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Article ; Online: Editorial: Developing therapeutics for antimicrobial resistant pathogens.

Veerapandian, Raja / Abdul Azees, Parveez Ahamed / Viswanathan, Thiruselvam / Amaechi, Bennett Tochukwu / Vediyappan, Govindsamy

Frontiers in cellular and infection microbiology

2022 Volume 12, Page(s) 1083501

Language	English
Publishing date	2022-11-24
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.1083501
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Article ; Online: The ArsQ permease and transport of the antibiotic arsinothricin.

Paul, Ngozi P / Viswanathan, Thiruselvam / Chen, Jian / Yoshinaga, Masafumi / Rosen, Barry P

Molecular microbiology

2023 Volume 119, Issue 4, Page(s) 505–514

Abstract: The pentavalent organoarsenical arsinothricin (AST) is a natural product synthesized by the rhizosphere bacterium Burkholderia gladioli GSRB05. AST is a broad-spectrum antibiotic effective against human pathogens such as carbapenem-resistant Enterobacter ...

Abstract	The pentavalent organoarsenical arsinothricin (AST) is a natural product synthesized by the rhizosphere bacterium Burkholderia gladioli GSRB05. AST is a broad-spectrum antibiotic effective against human pathogens such as carbapenem-resistant Enterobacter cloacae. It is a non-proteogenic amino acid and glutamate mimetic that inhibits bacterial glutamine synthetase. The AST biosynthetic pathway is composed of a three-gene cluster, arsQML. ArsL catalyzes synthesis of reduced trivalent hydroxyarsinothricin (R-AST-OH), which is methylated by ArsM to the reduced trivalent form of AST (R-AST). In the culture medium of B. gladioli, both trivalent species appear as the corresponding pentavalent arsenicals, likely due to oxidation in air. ArsQ is an efflux permease that is proposed to transport AST or related species out of the cells, but the chemical nature of the actual transport substrate is unclear. In this study, B. gladioli arsQ was expressed in Escherichia coli and shown to confer resistance to AST and its derivatives. Cells of E. coli accumulate R-AST, and exponentially growing cells expressing arsQ take up less R-AST. The cells exhibit little transport of their pentavalent forms. Transport was independent of cellular energy and appears to be equilibrative. A homology model of ArsQ suggests that Ser320 is in the substrate binding site. A S320A mutant exhibits reduced R-AST-OH transport, suggesting that it plays a role in ArsQ function. The ArsQ permease is proposed to be an energy-independent uniporter responsible for downhill transport of the trivalent form of AST out of cells, which is oxidized extracellularly to the active form of the antibiotic.
MeSH term(s)	Humans ; Membrane Transport Proteins/metabolism ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/metabolism ; Escherichia coli/metabolism ; Arsenicals/metabolism ; Escherichia coli Proteins/metabolism ; Symporters/metabolism ; Biological Transport, Active
Chemical Substances	Membrane Transport Proteins ; arsinothricin ; Anti-Bacterial Agents ; Arsenicals ; Escherichia coli Proteins ; Symporters
Language	English
Publishing date	2023-02-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.15045
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Article ; Online: Selective Methylation by an ArsM

Chen, Jian / Galván, Adriana E / Viswanathan, Thiruselvam / Yoshinaga, Masafumi / Rosen, Barry P

Environmental science & technology

2022 Volume 56, Issue 19, Page(s) 13858–13866

Abstract: Arsenic methylation contributes to the formation and diversity of environmental organoarsenicals, an important process in the arsenic biogeochemical cycle. ... ...

Abstract	Arsenic methylation contributes to the formation and diversity of environmental organoarsenicals, an important process in the arsenic biogeochemical cycle. The
MeSH term(s)	Anti-Bacterial Agents ; Arsenic/metabolism ; Arsenicals/metabolism ; Arsenites/metabolism ; Burkholderia gladioli/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Methylation ; Methyltransferases/chemistry ; Methyltransferases/genetics ; Methyltransferases/metabolism ; S-Adenosylmethionine/metabolism
Chemical Substances	Anti-Bacterial Agents ; Arsenicals ; Arsenites ; arsinothricin ; S-Adenosylmethionine (7LP2MPO46S) ; Methyltransferases (EC 2.1.1.-) ; Arsenic (N712M78A8G)
Language	English
Publishing date	2022-09-16
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ISSN	1520-5851
ISSN (online)	1520-5851
DOI	10.1021/acs.est.2c04324
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Article: A metal ion orients mRNA to ensure accurate 2'-

