137 – volume: 103 start-page: 13652 year: 2006 ident: ref_74 article-title: Purification and Molecular Cloning of a DNA ADP-Ribosylating Protein, CARP-1, from the Edible Clam Meretrix lamarckii publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0606140103 – volume: 16 start-page: 945 year: 2003 ident: ref_36 article-title: Analysis of HPRT and SupF Mutations Caused by Pierisin-1, a Guanine Specific ADP-Ribosylating Toxin Derived from the Cabbage Butterfly publication-title: Chem. Res. Toxicol. doi: 10.1021/tx034052o – volume: 323 start-page: 579 year: 2004 ident: ref_52 article-title: Mono(ADP-Ribosyl)Ation of the N 2 Amino Groups of Guanine Residues in DNA by Pierisin-2, from the Cabbage Butterfly, Pieris brassicae publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2004.08.132 – volume: 175 start-page: 2314 year: 1993 ident: ref_8 article-title: Cytotoxicity and ADP-Ribosylating Activity of the Mosquitocidal Toxin from Bacillus sphaericus SSII-1: Possible Roles of the 27- and 70-Kilodalton Peptides publication-title: J. Bacteriol. doi: 10.1128/jb.175.8.2314-2320.1993 – volume: 87 start-page: 308 year: 1990 ident: ref_43 article-title: Pseudomonas Exotoxin Contains a Specific Sequence at the Carboxyl Terminus That Is Required for Cytotoxicity publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.87.1.308 – volume: 37 start-page: 1777 year: 1998 ident: ref_26 article-title: Structure of the Shiga-like Toxin I B-Pentamer Complexed with an Analogue of Its Receptor Gb3 publication-title: Biochemistry doi: 10.1021/bi971806n – volume: 279 start-page: 27511 year: 2004 ident: ref_27 article-title: Structure of shiga toxin type 2 (Stx2) from Escherichia coli O157:H7 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M401939200 – volume: 296 start-page: 1037 year: 2002 ident: ref_38 article-title: Serendipitous Discoveries from Sudden Inspirations and the Joy of Being a Scientist publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(02)02011-9 – volume: 50 start-page: 4931 year: 1990 ident: ref_32 article-title: Inhibition by γ-Amino-n-Butyric Acid and Baclofen of Gastric Carcinogenesis Induced by N’-Methyl-N’-Nitro-N’-Nitrosoguanidine in Wistar Rats publication-title: Cancer Res. – volume: 63 start-page: 55 year: 2013 ident: ref_75 article-title: ADP-Ribosylation of Guanosine by SCO5461 Protein Secreted from Streptomyces coelicolor publication-title: Toxicon doi: 10.1016/j.toxicon.2012.11.019 – volume: 87 start-page: 1259 year: 1996 ident: ref_2 article-title: Presence in Pieris rapae of Cytotoxic Activity against Human Carcinoma Cells publication-title: Jpn. J. Cancer Res. doi: 10.1111/j.1349-7006.1996.tb03141.x – volume: 19 start-page: 337 year: 2018 ident: ref_55 article-title: Induction of Apoptosis by Pierisin-6 in HPV Positive HeLa