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Article ; Online: COVID-19: The Effect of Host Genetic Variations on Host-Virus Interactions.

Chakravarty, Suvobrata

2020 Volume 20, Issue 1, Page(s) 139–153

Abstract: Spurred into action by the COVID-19 pandemic, the global scientific community has, in a short of period of time, made astonishing progress in understanding and combating COVID-19. Given the known human protein machinery for (a) SARS-CoV-2 entry, (b) the ... ...

Abstract	Spurred into action by the COVID-19 pandemic, the global scientific community has, in a short of period of time, made astonishing progress in understanding and combating COVID-19. Given the known human protein machinery for (a) SARS-CoV-2 entry, (b) the host innate immune response, and (c) virus-host interactions (protein-protein and RNA-protein), the potential effects of human genetic variation in this machinery, which may contribute to clinical differences in SARS-CoV-2 pathogenesis and help determine individual risk for COVID-19 infection, are explored. The Genome Aggregation Database (gnomAD) was used to show that several
MeSH term(s)	Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/metabolism ; COVID-19/genetics ; COVID-19/immunology ; Genetic Variation ; Host-Pathogen Interactions/genetics ; Humans ; Immunity, Innate/genetics ; Quantitative Trait Loci ; RNA, Viral/metabolism ; SARS-CoV-2/pathogenicity ; Toll-Like Receptor 3/genetics ; Toll-Like Receptor 7/genetics ; Virus Internalization
Chemical Substances	RNA, Viral ; TLR3 protein, human ; TLR7 protein, human ; Toll-Like Receptor 3 ; Toll-Like Receptor 7 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2020-12-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.0c00637
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Article ; Online: AQcalc: A web server that identifies weak molecular interactions in protein structures.

Afshinpour, Maral / Smith, Logan A / Chakravarty, Suvobrata

Protein science : a publication of the Protein Society

2023 Volume 32, Issue 10, Page(s) e4762

Abstract: Weak molecular interactions play an important role in protein structure and function. Computational tools that identify weak molecular interactions are, therefore, valuable for the study of proteins. Here, we present AQcalc, a web server (https:// ... ...

Abstract	Weak molecular interactions play an important role in protein structure and function. Computational tools that identify weak molecular interactions are, therefore, valuable for the study of proteins. Here, we present AQcalc, a web server (https://aqcalcbiocomputing.com/) that can be used to identify anion-quadrupole (AQ) interactions, which are weak interactions involving aromatic residue (Trp, Tyr, and Phe) ring edges and anions (Asp, Glu, and phosphate ion) both within proteins and at their interfaces (protein-protein, protein-nucleic acids, and protein-lipid bilayer). AQcalc identifies AQ interactions as well as clusters involving AQ, cation-π, and salt bridges, among others. Utilizing AQcalc we analyzed weak interactions in protein models, even in the absence of experimental structures, to understand the contributions of weak interactions to deleterious structural changes, including those associated with oncogenic and germline disease variants. We identified several deleterious variants with disrupted AQ interactions (comparable in frequency to cation-π disruptions). Amyloid fibrils utilize AQ to bury anions at frequencies that far exceed those observed for globular proteins. AQ interactions were detected three and five times more frequently than the hydrogen-bonded AQ (HBAQ) in fibril structures and protein-lipid bilayer interfaces, respectively. By contrast, AQ and HBAQ interactions were detected with similar frequencies in globular proteins. Collectively, these findings suggest AQcalc will be effective in facilitating fine structural analysis. As other web utilities designed to identify protein residue interaction networks do not report AQ interactions, wide use of AQcalc will enrich our understanding of residue interaction networks and facilitate hypothesis testing by identifying and experimentally characterizing these comparably weak but important interactions.
MeSH term(s)	Lipid Bilayers ; Models, Molecular ; Proteins/chemistry ; Anions/chemistry ; Cations/chemistry
Chemical Substances	Lipid Bilayers ; Proteins ; Anions ; Cations
Language	English
Publishing date	2023-08-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4762
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: FRETting about the affinity of bimolecular protein-protein interactions.

Lin, Tao / Scott, Brandon L / Hoppe, Adam D / Chakravarty, Suvobrata

Protein science : a publication of the Protein Society

2018 Volume 27, Issue 10, Page(s) 1850–1856

Abstract: Fluorescence resonance energy transfer (FRET) is a powerful tool to study macromolecular interactions such as protein-protein interactions (PPIs). Fluorescent protein (FP) fusions enable FRET-based PPI analysis of signaling pathways and molecular ... ...

