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  • 1
    Language: English
    In: eLife, 2014-04-08, Vol.3, p.e02131-e02131
    Description: Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1-BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell-division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001.
    Subject(s): Arabidopsis Proteins - metabolism ; Endocytosis ; Cell Division ; Golgi Apparatus - metabolism ; Arabidopsis Proteins - secretion ; Arabidopsis - metabolism ; Protein Transport ; Seeds ; Cytokinesis ; Guanine ; Golgi apparatus ; Proteins ; Microscopy ; Phylogenetics ; Membrane trafficking ; Physiology ; Software ; Flowers & plants ; Recycling ; Molecular biology ; Guanine nucleotide exchange factor ; Localization ; Index Medicus ; Plant Biology ; ARF-GEF ; secretion ; Arabidopsis ; cell division ; post-Golgi trafficking ; recycling ; gegulation of vesicle traffic ; Cell Biology
    ISSN: 2050-084X
    E-ISSN: 2050-084X
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 2
    Language: English
    In: PLoS genetics, 2018-11, Vol.14 (11), p.e1007795-e1007795
    Description: In eukaryotes, GTP-bound ARF GTPases promote intracellular membrane traffic by mediating the recruitment of coat proteins, which in turn sort cargo proteins into the forming membrane vesicles. Mammals employ several classes of ARF GTPases which are activated by different ARF guanine-nucleotide exchange factors (ARF-GEFs). In contrast, flowering plants only encode evolutionarily conserved ARF1 GTPases (class I) but not the other classes II and III known from mammals, as suggested by phylogenetic analysis of ARF family members across the five major clades of eukaryotes. Instead, flowering plants express plant-specific putative ARF GTPases such as ARFA and ARFB, in addition to evolutionarily conserved ARF-LIKE (ARL) proteins. Here we show that all eight ARF-GEFs of Arabidopsis interact with the same ARF1 GTPase, whereas only a subset of post-Golgi ARF-GEFs also interacts with ARFA, as assayed by immunoprecipitation. Both ARF1 and ARFA were detected at the Golgi stacks and the trans-Golgi network (TGN) by both live-imaging with the confocal microscope and nano-gold labeling followed by EM analysis. ARFB representing another plant-specific putative ARF GTPase was detected at both the plasma membrane and the TGN. The activation-impaired form (T31N) of ARF1, but neither ARFA nor ARFB, interfered with development, although ARFA-T31N interfered, like ARF1-T31N, with the GDP-GTP exchange. Mutant plants lacking both ARFA and ARFB transcripts were viable, suggesting that ARF1 is sufficient for all essential trafficking pathways under laboratory conditions. Detailed imaging of molecular markers revealed that ARF1 mediated all known trafficking pathways whereas ARFA was not essential to any major pathway. In contrast, the hydrolysis-impaired form (Q71L) of both ARF1 and ARFA, but not ARFB, had deleterious effects on development and various trafficking pathways. However, the deleterious effects of ARFA-Q71L were abolished by ARFA-T31N inhibiting cognate ARF-GEFs, both in cis (ARFA-T31N,Q71L) and in trans (ARFA-T31N + ARFA-Q71L), suggesting indirect effects of ARFA-Q71L on ARF1-mediated trafficking. The deleterious effects of ARFA-Q71L were also suppressed by strong over-expression of ARF1, which was consistent with a subset of BIG1-4 ARF-GEFs interacting with both ARF1 and ARFA. Indeed, the SEC7 domain of BIG5 activated both ARF1 and ARFA whereas the SEC7 domain of BIG3 only activated ARF1. Furthermore, ARFA-T31N impaired root growth if ARF1-specific BIG3 was knocked out and only ARF1- and ARFA-activating BIG4 was functional. Activated ARF1 recruits different coat proteins to different endomembrane compartments, depending on its activation by different ARF-GEFs. Unlike ARF GTPases, ARF-GEFs not only localize at distinct compartments but also regulate specific trafficking pathways, suggesting that ARF-GEFs might play specific roles in traffic regulation beyond the activation of ARF1 by GDP-GTP exchange.