Viswanathan, Thiruselvam / Misra, Anurag / Chan, Siu-Hong / Qi, Shan / Dai, Nan / Arya, Shailee / Martinez-Sobrido, Luis / Gupta, Yogesh K

bioRxiv : the preprint server for biology

2021

Abstract: The SARS-CoV-2 nsp16/nsp10 enzyme complex modifies the 2'-OH of the first transcribed nucleotide of the viral mRNA by covalently attaching a methyl group to it. The 2'- ...

Abstract	The SARS-CoV-2 nsp16/nsp10 enzyme complex modifies the 2'-OH of the first transcribed nucleotide of the viral mRNA by covalently attaching a methyl group to it. The 2'-
Language	English
Publishing date	2021-03-12
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.03.12.435174
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Article ; Online: A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2′-O methylation of its first nucleotide

Thiruselvam Viswanathan / Anurag Misra / Siu-Hong Chan / Shan Qi / Nan Dai / Shailee Arya / Luis Martinez-Sobrido / Yogesh K. Gupta

Nature Communications, Vol 12, Iss 1, Pp 1-

2021 Volume 7

Abstract: The SARS-CoV-2 nsp16/nsp10 enzyme complex methylates the 2′-OH of the first nucleotide of the viral mRNA, converting the Cap-0 to Cap-1, which helps the virus to evade immune surveillance in the host cell. Here, the authors present the crystal structure ... ...

Abstract	The SARS-CoV-2 nsp16/nsp10 enzyme complex methylates the 2′-OH of the first nucleotide of the viral mRNA, converting the Cap-0 to Cap-1, which helps the virus to evade immune surveillance in the host cell. Here, the authors present the crystal structure of SARS-CoV-2 nsp16/nsp10 with the bound Cap-1 RNA nucleotide product and a post-release SAH containing structure.
Keywords	Science ; Q
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Crystal structure analysis of a hypothetical protein (MJ0366) from Methanocaldococcus jannaschii revealed a novel topological arrangement of the knot fold.

Thiruselvam, Viswanathan / Kumarevel, Thirumananseri / Karthe, Ponnuraj / Kuramitsu, Seiki / Yokoyama, Shigeyuki / Ponnuswamy, Mondikalipudur Nanjappagounder

Biochemical and biophysical research communications

2017 Volume 482, Issue 2, Page(s) 264–269

Abstract: The crystal structure of a hypothetical protein MJ0366, derived from Methanocaldococcus jannaschii was solved at 1.9 Å resolution using synchrotron radiation. MJ0366 was crystallized as a monomer and has knot structural arrangement. Intriguingly, the ... ...

Abstract	The crystal structure of a hypothetical protein MJ0366, derived from Methanocaldococcus jannaschii was solved at 1.9 Å resolution using synchrotron radiation. MJ0366 was crystallized as a monomer and has knot structural arrangement. Intriguingly, the solved structure consists of novel 'KNOT' fold conformation. The 3
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/ultrastructure ; Computer Simulation ; Crystallography ; Methanocaldococcus/metabolism ; Models, Chemical ; Models, Molecular ; Protein Conformation ; Protein Folding
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2017-01-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2016.11.052
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Article ; Online: Functional and structural characterization of AntR, an Sb(III) responsive transcriptional repressor.

Viswanathan, Thiruselvam / Chen, Jian / Wu, Minghan / An, Lijin / Kandavelu, Palani / Sankaran, Banumathi / Radhakrishnan, Manohar / Li, Mingshun / Rosen, Barry P

Molecular microbiology

2021 Volume 116, Issue 2, Page(s) 427–437

Abstract: The ant operon of the antimony-mining bacterium Comamonas testosterone JL40 confers resistance to Sb(III). The operon is transcriptionally regulated by the product of the first gene in the operon, antR. AntR is a member of ArsR/SmtB family of metal/ ... ...