Abstract	Fluorescence resonance energy transfer (FRET) is a powerful tool to study macromolecular interactions such as protein-protein interactions (PPIs). Fluorescent protein (FP) fusions enable FRET-based PPI analysis of signaling pathways and molecular structure in living cells. Despite FRET's importance in PPI studies, FRET has seen limited use in quantifying the affinities of PPIs in living cells. Here, we have explored the relationship between FRET efficiency and PPI affinity over a wide range when expressed from a single plasmid system in Escherichia coli. Using live-cell microscopy and a set of 20 pairs of small interacting proteins, belonging to different structural folds and interaction affinities, we demonstrate that FRET efficiency can reliably measure the dissociation constant (K
MeSH term(s)	Escherichia coli/chemistry ; Escherichia coli/cytology ; Escherichia coli/metabolism ; Fluorescence Resonance Energy Transfer ; Luminescent Proteins/chemistry ; Luminescent Proteins/metabolism ; Protein Binding
Chemical Substances	Luminescent Proteins
Language	English
Publishing date	2018-07-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.3482
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Article ; Online: A simple and sensitive SYBR Gold-based assay to quantify DNA-protein interactions.

Schreier, Spencer / Petla, Bhanu Prakash / Lin, Tao / Chakravarty, Suvobrata / Subramanian, Senthil

Plant molecular biology

2019 Volume 101, Issue 4-5, Page(s) 499–506

Abstract: A simple, accessible, and inexpensive assay to quantify the strength of DNA-protein interactions was developed. The assay relies on capturing DNA-protein complexes using an affinity resin that binds tagged, recombinant proteins. Sequential washes with ... ...

Abstract	A simple, accessible, and inexpensive assay to quantify the strength of DNA-protein interactions was developed. The assay relies on capturing DNA-protein complexes using an affinity resin that binds tagged, recombinant proteins. Sequential washes with filtration spin cups and centrifugation remove non-specific interactions in a gentle, uniform manner and a final elution isolates specific DNA-protein complexes. SYBR Gold nucleic acid stain is added to the eluted product and the fluorescence intensity accurately quantifies the amount of captured DNA, ultimately illustrating the relative strength of the DNA-protein interaction. The major utility of the assay resides in the versatility and quantitative nature of the SYBR Gold:nucleic acid interaction, eliminating the need for customized or labeled oligos and permitting relatively inexpensive quantification of binding capacity. The assay also employs DNA-protein complex capture by the very common purification tag, 6xHis, but other tags could likely be utilized. Further, SYBR Gold fluorescence is compatible with a wide variety of instruments, including UV transilluminators, a staple to any molecular biology laboratory. This assay was used to compare the binding capacities of different auxin response factor (ARF) transcription factors to various dsDNA targets, including the classical AuxRE motif and several divergent sequences. Results from dose-response assays suggest that different ARF proteins might show distinct comparative affinities for AuxRE variants, emphasizing that specific ARF-AuxRE binding strengths likely contribute to the complex and fine-tuned cellular auxin response.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; DNA, Plant/metabolism ; DNA-Binding Proteins/metabolism ; Fluorescence ; Organic Chemicals ; Plant Proteins/metabolism ; Protein Binding ; Sensitivity and Specificity ; Glycine max/metabolism ; Transcription Factors/metabolism
Chemical Substances	ARF1 protein, Arabidopsis ; Arabidopsis Proteins ; DNA, Plant ; DNA-Binding Proteins ; MONOPTEROS protein, Arabidopsis ; Organic Chemicals ; Plant Proteins ; SYBR Gold nucleic acid gel stain ; Transcription Factors
Language	English
Publishing date	2019-10-16
Publishing country	Netherlands
Document type	Journal Article ; Validation Study
ZDB-ID	778032-1
ISSN	1573-5028 ; 0167-4412
ISSN (online)	1573-5028
ISSN	0167-4412
DOI	10.1007/s11103-019-00922-x
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Article: A Comprehensive Analysis of Anion–Quadrupole Interactions in Protein Structures

Chakravarty, Suvobrata / Ung, Adron R / Moore, Brian / Shore, Jay / Alshamrani, Mona

Biochemistry. 2018 Feb. 26, v. 57, no. 12

2018

Abstract: The edgewise interactions of anions with phenylalanine (Phe) aromatic rings in proteins, known as anion–quadrupole interactions, have been well studied. However, the anion–quadrupole interactions of the tyrosine (Tyr) and tryptophan (Trp) rings have been ...