    Subject(s): Arabidopsis Proteins - genetics ; Guanine Nucleotide Exchange Factors - genetics ; Signal Transduction ; Arabidopsis - ultrastructure ; Genome, Plant ; Phylogeny ; Guanine Nucleotide Exchange Factors - classification ; Arabidopsis - metabolism ; Protein Transport ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; Up-Regulation - drug effects ; trans-Golgi Network - metabolism ; GTP Phosphohydrolases - metabolism ; GTP Phosphohydrolases - genetics ; Guanine Nucleotide Exchange Factors - metabolism ; Models, Biological ; GTP Phosphohydrolases - classification ; Plants, Genetically Modified ; Arabidopsis Proteins - classification ; Estradiol - pharmacology ; Intracellular Membranes - metabolism ; Arabidopsis thaliana ; Physiological aspects ; Guanosine triphosphatase ; Proteins ; Traffic regulations ; G proteins ; Index Medicus ; Biology and Life Sciences ; Research and Analysis Methods ; Immunoprecipitation ; Peptides ; Cell division ; Membrane vesicles ; Guanosine triphosphatases ; Genomes ; Kinases ; Mammals ; Gene expression ; Guanine ; Golgi apparatus ; Guanosine triphosphate ; Overexpression ; Guanosine diphosphate ; Proteomics ; Flowering ; Membrane trafficking ; Molecular biology ; Guanine nucleotide exchange factor ; Endoplasmic reticulum
    ISSN: 1553-7404
    ISSN: 1553-7390
    E-ISSN: 1553-7404
    Source: Academic Search Ultimate
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 3
    Language: English
    In: The Plant cell, 2020-08, Vol.32 (8), p.2491-2507
    Description: Membrane trafficking maintains the organization of the eukaryotic cell and delivers cargo proteins to their subcellular destinations, such as sites of action or degradation. The formation of membrane vesicles requires the activation of the ADP-ribosylation factor ARF GTPase by the SEC7 domain of ARF guanine-nucleotide exchange factors (ARF-GEFs), resulting in the recruitment of coat proteins by GTP-bound ARFs. In vitro exchange assays were done with monomeric proteins, although ARF-GEFs form dimers in vivo. This feature is conserved across eukaryotes, although its biological significance is unknown. Here, we demonstrate the proximity of ARF1•GTPs in vivo by fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy, mediated through coordinated activation by dimers of Arabidopsis ( ) ARF-GEF GNOM, which is involved in polar recycling of the auxin transporter PIN-FORMED1. Mutational disruption of ARF1 spacing interfered with ARF1-dependent trafficking but not with coat protein recruitment. A mutation impairing the interaction of one of the two SEC7 domains of the GNOM ARF-GEF dimer with its ARF1 substrate reduced the efficiency of coordinated ARF1 activation. Our results suggest a model of coordinated activation-dependent membrane insertion of ARF1•GTP molecules required for coated membrane vesicle formation. Considering the evolutionary conservation of ARFs and ARF-GEFs, this initial regulatory step of membrane trafficking might well occur in eukaryotes in general.
    Subject(s): Arabidopsis Proteins - metabolism ; DNA-Binding Proteins - metabolism ; Transcription Factors - metabolism ; Phenotype ; Guanine Nucleotide Exchange Factors - metabolism ; Models, Biological ; Transport Vesicles - metabolism ; Plants, Genetically Modified ; Protein Multimerization ; Protein Binding ; Cell Membrane - metabolism ; Arabidopsis - metabolism ; Index Medicus
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 4
    Language: English
    In: Current biology, 2014, Vol.24 (12), p.1383-1389
    Description: Plasma-membrane proteins such as ligand-binding receptor kinases, ion channels, or nutrient transporters are turned over by targeting to a lytic compartment--lysosome or vacuole--for degradation. After their internalization, these proteins arrive at an early endosome, which then matures into a late endosome with intraluminal vesicles (multivesicular body, MVB) before fusing with the lysosome/vacuole in animals or yeast. The endosomal maturation step involves a SAND family protein mediating Rab5-to-Rab7 GTPase conversion. Vacuolar trafficking is much less well understood in plants. Here we analyze the role of the single-copy SAND gene of Arabidopsis. In contrast to its animal or yeast counterpart, Arabidopsis SAND protein is not required for early-to-late endosomal maturation, although its role in mediating Rab5-to-Rab7 conversion is conserved. Instead, Arabidopsis SAND protein is essential for the subsequent fusion of MVBs with the vacuole. The inability of sand mutant to mediate MVB-vacuole fusion is not caused by the continued Rab5 activity but rather reflects the failure to activate Rab7. In conclusion, regarding the endosomal passage of cargo proteins for degradation, a major difference between plants and nonplant organisms might result from the relative timing of endosomal maturation and SAND-dependent Rab GTPase conversion as a prerequisite for the fusion of late endosomes/MVBs with the lysosome/vacuole.
