LIVIVO - Search results -

Search results

Result 1 - 10 of total 13

Article ; Online: PI(4,5)P

Johnson, Kristen A / Budicini, Melissa R / Bhattarai, Nisha / Sharma, Tej / Urata, Sarah / Gerstman, Bernard S / Chapagain, Prem P / Li, Sheng / Stahelin, Robert V

Journal of lipid research

2024 Volume 65, Issue 3, Page(s) 100512

Abstract: Ebola virus (EBOV) causes severe hemorrhagic fever in humans and is lethal in a large percentage of those infected. The EBOV matrix protein viral protein 40 kDa (VP40) is a peripheral binding protein that forms a shell beneath the lipid bilayer in ... ...

Abstract	Ebola virus (EBOV) causes severe hemorrhagic fever in humans and is lethal in a large percentage of those infected. The EBOV matrix protein viral protein 40 kDa (VP40) is a peripheral binding protein that forms a shell beneath the lipid bilayer in virions and virus-like particles (VLPs). VP40 is required for virus assembly and budding from the host cell plasma membrane. VP40 is a dimer that can rearrange into oligomers at the plasma membrane interface, but it is unclear how these structures form and how they are stabilized. We therefore investigated the ability of VP40 to form stable oligomers using in vitro and cellular assays. We characterized two lysine-rich regions in the VP40 C-terminal domain (CTD) that bind phosphatidylinositol-4,5-bisphosphate (PI(4,5)P
MeSH term(s)	Humans ; Ebolavirus/metabolism ; Hemorrhagic Fever, Ebola/metabolism ; Lysine/metabolism ; Binding Sites ; Lipids ; Protein Binding
Chemical Substances	Lysine (K3Z4F929H6) ; Lipids
Language	English
Publishing date	2024-01-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2024.100512
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 175: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Crystal Structure of the Marburg Virus VP35 Oligomerization Domain.

Bruhn, Jessica F / Kirchdoerfer, Robert N / Urata, Sarah M / Li, Sheng / Tickle, Ian J / Bricogne, Gérard / Saphire, Erica Ollmann

Journal of virology

2017 Volume 91, Issue 2

Abstract: Marburg virus (MARV) is a highly pathogenic filovirus that is classified in a genus distinct from that of Ebola virus (EBOV) (genera Marburgvirus and Ebolavirus, respectively). Both viruses produce a multifunctional protein termed VP35, which acts as a ... ...

Abstract	Marburg virus (MARV) is a highly pathogenic filovirus that is classified in a genus distinct from that of Ebola virus (EBOV) (genera Marburgvirus and Ebolavirus, respectively). Both viruses produce a multifunctional protein termed VP35, which acts as a polymerase cofactor, a viral protein chaperone, and an antagonist of the innate immune response. VP35 contains a central oligomerization domain with a predicted coiled-coil motif. This domain has been shown to be essential for RNA polymerase function. Here we present crystal structures of the MARV VP35 oligomerization domain. These structures and accompanying biophysical characterization suggest that MARV VP35 is a trimer. In contrast, EBOV VP35 is likely a tetramer in solution. Differences in the oligomeric state of this protein may explain mechanistic differences in replication and immune evasion observed for MARV and EBOV. Importance: Marburg virus can cause severe disease, with up to 90% human lethality. Its genome is concise, only producing seven proteins. One of the proteins, VP35, is essential for replication of the viral genome and for evasion of host immune responses. VP35 oligomerizes (self-assembles) in order to function, yet the structure by which it assembles has not been visualized. Here we present two crystal structures of this oligomerization domain. In both structures, three copies of VP35 twist about each other to form a coiled coil. This trimeric assembly is in contrast to tetrameric predictions for VP35 of Ebola virus and to known structures of homologous proteins in the measles, mumps, and Nipah viruses. Distinct oligomeric states of the Marburg and Ebola virus VP35 proteins may explain differences between them in polymerase function and immune evasion. These findings may provide a more accurate understanding of the mechanisms governing VP35's functions and inform the design of therapeutics.
MeSH term(s)	Amino Acid Sequence ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Marburgvirus/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Stability ; Thermodynamics ; Viral Regulatory and Accessory Proteins/chemistry ; Viral Regulatory and Accessory Proteins/metabolism
Chemical Substances	VP35 protein, filovirus ; Viral Regulatory and Accessory Proteins
Language	English
Publishing date	2017-01-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01085-16
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometry.