Abstract	The edgewise interactions of anions with phenylalanine (Phe) aromatic rings in proteins, known as anion–quadrupole interactions, have been well studied. However, the anion–quadrupole interactions of the tyrosine (Tyr) and tryptophan (Trp) rings have been less well studied, probably because these have been considered weaker than interactions of anions hydrogen bonded to Trp/Tyr side chains. Distinguishing such hydrogen bonding interactions, we comprehensively surveyed the edgewise interactions of certain anions (aspartate, glutamate, and phosphate) with Trp, Tyr, and Phe rings in high-resolution, nonredundant protein single chains and interfaces (protein–protein, DNA/RNA–protein, and membrane–protein). Trp/Tyr anion–quadrupole interactions are common, with Trp showing the highest propensity and average interaction energy for this type of interaction. The energy of an anion–quadrupole interaction (−15.0 to 0.0 kcal/mol, based on quantum mechanical calculations) depends not only on the interaction geometry but also on the ring atom. The phosphate anions at DNA/RNA–protein interfaces interact with aromatic residues with energies comparable to that of aspartate/glutamate anion–quadrupole interactions. At DNA–protein interfaces, the frequency of aromatic ring participation in anion–quadrupole interactions is comparable to that of positive charge participation in salt bridges, suggesting an underappreciated role for anion–quadrupole interactions at DNA–protein (or membrane–protein) interfaces. Although less frequent than salt bridges in single-chain proteins, we observed highly conserved anion–quadrupole interactions in the structures of remote homologues, and evolutionary covariance-based residue contact score predictions suggest that conserved anion–quadrupole interacting pairs, like salt bridges, contribute to polypeptide folding, stability, and recognition.
Keywords	anions ; aromatic compounds ; aspartic acid ; energy ; glutamic acid ; hydrogen bonding ; phenylalanine ; phosphates ; polypeptides ; prediction ; protein structure ; proteins ; quantum mechanics ; tryptophan ; tyrosine
Language	English
Dates of publication	2018-0226
Size	p. 1852-1867.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.7b01006
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Histone Peptide Recognition by KDM5B-PHD1: A Case Study.

Chakravarty, Suvobrata / Essel, Francisca / Lin, Tao / Zeigler, Stad

Biochemistry

2015 Volume 54, Issue 37, Page(s) 5766–5780

Abstract: A detailed understanding of the energetic contributions to histone peptide recognition would be valuable for a better understanding of chromatin anchoring mechanisms and histone diagnostic design. Here, we probed the energetic contributions to recognize ... ...

Abstract	A detailed understanding of the energetic contributions to histone peptide recognition would be valuable for a better understanding of chromatin anchoring mechanisms and histone diagnostic design. Here, we probed the energetic contributions to recognize the same unmodified histone H3 by three different plant homeodomain (PHD) H3K4me0 readers: hKDM5B-PHD1 (first PHD finger of hKDM5B), hBAZ2A-PHD, and hAIRE-PHD1. The energetic contributions of residues differ significantly from one complex to the next. For example, H3K4A substitution completely aborts the formation of the hAIRE-histone peptide complex, while it has only a small destabilizing effect on binding of the other readers, even though H3K4 methylation disrupts all three complexes. Packing density suggests that methylation of more tightly packed Lys/Arg residues can disrupt binding, even if the energetic contribution is small. The binding behavior of hKDM5B-PHD1 and hBAZ2A-PHD is similar, and like PHD H3R2 readers, both possess a pair of Asp residues in the treble clef for interaction with H3R2. PHD subtype sequences, especially the tandem PHD-PHD fingers, show enrichment in the treble clef Asp residues, suggesting that it is a subtype-specific property. These Asp residues make significant energetic contributions to the formation of the hKDM5B-histone peptide complex, suggesting that there are interactions in addition to those reported in the recent NMR structure. However, the presence of the treble clef Asp in PHD sequences may not always be sufficient for histone peptide binding. This study showcases reader-histone peptide interactions in the context of residue conservation, energetic contributions, interfacial packing, and sequence-based reader subtype predictability.
MeSH term(s)	Amino Acid Sequence ; Chromosomal Proteins, Non-Histone/chemistry ; Histones/chemistry ; Humans ; Jumonji Domain-Containing Histone Demethylases/chemistry ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nuclear Proteins/chemistry ; Peptides/chemistry ; Protein Structure, Tertiary ; Repressor Proteins/chemistry ; Sequence Homology, Amino Acid ; Thermodynamics ; Transcription Factors/chemistry ; AIRE Protein
Chemical Substances	BAZ2A protein, human ; Chromosomal Proteins, Non-Histone ; Histones ; Nuclear Proteins ; Peptides ; Repressor Proteins ; Transcription Factors ; Jumonji Domain-Containing Histone Demethylases (EC 1.14.11.-) ; KDM5B protein, human (EC 1.14.11.-)
Language	English
Publishing date	2015-09-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.5b00617
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Article ; Online: A Comprehensive Analysis of Anion-Quadrupole Interactions in Protein Structures.