    Subject(s): rab GTP-Binding Proteins - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis - enzymology ; Nuclear Proteins - metabolism ; rab GTP-Binding Proteins - genetics ; Endosomes - metabolism ; Arabidopsis - metabolism ; Protein Transport ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; Lysosomes - metabolism ; Gene Expression Regulation, Plant ; Vacuoles - metabolism ; Multivesicular Bodies - metabolism ; Nuclear Proteins - genetics ; Arabidopsis thaliana ; Plant physiology ; Analysis ; Physiological aspects ; Molecular biology ; Phosphotransferases ; Membrane proteins ; Protein binding ; Index Medicus
    ISSN: 0960-9822
    E-ISSN: 1879-0445
    Source: Backfile Package - All of Back Files EBS [ALLOFBCKF]
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 5
    Language: English
    In: The Plant cell, 2020-08-03, Vol.32 (8), p.2491
    Description: Membrane trafficking maintains the organization of the eukaryotic cell and delivers cargo proteins to their subcellular destinations, such as sites of action or degradation. The formation of membrane vesicles requires the activation of the ADP-ribosylation factor ARF GTPase by the SEC7 domain of ARF guanine-nucleotide exchange factors (ARF-GEFs), resulting in the recruitment of coat proteins by GTP-bound ARFs. In vitro exchange assays were done with monomeric proteins, although ARF-GEFs form dimers in vivo. This feature is conserved across eukaryotes, although its biological significance is unknown. Here, we demonstrate the proximity of ARF1•GTPs in vivo by fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy, mediated through coordinated activation by dimers of Arabidopsis (Arabidopsis thaliana) ARF-GEF GNOM, which is involved in polar recycling of the auxin transporter PIN-FORMED1. Mutational disruption of ARF1 spacing interfered with ARF1-dependent trafficking but not with coat protein recruitment. A mutation impairing the interaction of one of the two SEC7 domains of the GNOM ARF-GEF dimer with its ARF1 substrate reduced the efficiency of coordinated ARF1 activation. Our results suggest a model of coordinated activation-dependent membrane insertion of ARF1•GTP molecules required for coated membrane vesicle formation. Considering the evolutionary conservation of ARFs and ARF-GEFs, this initial regulatory step of membrane trafficking might well occur in eukaryotes in general.
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
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  • 6
    Language: English
    In: European journal of cell biology, 2010, Vol.89 (2), p.138-144
    Description: How the apical-basal axis of polarity is established in embryogenesis is still a mystery in plant development. This axis appeared specifically compromised by mutations in the Arabidopsis GNOM gene. Surprisingly, GNOM encodes an ARF guanine-nucleotide exchange factor (ARF-GEF) that regulates the formation of vesicles in membrane trafficking. In-depth functional analysis of GNOM and its closest relative, GNOM-LIKE 1 (GNL1), has provided a mechanistic explanation for the development-specific role of a seemingly mundane trafficking regulator. The current model proposes that GNOM is specifically involved in the endosomal recycling of the auxin-efflux carrier PIN1 to the basal plasma membrane in provascular cells, which in turn is required for the accumulation of the plant hormone auxin at the future root pole through polar auxin transport. Thus, the analysis of GNOM highlights the importance of cell-biological processes for a mechanistic understanding of development.