Abstract	The ant operon of the antimony-mining bacterium Comamonas testosterone JL40 confers resistance to Sb(III). The operon is transcriptionally regulated by the product of the first gene in the operon, antR. AntR is a member of ArsR/SmtB family of metal/metalloid-responsive repressors resistance. We purified and characterized C. testosterone AntR and demonstrated that it responds to metalloids in the order Sb(III) = methylarsenite (MAs(III) >> As(III)). The protein was crystallized, and the structure was solved at 2.1 Å resolution. The homodimeric structure of AntR adopts a classical ArsR/SmtB topology architecture. The protein has five cysteine residues, of which Cys103
MeSH term(s)	Amino Acid Sequence ; Antimony/pharmacology ; Arsenic/pharmacology ; Arsenicals/pharmacology ; Binding Sites ; Comamonas testosteroni/drug effects ; Comamonas testosteroni/genetics ; Comamonas testosteroni/metabolism ; Gene Expression Regulation, Bacterial/drug effects ; Gene Expression Regulation, Bacterial/genetics ; Protein Conformation ; Repressor Proteins/drug effects ; Repressor Proteins/metabolism ; Transcription Factors/drug effects ; Transcription Factors/genetics ; Transcription, Genetic/drug effects ; Transcription, Genetic/genetics
Chemical Substances	Arsenicals ; Repressor Proteins ; Transcription Factors ; methylarsine ; Antimony (9IT35J3UV3) ; Arsenic (N712M78A8G)
Language	English
Publishing date	2021-04-16
Publishing country	England
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	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.14721
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Article: Crystal structure analysis of a hypothetical protein (MJ0366) from Methanocaldococcus jannaschii revealed a novel topological arrangement of the knot fold

Thiruselvam, Viswanathan / Thirumananseri Kumarevel / Ponnuraj Karthe / Seiki Kuramitsu / Shigeyuki Yokoyama / Mondikalipudur Nanjappagounder Ponnuswamy

Biochemical and biophysical research communications. 2017 Jan. 08, v. 482

2017

Abstract: The crystal structure of a hypothetical protein MJ0366, derived from Methanocaldococcus jannaschii was solved at 1.9Â Ã resolution using synchrotron radiation. MJ0366 was crystallized as a monomer and has knot structural arrangement. Intriguingly, the ... ...

Abstract	The crystal structure of a hypothetical protein MJ0366, derived from Methanocaldococcus jannaschii was solved at 1.9Â Ã resolution using synchrotron radiation. MJ0366 was crystallized as a monomer and has knot structural arrangement. Intriguingly, the solved structure consists of novel âKNOTâ fold conformation. The 31 trefoil knot was observed in the structure. The N-terminal and C-terminal ends did not participate in knot formation.
Keywords	Methanocaldococcus jannaschii ; crystal structure ; topology
Language	English
Dates of publication	2017-0108
Size	p. 264-269.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2016.11.052
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2'-O methylation of its first nucleotide.

Viswanathan, Thiruselvam / Misra, Anurag / Chan, Siu-Hong / Qi, Shan / Dai, Nan / Arya, Shailee / Martinez-Sobrido, Luis / Gupta, Yogesh K

Nature communications

2021 Volume 12, Issue 1, Page(s) 3287

Abstract: The SARS-CoV-2 nsp16/nsp10 enzyme complex modifies the 2'-OH of the first transcribed nucleotide of the viral mRNA by covalently attaching a methyl group to it. The 2'-O methylation of the first nucleotide converts the status of mRNA cap from Cap-0 to ... ...