Chakravarty, Suvobrata / Ung, Adron R / Moore, Brian / Shore, Jay / Alshamrani, Mona

Biochemistry

2018 Volume 57, Issue 12, Page(s) 1852–1867

Abstract: The edgewise interactions of anions with phenylalanine (Phe) aromatic rings in proteins, known as anion-quadrupole interactions, have been well studied. However, the anion-quadrupole interactions of the tyrosine (Tyr) and tryptophan (Trp) rings have been ...

Abstract	The edgewise interactions of anions with phenylalanine (Phe) aromatic rings in proteins, known as anion-quadrupole interactions, have been well studied. However, the anion-quadrupole interactions of the tyrosine (Tyr) and tryptophan (Trp) rings have been less well studied, probably because these have been considered weaker than interactions of anions hydrogen bonded to Trp/Tyr side chains. Distinguishing such hydrogen bonding interactions, we comprehensively surveyed the edgewise interactions of certain anions (aspartate, glutamate, and phosphate) with Trp, Tyr, and Phe rings in high-resolution, nonredundant protein single chains and interfaces (protein-protein, DNA/RNA-protein, and membrane-protein). Trp/Tyr anion-quadrupole interactions are common, with Trp showing the highest propensity and average interaction energy for this type of interaction. The energy of an anion-quadrupole interaction (-15.0 to 0.0 kcal/mol, based on quantum mechanical calculations) depends not only on the interaction geometry but also on the ring atom. The phosphate anions at DNA/RNA-protein interfaces interact with aromatic residues with energies comparable to that of aspartate/glutamate anion-quadrupole interactions. At DNA-protein interfaces, the frequency of aromatic ring participation in anion-quadrupole interactions is comparable to that of positive charge participation in salt bridges, suggesting an underappreciated role for anion-quadrupole interactions at DNA-protein (or membrane-protein) interfaces. Although less frequent than salt bridges in single-chain proteins, we observed highly conserved anion-quadrupole interactions in the structures of remote homologues, and evolutionary covariance-based residue contact score predictions suggest that conserved anion-quadrupole interacting pairs, like salt bridges, contribute to polypeptide folding, stability, and recognition.
MeSH term(s)	Anions ; DNA/chemistry ; DNA-Binding Proteins/chemistry ; Membrane Proteins/chemistry ; Models, Molecular ; Protein Conformation ; RNA/chemistry ; RNA-Binding Proteins/chemistry
Chemical Substances	Anions ; DNA-Binding Proteins ; Membrane Proteins ; RNA-Binding Proteins ; RNA (63231-63-0) ; DNA (9007-49-2)
Language	English
Publishing date	2018-03-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.7b01006
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Article: Histone Peptide Recognition by KDM5B-PHD1: A Case Study

Chakravarty, Suvobrata / Essel Francisca / Lin Tao / Zeigler Stad

Biochemistry. 2015 Sept. 22, v. 54, no. 37

2015

Abstract	A detailed understanding of the energetic contributions to histone peptide recognition would be valuable for a better understanding of chromatin anchoring mechanisms and histone diagnostic design. Here, we probed the energetic contributions to recognize the same unmodified histone H3 by three different plant homeodomain (PHD) H3K4me0 readers: hKDM5B-PHD1 (first PHD finger of hKDM5B), hBAZ2A-PHD, and hAIRE-PHD1. The energetic contributions of residues differ significantly from one complex to the next. For example, H3K4A substitution completely aborts the formation of the hAIREâhistone peptide complex, while it has only a small destabilizing effect on binding of the other readers, even though H3K4 methylation disrupts all three complexes. Packing density suggests that methylation of more tightly packed Lys/Arg residues can disrupt binding, even if the energetic contribution is small. The binding behavior of hKDM5B-PHD1 and hBAZ2A-PHD is similar, and like PHD H3R2 readers, both possess a pair of Asp residues in the treble clef for interaction with H3R2. PHD subtype sequences, especially the tandem PHDâPHD fingers, show enrichment in the treble clef Asp residues, suggesting that it is a subtype-specific property. These Asp residues make significant energetic contributions to the formation of the hKDM5Bâhistone peptide complex, suggesting that there are interactions in addition to those reported in the recent NMR structure. However, the presence of the treble clef Asp in PHD sequences may not always be sufficient for histone peptide binding. This study showcases readerâhistone peptide interactions in the context of residue conservation, energetic contributions, interfacial packing, and sequence-based reader subtype predictability.
Keywords	case studies ; chromatin ; histones ; methylation ; nuclear magnetic resonance spectroscopy
Language	English
Dates of publication	2015-0922
Size	p. 5766-5780.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021%2Facs.biochem.5b00617
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Phenethylisothiocyanate alters site- and promoter-specific histone tail modifications in cancer cells.