    Subject(s): Membrane traffic ; Polarity ; Patterning ; ARF-GEF ; Arabidopsis Proteins - genetics ; Guanine Nucleotide Exchange Factors - genetics ; Arabidopsis - growth & development ; Arabidopsis - embryology ; Phylogeny ; Guanine Nucleotide Exchange Factors - classification ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; Phenotype ; Animals ; Guanine Nucleotide Exchange Factors - metabolism ; Cloning, Molecular ; Cell Membrane - metabolism ; Mutation ; Arabidopsis Proteins - classification ; Morphogenesis - physiology ; Arabidopsis thaliana ; Analysis ; Genetic aspects ; Index Medicus
    ISSN: 0171-9335
    E-ISSN: 1618-1298
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 7
    Language: English
    In: Breast cancer research and treatment, 2020-08-27, Vol.184 (2), p.311-324
    Description: PURPOSEVarious aberrations in the fibroblast growth factor receptor genes FGFR1, FGFR2, and FGFR3 are found in different cancers, including breast cancer (BC). This study analyzed the impact of FGFR amplification on the BC prognosis. METHODSThe study included 894 BC patients. The amplification rates of FGFR1, FGFR2, and FGFR3 were evaluated on tissue microarrays using fluorescence in situ hybridization (FISH). Associations between these parameters and prognosis were analyzed using multivariate Cox regression analyses. RESULTSFGFR1 FISH was assessable in 503 samples, FGFR2 FISH in 447, and FGFR3 FISH in 562. The FGFR1 amplification rate was 6.6% (n = 33). Increased FGFR2 copy numbers were seen in 0.9% (n = 4); only one patient had FGFR3 amplification (0.2%). Most patients with FGFR1 amplification had luminal B-like tumors (69.7%, n = 23); only 32.6% (n = 153) of patients without FGFR1 amplification had luminal B-like BC. Other patient and tumor characteristics appeared similar between these two groups. Observed outcome differences between BC patients with and without FGFR1 amplification did not achieve statistical significance; however, there was a trend toward poorer distant metastasis-free survival in BC patients with FGFR1 amplification (HR = 2.08; 95% CI 0.98 to 4.39, P = 0.05). CONCLUSIONFGFR1 amplification occurs most frequently in patients with luminal B-like BC. The study showed a nonsignificant correlation with the prognosis, probably due to the small sample size. Further research is therefore needed to address the role of FGFR1 amplifications in early BC patients. FGFR2 and FGFR3 amplifications are rare in patients with primary BC.
    Subject(s): Index Medicus ; Amplification ; Prognosis ; FISH ; Breast cancer ; Preclinical Study ; FGFR3 ; FGFR2 ; FGFR1
    ISSN: 0167-6806
    E-ISSN: 1573-7217
    Source: Alma/SFX Local Collection
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 8
    Language: English
    In: BMC cancer, 2017-12-14, Vol.17 (1), p.850-850
    Description: Over the last decades numerous initiatives have been set up that aim at translating the best available medical knowledge and treatment into clinical practice. The inherent complexity of the programs and discrepancies in the terminology used make it difficult to appreciate each of them distinctly and compare their specific strengths and weaknesses. To allow comparison and stimulate dialogue between different programs, we in this paper provide an overview of the German Cancer Society certification program for multidisciplinary cancer centers that was established in 2003. In the early 2000s the German Cancer Society assessed the available information on quality of cancer care in Germany and concluded that there was a definite need for a comprehensive, transparent and evidence-based system of quality assessment and control. This prompted the development and implementation of a voluntary cancer center certification program that was promoted by scientific societies, health-care providers, and patient advocacy groups and based on guidelines of the highest quality level (S3). The certification system structures the entire process of care from prevention to screening and multidisciplinary treatment of cancer and places multidisciplinary teams at the heart of this program. Within each network of providers, the quality of care is documented using tumor-specific quality indicators. The system started with breast cancer centers in 2003 and colorectal cancer centers in 2006. In 2017, certification systems are established for the majority of cancers. Here we describe the rationale behind the certification program, its history, the development of the certification requirements, the process of data collection, and the certification process as an example for the successful implementation of a voluntary but powerful system to ensure and improve quality of cancer care. Since 2003, over 1 million patients had their primary tumors treated in a certified center. There are now over 1200 sites for different tumor entities in four countries that have been certified in accordance with the program and transparently report their results from multidisciplinary treatment for a substantial proportion of cancers. This led to a fundamental change in the structure of cancer care in Germany and neighboring countries within one decade.