Abstract	The SARS-CoV-2 nsp16/nsp10 enzyme complex modifies the 2'-OH of the first transcribed nucleotide of the viral mRNA by covalently attaching a methyl group to it. The 2'-O methylation of the first nucleotide converts the status of mRNA cap from Cap-0 to Cap-1, and thus, helps the virus evade immune surveillance in host cells. Here, we report two structures of nsp16/nsp10 representing pre- and post-release states of the RNA product (Cap-1). We observe overall widening of the enzyme upon product formation, and an inward twisting motion in the substrate binding region upon product release. These conformational changes reset the enzyme for the next round of catalysis. The structures also identify a unique binding mode and the importance of a divalent metal ion for 2'-O methylation. We also describe underlying structural basis for the perturbed enzymatic activity of a clinical variant of SARS-CoV-2, and a previous SARS-CoV outbreak strain.
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Biocatalysis ; Cloning, Molecular ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression Regulation, Viral ; Humans ; Magnesium/chemistry ; Magnesium/metabolism ; Methylation ; Methyltransferases ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; RNA Caps/chemistry ; RNA Caps/genetics ; RNA Caps/metabolism ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; S-Adenosylmethionine/chemistry ; S-Adenosylmethionine/metabolism ; SARS-CoV-2/enzymology ; SARS-CoV-2/genetics ; SARS-CoV-2/ultrastructure ; Sequence Alignment ; Sequence Homology, Amino Acid ; Substrate Specificity ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Viral Regulatory and Accessory Proteins/chemistry ; Viral Regulatory and Accessory Proteins/genetics ; Viral Regulatory and Accessory Proteins/metabolism
Chemical Substances	NSP10 protein, SARS-CoV-2 ; NSP16 protein, SARS-CoV-2 ; RNA Caps ; RNA, Viral ; Recombinant Proteins ; Viral Nonstructural Proteins ; Viral Regulatory and Accessory Proteins ; S-Adenosylmethionine (7LP2MPO46S) ; Methyltransferases (EC 2.1.1.-) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2021-06-02
Publishing country	England
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	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23594-y
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Article ; Online: Structural analyses of the nucleosome complexes with human testis-specific histone variants, hTh2a and hTh2b.

Padavattan, Sivaraman / Thiruselvam, Viswanathan / Shinagawa, Toshie / Hasegawa, Kazuya / Kumasaka, Takashi / Ishii, Shunsuke / Kumarevel, Thirumananseri

Biophysical chemistry

2017 Volume 221, Page(s) 41–48

Abstract: Th2a and Th2b are the testis-specific histone variants highly expressed during spermatogenesis. Approximately 4% of the genome is retained in nucleosomes in mature human sperm, which is enriched at loci of developmental importance. Our recent studies ... ...

Abstract	Th2a and Th2b are the testis-specific histone variants highly expressed during spermatogenesis. Approximately 4% of the genome is retained in nucleosomes in mature human sperm, which is enriched at loci of developmental importance. Our recent studies revealed that the mouse histone variant homologs TH2a and TH2b are involved in reprogramming. In the present work, we report three nucleosome structures (NCPs) with human testis-specific histone variants hTh2a and hTh2b, [hGcH (hTh2a-hTh2b-H3-H4), hGcHV1 (hTh2a-H2b-H3-H4) and hGcHV2 (H2a-hTh2b-H3-H4)] and a 146-base pair (bp) duplex DNA fragment at ~3.0Å resolutions. These crystal structures revealed two major changes within the nucleosomes, either with hTh2a, hTh2b or both variants, as compared to the canonical counterpart. First, the H-bonding interactions between the L1-L1' interfaces mediated by the hTh2a/hTh2a' L1-loops are lost. Second, the histone dimer-DNA contacts are considerably reduced, and these changes are localized around ±31 to 35-bp from the nucleosome entry/exit sites. Thus, the modified functional residues at the N- and C-terminal ends of histone variants are responsible for the observed structural changes and regulate the gene expression through specific structural alterations in the chromatin by modulating the chromatin-associated binding proteins.
MeSH term(s)	Chromatin/chemistry ; Chromatin Assembly and Disassembly/genetics ; Crystallization ; DNA/chemistry ; Gene Expression Regulation ; Genetic Variation ; Histones/genetics ; Humans ; Hydrogen Bonding ; Male ; Nucleosomes/chemistry
Chemical Substances	Chromatin ; Histones ; Nucleosomes ; histone H2B type 1-A ; testis-specific histone TH2A, human ; DNA (9007-49-2)
Language	English
Publishing date	2017-02
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	185052-0
ISSN	1873-4200 ; 0301-4622
ISSN (online)	1873-4200
ISSN	0301-4622
DOI	10.1016/j.bpc.2016.11.013
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