and HepG2 Cancer Cells Is Mediated by the Caspase-3 Dependent Mitochondrial Pathway publication-title: Anticancer. Agents Med. Chem. doi: 10.2174/1871520619666181127113848 – volume: 139 start-page: 125 year: 2004 ident: ref_57 article-title: Developmental Stage-Specific Expression and Tissue Distribution of Pierisin-1, a Guanine-Specific ADP-Ribosylating Toxin, in Pieris rapae publication-title: Comp. Biochem. Physiol. A Mol. Integr. Physiol. doi: 10.1016/j.cbpb.2004.07.010 – volume: 243 start-page: 3553 year: 1968 ident: ref_9 article-title: Diphtheria Toxin-Dependent Adenosine Diphosphate Ribosylation of Aminoacyl Transferase II and Inhibition of Protein Synthesis publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)93347-8 – volume: 62 start-page: 621 year: 2006 ident: ref_4 article-title: Bacillus sphaericus Mosquitocidal Toxin (MTX) and Pierisin: The Enigmatic Offspring from the Family of ADP-Ribosyltransferases publication-title: Mol. Microbiol. doi: 10.1111/j.1365-2958.2006.05401.x – ident: ref_73 doi: 10.1007/82_2014_416 – volume: 57 start-page: 231 year: 2011 ident: ref_68 article-title: RNA Interference in Lepidoptera: An Overview of Successful and Unsuccessful Studies and Implications for Experimental Design publication-title: J. Insect Physiol. doi: 10.1016/j.jinsphys.2010.11.006 – ident: ref_81 doi: 10.1042/BSR20203727 – volume: 58 start-page: 3173 year: 1990 ident: ref_14 article-title: Cloning and Complete Nucleotide Sequence of the Gene for the Main Component of Hemagglutinin Produced by Clostridium botulinum Type C publication-title: Infect. Immun. doi: 10.1128/iai.58.10.3173-3177.1990 – volume: 96 start-page: 10608 year: 1999 ident: ref_15 article-title: Molecular Cloning of an Apoptosis-Inducing Protein, Pierisin, from Cabbage Butterfly: Possible Involvement of ADP-Ribosylation in Its Activity publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.96.19.10608 – volume: 322 start-page: 390 year: 1986 ident: ref_20 article-title: Botulinum C2 Toxin ADP-Ribosylates Actin publication-title: Nature doi: 10.1038/322390a0 – volume: 56 start-page: 3772 year: 1990 ident: ref_35 article-title: Adhesion of Macroconidia to the Plant Surface and Virulence of Nectria haematococca publication-title: Appl. Environ. Microbiol. doi: 10.1128/aem.56.12.3772-3778.1990 – volume: 76 start-page: 1064 year: 1985 ident: ref_1 article-title: Growth-Promoting Effect of Gastrin on Human Gastric Carcinoma Cell Line Tmk-1 publication-title: Jpn. J. Cancer Res. – volume: 33 start-page: 3239 year: 1973 ident: ref_30 article-title: Quantitative and Qualitative Studies of Chemical Transformation of Cloned C3H Mouse Embryo Cells Sensitive to Postconfluence Inhibition of Cell Division publication-title: Cancer Res. – volume: 78 start-page: 305 year: 2002 ident: