cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.c.3636716_d6.v1
title: Additional file 4: Table S3. of Transcriptional analysis of phloem-associated cells of potato

description: Differentially expressed genes between petiole and stem phloem-associated cells. (XLSX 192 kb)
DOI: 10.6084/m9.figshare.c.3636716_d8.v1
title: Additional file 5: Table S4. of Transcriptional analysis of phloem-associated cells of potato

description: Expression of genes in pet-PAC and stem-PAC with select GO terms. (XLSX 331 kb)
DOI: 10.6084/m9.figshare.c.3636716_d9.v1
title: Additional file 18: Table S12. of Transcriptional analysis of phloem-associated cells of potato

description: RNA-seq of RNA-binding proteins and select TFs. (XLSX 54 kb)
DOI: 10.6084/m9.figshare.c.3636716_d10.v1
title: Additional file 13: Table S11. of Transcriptional analysis of phloem-associated cells of potato

description: Abundant transcripts significantly up-regulated under short days. (XLSX 59 kb)
DOI: 10.6084/m9.figshare.c.3636716_d11.v1
title: Additional file 19: Table S13. of Transcriptional analysis of phloem-associated cells of potato

description: Comparison to Arabidopsis phloem transcripts. (XLSX 42 kb)
DOI: 10.6084/m9.figshare.c.3636716_d13.v1
title: Additional file 6: Table S5. of Transcriptional analysis of phloem-associated cells of potato

description: Expression level of RNA-binding proteins. (XLSX 78 kb)
DOI: 10.6084/m9.figshare.c.3636848_d2.v1
title: MOESM1 of Repositioning of bromocriptine for treatment of acute myeloid leukemia

description: Additional file 1: Table S1. Upregulated probe set upon AML differentiation.
DOI: 10.6084/m9.figshare.28049444.v1
title: 129916_TTAGGC_2_1x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049435.v1
title: 129914_ATCACG_1_1x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049438
title: 129915_CGATGT_1_2x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049438.v1
title: 129915_CGATGT_1_2x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049441
title: 129917_TGACCA_2_2x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049441.v1
title: 129917_TGACCA_2_2x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049444
title: 129916_TTAGGC_2_1x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049447.v1
title: 129918_ACAGTG_3_1x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049435
title: 129914_ATCACG_1_1x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049447
title: 129918_ACAGTG_3_1x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049450
title: 129919_GCCAAT_3_2x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049456
title: 129921_ACTTGA_1_2x_NMM_R1_001_edited_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049456.v1
title: 129921_ACTTGA_1_2x_NMM_R1_001_edited_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049453
title: 129920_CAGATC_1_1x_NMM_R1_001_edited_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049450.v1
title: 129919_GCCAAT_3_2x_SOB_R1_001_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049453.v1
title: 129920_CAGATC_1_1x_NMM_R1_001_edited_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.
DOI: 10.6084/m9.figshare.28049459.v1
title: 129923_TAGCTT_2_2x_NMM_R1_001_edited_Reads_per_uniqueLocation.wig

description: G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in <em>Escherichia coli</em>that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4- stabilizing conditions. Proteomic and transcriptomic analyses demonstrate that ribosome assembly factors and other proteins involved in translation are less abundant in G4-stabilizing conditions. Our results support a model in which reducing the rate of translation by altering translation initiation/elongation, or ribosome assembly can compensate for G4-related stress in E. coli.