    Subject(s): Humans ; Patient Care Team - trends ; Quality of Health Care - organization & administration ; Cancer Care Facilities - trends ; Certification ; Interdisciplinary Communication ; Neoplasms - therapy ; Quality of Health Care - trends ; Patient Care Team - organization & administration ; Program Evaluation ; Cancer Care Facilities - organization & administration ; Societies, Medical - standards ; Germany ; Cancer Care Facilities - standards ; Practice Guidelines as Topic ; Care and treatment ; Usage ; Diagnosis ; Physical therapy ; Therapeutics, Physiological ; Cancer ; Index Medicus ; Multidisciplinarity ; Quality indicators ; Quality of care ; Debate
    ISSN: 1471-2407
    E-ISSN: 1471-2407
    Source: BioMedCentral Open Access
    Source: Academic Search Ultimate
    Source: PubMed Central
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 9
    Language: English
    In: Brain stimulation, 2020-05, Vol.13 (3), p.696-704
    Description: Electroconvulsive therapy (ECT) is the most effective treatment option for major depressive disorder, so understanding whether its clinical effect relates to structural brain changes is vital for current and future antidepressant research. To determine whether clinical response to ECT is related to structural volumetric changes in the brain as measured by structural magnetic resonance imaging (MRI) and, if so, which regions are related to this clinical effect. We also determine whether a similar model can be used to identify regions associated with electrode placement (unilateral versus bilateral ECT). Longitudinal MRI and clinical data (Hamilton Depression Rating Scale) was collected from 10 sites as part of the Global ECT-MRI research collaboration (GEMRIC). From 192 subjects, relative changes in 80 (sub)cortical areas were used as potential features for classifying treatment response. We used recursive feature elimination to extract relevant features, which were subsequently used to train a linear classifier. As a validation, the same was done for electrode placement. We report accuracy as well as the structural coefficients of regions included in the discriminative spatial patterns obtained. A pattern of structural changes in cortical midline, striatal and lateral prefrontal areas discriminates responders from non-responders (75% accuracy, p 〈 0.001) while left-sided mediotemporal changes discriminate unilateral from bilateral electrode placement (81% accuracy, p 〈 0.001). The identification of a multivariate discriminative pattern shows that structural change is relevant for clinical response to ECT, but this pattern does not include mediotemporal regions that have been the focus of electroconvulsive therapy research so far. •A pattern of structural change induced by ECT is associated with clinical response.•This pattern includes areas heavily implicated in the pathophysiology of depression.•Mediotemporal changes were related to electrode placement, but not clinical outcome.
    Subject(s): Depression ; Electroconvulsive therapy ; MRI ; Major depressive disorder ; Physiological aspects ; Care and treatment ; Usage ; Prefrontal cortex ; Index Medicus ; Clinical Medicine ; Radiologi och bildbehandling ; Medical and Health Sciences ; Medicin och hälsovetenskap ; Radiology, Nuclear Medicine and Medical Imaging ; Klinisk medicin
    ISSN: 1935-861X
    E-ISSN: 1876-4754
    Source: Directory of Open Access Journals
    Source: © ProQuest LLC All rights reserved〈img src="https://exlibris-pub.s3.amazonaws.com/PQ_Logo.jpg" style="vertical-align:middle;margin-left:7px"〉
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  • 10
    Language: English
    In: Brain stimulation, 2020-05-01, Vol.13 (3), p.696-704
    Description: Background: Electroconvulsive therapy (ECT) is the most effective treatment option for major depressive disorder, so understanding whether its clinical effect relates to structural brain changes is vital for current and future antidepressant research. Objective: To determine whether clinical response to ECT is related to structural volumetric changes in the brain as measured by structural magnetic resonance imaging (MRI) and, if so, which regions are related to this clinical effect. We also determine whether a similar model can be used to identify regions associated with electrode placement (unilateral versus bilateral ECT). Methods: Longitudinal MRI and clinical data (Hamilton Depression Rating Scale) was collected from 10 sites as part of the Global ECT-MRI research collaboration (GEMRIC). From 192 subjects, relative changes in 80 (sub)cortical areas were used as potential features for classifying treatment response. We used recursive feature elimination to extract relevant features, which were subsequently used to train a linear classifier. As a validation, the same was done for electrode placement. We report accuracy as well as the structural coefficients of regions included in the discriminative spatial patterns obtained. Results: A pattern of structural changes in cortical midline, striatal and lateral prefrontal areas discriminates responders from non-responders (75% accuracy, p 〈 0.001) while left-sided mediotemporal changes discriminate unilateral from bilateral electrode placement (81% accuracy, p 〈 0.001). Conclusions: The identification of a multivariate discriminative pattern shows that structural change is relevant for clinical response to ECT, but this pattern does not include mediotemporal regions that have been the focus of electroconvulsive therapy research so far.
    Subject(s): Electroconvulsive therapy ; Clinical Neurology ; MRI ; Depression ; Biophysics ; Neuroscience(all) ; Major depressive disorder
    ISSN: 1935-861X
    E-ISSN: 1876-4754
    Source: Directory of Open Access Journals
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