ref_40 article-title: Pierisin-1 from Cabbage Butterfly Suppresses HeLa Tumor Growth in Nude Mice publication-title: Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. doi: 10.2183/pjab.78.305 – volume: 267 start-page: 5742 year: 2000 ident: ref_51 article-title: Purification and Cloning of Pierisin-2, an Apoptosis-Inducing Protein from the Cabbage Butterfly, Pieris brassicae publication-title: Fed. Eur. Biochem. Soc. J. doi: 10.1046/j.1432-1327.2000.01640.x – volume: 135 start-page: 471 year: 2004 ident: ref_37 article-title: Enzymatic Properties of Pierisin-1 and Its N-Terminal Domain, a Guanine-Specific ADP-Ribosyltransferase from the Cabbage Butterfly publication-title: J. Biochem. doi: 10.1093/jb/mvh062 – volume: 31 start-page: 123 year: 2006 ident: ref_41 article-title: Acute Toxicity of Pierisin-1, a Cytotoxic Protein from Pieris rapae, in Mouse and Rat publication-title: J. Toxicol. Sci. doi: 10.2131/jts.31.123 – volume: 292 start-page: 15445 year: 2017 ident: ref_18 article-title: Structural Basis of Autoinhibition and Activation of the DNA-Targeting ADP-Ribosyltransferase Pierisin-1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M117.776641 – ident: ref_67 doi: 10.3389/fmolb.2022.944774 – volume: 125 start-page: 275 year: 1990 ident: ref_33 article-title: A Set of LacZ Mutations in Escherichia coli That Allow Rapid Detection of Specific Frameshift Mutations publication-title: Genetics doi: 10.1093/genetics/125.2.275 – volume: 7 start-page: 1063 year: 2000 ident: ref_62 article-title: Programmed Cell Death and Patterning in Drosophila publication-title: Cell Death Differ. doi: 10.1038/sj.cdd.4400767 – volume: 112 start-page: 1464 year: 2020 ident: ref_65 article-title: Mapping and Identification of Potential Target Genes from Short–RNA Seq for the Control of Pieris rapae Larvae publication-title: Genomics doi: 10.1016/j.ygeno.2019.08.017 – volume: 207 start-page: 68 year: 2016 ident: ref_12 article-title: An Entamoeba Histolytica ADP-Ribosyl Transferase from the Diphtheria Toxin Family Modifies the Bacterial Elongation Factor Tu publication-title: Mol. Biochem. Parasitol. doi: 10.1016/j.molbiopara.2016.05.012 – volume: 156 start-page: 361 year: 1988 ident: ref_19 article-title: Different Types of ADP-Ribose Protein Bonds Formed by Botulinum C2 Toxin, Botulinum ADP-Ribosyltransferase C3 and Pertussis Toxin publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(88)80849-0 – volume: 242 start-page: 67 year: 1990 ident: ref_34 article-title: Characterization of the Effects of Direct Alkylators on In Vitro Immune Responses publication-title: Mutat. Res./Genet. Toxicol. doi: 10.1016/0165-1218(90)90100-G – volume: 154 start-page: 326 year: 2009 ident: ref_53 article-title: Molecular Cloning of Apoptosis-Inducing Pierisin-like Proteins, from Two Species of White Butterfly, Pieris melete and Aporia crataegi publication-title: Comp. Biochem. Physiol.