Yi Liu / Suvobrata Chakravarty / Moul Dey

PLoS ONE, Vol 8, Iss 5, p e

2013 Volume 64535

Abstract: Site-specific histone modifications are important epigenetic regulators of gene expression. As deregulation of genes often results in complex disorders, corrective modulation of site-specific histone marks could be a powerful therapeutic or disease- ... ...

Abstract	Site-specific histone modifications are important epigenetic regulators of gene expression. As deregulation of genes often results in complex disorders, corrective modulation of site-specific histone marks could be a powerful therapeutic or disease-preventive strategy. However, such modulation by dietary compounds and the resulting impact on disease risk remain relatively unexplored. Here we examined phenethylisothiocyanate (PEITC), a common dietary compound derived from cruciferous vegetables with known chemopreventive properties under experimental conditions, as a possible modulator of histone modifications in human colon cancer cells. The present study reports novel, dynamic, site-specific chemical changes to histone H3 in a gene-promoter-specific manner, associated with PEITC exposure in human colon tumor-derived SW480 epithelial cells. In addition, PEITC attenuated cell proliferation in a concentration- and time-dependent manner, likely mediated by caspase-dependent apoptotic signalling. The effects of PEITC on histone modifications and gene expression changes were achieved at low, non-cytotoxic concentrations, in contrast to the higher concentrations necessary to halt cancer cell proliferation. Increased understanding of specific epigenetic alterations by dietary compounds may provide improved chemopreventive strategies for reducing the healthcare burden of cancer and other human diseases.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Phenethylisothiocyanate alters site- and promoter-specific histone tail modifications in cancer cells.

Liu, Yi / Chakravarty, Suvobrata / Dey, Moul

PloS one

2013 Volume 8, Issue 5, Page(s) e64535

Abstract	Site-specific histone modifications are important epigenetic regulators of gene expression. As deregulation of genes often results in complex disorders, corrective modulation of site-specific histone marks could be a powerful therapeutic or disease-preventive strategy. However, such modulation by dietary compounds and the resulting impact on disease risk remain relatively unexplored. Here we examined phenethylisothiocyanate (PEITC), a common dietary compound derived from cruciferous vegetables with known chemopreventive properties under experimental conditions, as a possible modulator of histone modifications in human colon cancer cells. The present study reports novel, dynamic, site-specific chemical changes to histone H3 in a gene-promoter-specific manner, associated with PEITC exposure in human colon tumor-derived SW480 epithelial cells. In addition, PEITC attenuated cell proliferation in a concentration- and time-dependent manner, likely mediated by caspase-dependent apoptotic signalling. The effects of PEITC on histone modifications and gene expression changes were achieved at low, non-cytotoxic concentrations, in contrast to the higher concentrations necessary to halt cancer cell proliferation. Increased understanding of specific epigenetic alterations by dietary compounds may provide improved chemopreventive strategies for reducing the healthcare burden of cancer and other human diseases.
MeSH term(s)	Acetylation/drug effects ; Apoptosis/drug effects ; Apoptosis/genetics ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Chemokines/metabolism ; Colonic Neoplasms/enzymology ; Colonic Neoplasms/genetics ; Colonic Neoplasms/pathology ; DNA Fragmentation/drug effects ; Dose-Response Relationship, Drug ; Down-Regulation/drug effects ; Down-Regulation/genetics ; Gene Expression Regulation, Neoplastic/drug effects ; Histones/metabolism ; Humans ; Isothiocyanates/pharmacology ; Matrix Metalloproteinases/metabolism ; Methylation/drug effects ; Promoter Regions, Genetic ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Time Factors ; Transcription Factors/metabolism
Chemical Substances	Chemokines ; Histones ; Isothiocyanates ; RNA, Messenger ; Transcription Factors ; phenethyl isothiocyanate (6U7TFK75KV) ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2013-05-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0064535
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