MARC details
000 -LEADER |
fixed length control field |
02279nam a22002897a 4500 |
003 - CONTROL NUMBER IDENTIFIER |
control field |
ZW-GwMSU |
005 - DATE AND TIME OF LATEST TRANSACTION |
control field |
20250319072718.0 |
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
fixed length control field |
250319b |||||||| |||| 00| 0 eng d |
022 ## - INTERNATIONAL STANDARD SERIAL NUMBER |
International Standard Serial Number |
0176-1617 |
040 ## - CATALOGING SOURCE |
Original cataloging agency |
MSU |
Language of cataloging |
English |
Transcribing agency |
MSU |
Description conventions |
rda |
050 00 - LIBRARY OF CONGRESS CALL NUMBER |
Classification number |
QK711..2 JOU |
100 1# - MAIN ENTRY--PERSONAL NAME |
Personal name |
Bajsa, Joanna |
Relator term |
author |
245 10 - TITLE STATEMENT |
Title |
Cantharidin, a protein phosphatase inhibitor, strongly upregulates detoxification enzymes in the Arabidopsis proteome |
Statement of responsibility, etc. |
created by Joanna Bajsa, Zhiqiang Pan and Stephen O. Duke |
264 1# - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE |
Place of production, publication, distribution, manufacture |
Amsterdam: |
Name of producer, publisher, distributor, manufacturer |
Elsevier GmbH, |
336 ## - CONTENT TYPE |
Source |
rdacontent |
Content type term |
text |
Content type code |
txt |
337 ## - MEDIA TYPE |
Source |
rdamedia |
Media type term |
unmediated |
Media type code |
n |
338 ## - CARRIER TYPE |
Source |
rdacarrier |
Carrier type term |
volume |
Carrier type code |
nc |
440 ## - SERIES STATEMENT/ADDED ENTRY--TITLE |
Title |
Journal of Plant Physiology |
Volume/sequential designation |
Volume 173 |
520 3# - SUMMARY, ETC. |
Summary, etc. |
Cantharidin, a potent inhibitor of plant serine/threonine protein phosphatases (PPPs), is highly phytotoxic and dramatically affects the transcriptome in Arabidopsis. To investigate the effect of cantharidin on the Arabidopsis proteome, a combination of two-dimensional difference gel electrophoresis (2-D DIGE) and matrix-assisted laser desorption ionization time-of-flight (MALDI/TOF) mass spectrometry was employed for protein profiling. Multivariate statistical analysis identified 75 significant differential spots corresponding to 59 distinct cantharidin-responsive proteins, which were representative of different biological processes, cellular components, and molecular functions categories. The majority of identified proteins localized in the chloroplast had a significantly decreased presence, especially proteins involved in photosynthesis. Detoxification enzymes, especially glutathione-S-transferases (GSTs), were the most upregulated group (ca. 1.5- to 3.3-fold). Given that the primary role of GSTs is involved in the process of detoxification of both xenobiotic and endobiotic compounds, the induction of GSTs suggests that cantharidin promoted inhibition of PPPs may lead to defense-like responses through regulation of GST enzymes as well as other metabolic pathways. |
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
Topical term or geographic name entry element |
Cantharidin |
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
Topical term or geographic name entry element |
Glutathione-S-transferase |
650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
Topical term or geographic name entry element |
Protein phosphatase |
700 1# - ADDED ENTRY--PERSONAL NAME |
Personal name |
Pan, Zhiqiang |
Relator term |
co-author |
700 1# - ADDED ENTRY--PERSONAL NAME |
Personal name |
Duke, Stephen O. |
Relator term |
co-author |
856 ## - ELECTRONIC LOCATION AND ACCESS |
Uniform Resource Identifier |
https://doi.org/10.1016/j.jplph.2014.09.002 |
942 ## - ADDED ENTRY ELEMENTS (KOHA) |
Source of classification or shelving scheme |
Library of Congress Classification |
Koha item type |
Journal Article |