-B Biochem. Mol. Biol. doi: 10.1016/j.cbpb.2009.07.007 – volume: 43 start-page: 1204 year: 2004 ident: ref_11 article-title: Transition State Structure for ADP-Ribosylation of Eukaryotic Elongation Factor 2 Catalyzed by Diphtheria Toxin publication-title: Biochemistry doi: 10.1021/bi035907z – volume: 267 start-page: 1445 year: 1995 ident: ref_64 article-title: Mechanisms and Genes of Cellular Suicide publication-title: Science doi: 10.1126/science.7878463 – volume: 9 start-page: 10 year: 1926 ident: ref_89 article-title: The Bacteriophage and Its Behavior publication-title: Sci. News-Lett. doi: 10.2307/3901826 – ident: ref_72 doi: 10.1371/journal.pone.0060539 – ident: ref_87 doi: 10.3389/fmicb.2019.03045 – volume: 89 start-page: 556 year: 1998 ident: ref_3 article-title: Purification of Pierisin, an Inducer of Apoptosis in Human Gastric Carcinoma Cells, from Cabbage Butterfly, Pieris rapae publication-title: Jpn. J. Cancer Res. doi: 10.1111/j.1349-7006.1998.tb03297.x – volume: 277 start-page: 11941 year: 2002 ident: ref_7 article-title: The ADP-Ribosylating Mosquitocidal Toxin from Bacillus sphaericus publication-title: J. Biol. Chem. doi: 10.1074/jbc.M108463200 – volume: 21 start-page: 77 year: 2004 ident: ref_13 article-title: Cholera Toxin: A Paradigm for Multi-Functional Engagement of Cellular Mechanisms (Review) publication-title: Mol. Membr. Biol. doi: 10.1080/09687680410001663267 |
SSID | ssib045316353 ssj0000331917 ssib045315935 ssib045316346 |
Score | 2.356209 |
SecondaryResourceType | review_article |
Snippet | Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer... Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly against cancer cell lines.... Pierisin-1 was serendipitously discovered as a strong cytotoxic and apoptosis-inducing protein from pupae of the cabbage butterfly Pieris rapae against cancer... |
SourceID | doaj pubmedcentral proquest gale pubmed crossref nii |
SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 270 |
SubjectTerms | Adenosine diphosphate ADP Ribose Transferases - genetics ADP Ribose Transferases - metabolism Amino acids Animals Antineoplastic Agents - pharmacology Antitumor activity Apoptosis Apoptosis - drug effects Biotechnology Botulinum toxin Butterflies Butterflies & moths Cancer Causes of Cell surface Cells Cloning Cytotoxicity Deoxyribonucleic acid DNA DNA ADP-ribosylation DNA damage Glycosphingolipids Health aspects Hormones Humans Insect Proteins - chemistry Insect Proteins - metabolism Medical research Medicine Metamorphosis Microorganisms Molecular biology Mutation Physiological aspects Pieris rapae Pierisin-1 Proteins R Radioactivity Review Therapeutic applications Toxins Tumor cell lines |
SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1di9QwFA26T76Iun5UdyWC6Itlp0mazDzWWZdFcBn8gH0QSpM0WFjTwemC8-89t-0OU1F8EYZ5aDJtmntz7znDzQljL40KsjK1T9Fep8oakVb5IqTBeZjbeJFJ2u_84UKff1HvL_PLvaO-qCZskAceJu5kYZXLtQOOQLKbSQ_GpnDLnERgvLKWoi9y3h6Z6mOwlEREBpVGCV5_0rU_m7jJgNdBxGaTLNSL9e9C8u3YNH-Cm79XTe6lobN77O6IH3kxjPs-u1XHB-ywiODO37f8Fe8rOvu_yg_Z11VDQsxNfMOX266lsTleRc-Ldbvu2k2zSenkDofsxU8vCl6crtKPjW03WyqQw8UViTg0keOzrKxF6OHjwdZX24fs09m7z8vzdDxNIXVamQ4myLNKag_E5YVeBK8zXQWDfC-EVSIY77x0-dzpEObWeTvLvbQzQ-o8yspH7CC2sX7CuAh1jlU8N14vQF5CJYHaHHiLARUyIUtYejO3pRuFxum8i6sShINsUU5tkbDXu_7rQWLjrz3fkql2vUgau78AhylHhyn_5TB4HBm6pAWMYblq3IeAlyMprLIwoIA5xb2EHU16YuG5SfMxXAWvSN8ZiGemjCa5fYqLQJL4-Y0TlWNg2JQIqULPQXJlwl7smunOVOwW6_Z66CMWGlgrYY8Hn9u9MvClEKC4CZtPvHEyJ9OW2HzrZcMz2iaNsT39H7P4jN0RgHdUNJepI3bQ_biujwHPOvu8X4m_ANGnM48 priority: 102 providerName: Directory of Open Access Journals – databaseName: ProQuest Health & Medical Collection dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3fb9MwELbYeOEFAeNHYENGQvCCtcZ27OQJhY5pQmKq-CH1ASmK7XhEGk5ZMon-99wlaSAIkKo-xG5r587n73Mv3xHyXEsvSl05Bu0Vk0ZzViaZZ946MLd2PBb4vPP7c3X2Wb5bJ-vxwK0d0yp3MbEP1K6xeEZ-DL7IVQrsQLzefGdYNQr_XR1LaOyRmyhdhildeq2nM5aFEEhHBq1GAez-uGt-1KGNAbUDHVvM9qJesn8KzHuhrv8GOv_MnfxtMzq9Q26PKJLmg9nvkhtVuEcO8gAM-tuWvqB9Xmd_YH5AvqxqlGOuwyu63HYNjs3SMjiab5pN17R1y7B-h4U9jJ6c5zQ_WbEPtWnaLabJwcUVSjnUgcJrWRoDAYiO5a0vt_fJx9O3n5ZnbKypwKySugNDJHEplAPc5bjKvFOxKr2GXZ9zI7nXzjphk9Qq71NjnVkkTpiFRo0eacQDsh-aUD0ilPsqgbWcaqcyoDC-FIDdLLAXDYRI-zgibHdvCzvKjWPVi8sCaAfaopjbIiIvp_6bQWjjnz3foKmmXiiQ3V9ori6Kcb0VmZE2URbgJ2CkhXBA9CV4YoLaQU4aAz-Hhi5wGcOwbDk-jQCTQ0GsItdABBOMfhE5nPWE5WdnzUfgKjBFfI-BfsZSKxTdx-gIeBI-vnOiYgwPbfHLmSPybGrGb8aUt1A110MfnilAXBF5OPjcNGVAmZwD0Y1IOvPG2T2Zt4T6ay8eHuPD0jC2x_8f1xNyiwN8w6S4WB6S_e7qujoC-NWZp_0a-wmHKyyG priority: 102 providerName: ProQuest |
Title | Pierisin, Cytotoxic and Apoptosis-Inducing DNA ADP-Ribosylating Protein in Cabbage Butterfly |
URI | https://cir.nii.ac.jp/crid/1871147691550400256 https://www.ncbi.nlm.nih.gov/pubmed/38922164 https://www.proquest.com/docview/3072688993 https://www.proquest.com/docview/3072296240 https://pubmed.ncbi.nlm.nih.gov/PMC11209040 https://doaj.org/article/9b4c56c50807403d88844b750556d4bb |
Volume | 16 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Bb9MwFLbYJqFdEDBgGVtlJAQXAo3t2O0BoazbNCGtqgaTekCKYjuGSMXp2kxa_j3vpWkhqFyQqh5iu7X93rO_L3r-TMhrJRzPVG5DKM9DoRULs3joQmcsmFtZFnE873w1lpc34vM0nv7Of2oncLmV2uF9UjeL2fv72_oTBPxHZJxA2T9U5X3hlxFAceBYQN_3YFdSGKRXLdRvVmXOkZqsdBu3NNsnD2HvZiySorNFNUr-m_V6xxfFNiz6d0rlH3vUxWPyqAWXNFl5wxPyIPdPyUHigVj_rOkb2qR7Nu_RD8i3SYEqzYV_R0d1VWI3Dc28pcm8nFflsliGeK2Hga2Nno0TmpxNwutCl8sas-fg4QQVHgpP4TPKtIZ1iba3Xs_qZ-TLxfnX0WXYXrUQGilUBfaJo4xLC3DMMjl0VkYycwrAAGNaMKessdzEAyOdG2hjdT-2XPcVSvcIzZ-TXV_6_JBQ5vIYQnygrBwCs3EZB0hngNQo4EnKRQEJ13ObmlaFHC_DmKXARtAsadcsAXm7qT9f6W_8s-YpmmpTC3Wzmwfl4nvahmE61MLE0gAqBejU5xb4vwAHjVFSyAqt4e_Q0Cn6G3TLZO0hBRgc6mSliQJ-GOOiGJDjTk2IStMpPgFXgSHidwSsNBJKohY_LpoAM6H52onStdOnsN4yOQAGzAPyalOMv4yZcD4v71Z12FACEAvIi5XPbYa8duCADDre2JmTbokvfjSa4hGeoYa-Hf1_05dknwHiwzy6SByT3Wpxl58AYqt0j-yoqeqRvdPz8eS617z36DXh-QudbUDv |
linkProvider | Scholars Portal |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwELba7QEuCCiPQAtG4nEh6sZ27OwBoXS31Za2q1UpUg8VUWwnEKkkS5MK9j_xI5lJsoEg4FYp2kPsJLZnPP4-73iGkOdKpDxWiXWhPHGFVsyN_VHqpsaCuJVlHsfzzsczOf0g3p35Z2vkx-osDLpVrmxibahtYXCPfAd0kckA2AF_u_jqYtYo_Hd1lUKjUYvDZPkNKFv55mAC8n3B2P7e6XjqtlkFXCOFqqApvhdzaQF5WCZHqZWejFMF6x5jWrBUWWO58QMj0zTQxuqhb7kGug_YQGgOb10nG4IDkRmQjd292fyk29MZco70p4kNyflouFMV37O89IAlAP0b9ta-OkVAtxCs51n2N5D7p6_mb4vf_m1yq0WtNGzU7A5ZS_K7ZDPMgbF_WdKXtPYjrTfoN8n5PMPwz1n-mo6XVYFtMzTOLQ0XxaIqyqx0MV-IgTWTTmYhDSdz9yTTRblEtzy4OcfQEVlO4RrHWoPBo2067YvlPfL-Gkb7PhnkRZ48JJSliQ-2I1BWjoAypTEHrGiALSkgYCr1HOKuxjYybXhzzLJxEQHNQVlEfVk45FVXf9EE9vhnzV0UVVcLA3LXN4rLT1E7v6ORFsaXBuAuYLIht0EQCNB8H2MVWaE1fA4FHaHZgGaZuD39AJ3DAFxRqIB4-mhtHbLVqwnT3fSKt0FVoIv46wHd9YSSGOQfrTHgV3h8pURRa47K6NfkccizrhjfjC52eVJcNXXYSALCc8iDRue6LgOqZQyItUOCnjb2xqRfkmef62DlHh7OhrY9-n-7npIb09Pjo-joYHb4mNxkAB3RIc8TW2RQXV4l2wD9Kv2knXGUfLzeKf4TIrRpsQ |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1bb9MwFLa2ISFeEDAuGRsYicsLURs7sZMHhEJLtTGoKi5SHxBRbMcQaUvKkgn6z_h5nJOkgSDgbVLVh9hN7JyLv889PoeQh9K3PJWZcaE9c30lmZsGkXWtNiBuaZjH8bzzm7k4_OC_WgbLLfJjcxYGwyo3PrFx1KbUuEc-Al1kIgR2wEe2C4tYTGfPV19drCCF_7Ruymm0KnKcrb8BfaueHU1B1o8Ym718Pzl0uwoDrha-rGFYgZdyYQCFGCYia4QnUithDWRM-cxKow3XQaiFtaHSRo0DwxVQf8AJvuJw121ySfLAQwuTS9nv7ow5RyLUZonkPBqP6vJ7XlQe8AUgguPBKtgUC-iXhO0iz_8Gd_-M2vxtGZxdI1c7_ErjVuGuk62suEF24wK4--maPqZNRGmzVb9LPi5yTASdF0_pZF2XODZN08LQeFWu6rLKKxcrh2hYPel0HtN4unDf5qqs1higBxcXmEQiLyh8JqlS4PpoV1j7ZH2TvLuAd32L7BRlkd0hlNksAC8SSiMiIE825YAaNfAmCVRMWs8h7ubdJrpLdI71Nk4SIDwoi2QoC4c86fuv2hQf_-z5AkXV98LU3M2F8uxz0ll6EilfB0ID8AV0NuYmDEMfbCDArEXGVwoeh4JO0IHAsHTanYOAyWEqriSWQEED9LsO2R_0BMPXg-YDUBWYIn57QHw9XwpM949-GZAs_HyjREnnmKrklxk55EHfjHfGYLsiK8_bPiwSgPUccrvVuX7KgG8ZA4rtkHCgjYN3Mmwp8i9N2nIPj2nD2Pb-P6775DIYdvL6aH58l1xhgCExMs_z98lOfXaeHQAGrNW9xtwo-XSx1v0TATtsgQ |
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=Pierisin%2C+Cytotoxic+and+Apoptosis-Inducing+DNA+ADP-Ribosylating+Protein+in+Cabbage+Butterfly&rft.jtitle=Toxins&rft.au=Takahashi-Nakaguchi%2C+Azusa&rft.au=Horiuchi%2C+Yu&rft.au=Yamamoto%2C+Masafumi&rft.au=Totsuka%2C+Yukari&rft.date=2024-06-14&rft.pub=MDPI&rft.eissn=2072-6651&rft.volume=16&rft.issue=6&rft_id=info:doi/10.3390%2Ftoxins16060270&rft_id=info%3Apmid%2F38922164&rft.externalDocID=PMC11209040 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2072-6651&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2072-6651&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2072-6651&client=summon |