Wijesinghe, Kaveesha J / Urata, Sarah / Bhattarai, Nisha / Kooijman, Edgar E / Gerstman, Bernard S / Chapagain, Prem P / Li, Sheng / Stahelin, Robert V

The Journal of biological chemistry

2017 Volume 292, Issue 15, Page(s) 6108–6122

Abstract: Marburg virus (MARV) is a lipid-enveloped virus from ... ...

Abstract	Marburg virus (MARV) is a lipid-enveloped virus from the
MeSH term(s)	Deuterium Exchange Measurement ; Marburgvirus/chemistry ; Marburgvirus/genetics ; Marburgvirus/metabolism ; Mass Spectrometry ; Models, Chemical ; Phosphatidylcholines/chemistry ; Phosphatidylserines/chemistry ; Protein Multimerization ; Protein Structure, Quaternary ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism
Chemical Substances	Phosphatidylcholines ; Phosphatidylserines ; VP40 protein, virus ; Viral Matrix Proteins ; 1-palmitoyl-2-oleoylglycero-3-phosphoserine (40290-44-6) ; 1-palmitoyl-2-oleoylphosphatidylcholine (TE895536Y5)
Language	English
Publishing date	2017-02-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M116.758300
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Cryo-electron microscopy structure and analysis of the P-Rex1-Gβγ signaling scaffold.

Cash, Jennifer N / Urata, Sarah / Li, Sheng / Ravala, Sandeep K / Avramova, Larisa V / Shost, Michael D / Gutkind, J Silvio / Tesmer, John J G / Cianfrocco, Michael A

Science advances

2019 Volume 5, Issue 10, Page(s) eaax8855

Abstract: ... ...

Abstract	PIP
MeSH term(s)	Amino Acid Sequence ; Binding Sites/physiology ; Cell Membrane/metabolism ; Cell Movement/physiology ; Cryoelectron Microscopy/methods ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; PTEN Phosphohydrolase/metabolism ; Protein Binding/physiology ; Protein Domains/physiology ; Sequence Alignment ; Signal Transduction/physiology
Chemical Substances	Guanine Nucleotide Exchange Factors ; PREX1 protein, human ; PTEN Phosphohydrolase (EC 3.1.3.67)
Language	English
Publishing date	2019-10-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.aax8855
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Potent anti-influenza H7 human monoclonal antibody induces separation of hemagglutinin receptor-binding head domains.

Turner, Hannah L / Pallesen, Jesper / Lang, Shanshan / Bangaru, Sandhya / Urata, Sarah / Li, Sheng / Cottrell, Christopher A / Bowman, Charles A / Crowe, James E / Wilson, Ian A / Ward, Andrew B

PLoS biology

2019 Volume 17, Issue 2, Page(s) e3000139

Abstract: Seasonal influenza virus infections can cause significant morbidity and mortality, but the threat from the emergence of a new pandemic influenza strain might have potentially even more devastating consequences. As such, there is intense interest in ... ...

Abstract	Seasonal influenza virus infections can cause significant morbidity and mortality, but the threat from the emergence of a new pandemic influenza strain might have potentially even more devastating consequences. As such, there is intense interest in isolating and characterizing potent neutralizing antibodies that target the hemagglutinin (HA) viral surface glycoprotein. Here, we use cryo-electron microscopy (cryoEM) to decipher the mechanism of action of a potent HA head-directed monoclonal antibody (mAb) bound to an influenza H7 HA. The epitope of the antibody is not solvent accessible in the compact, prefusion conformation that typifies all HA structures to date. Instead, the antibody binds between HA head protomers to an epitope that must be partly or transiently exposed in the prefusion conformation. The "breathing" of the HA protomers is implied by the exposure of this epitope, which is consistent with metastability of class I fusion proteins. This structure likely therefore represents an early structural intermediate in the viral fusion process. Understanding the extent of transient exposure of conserved neutralizing epitopes also may lead to new opportunities to combat influenza that have not been appreciated previously.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/genetics ; Antibodies, Neutralizing/metabolism ; Antibody Specificity ; Baculoviridae/genetics ; Baculoviridae/metabolism ; Binding Sites ; Cloning, Molecular ; Cryoelectron Microscopy ; Gene Expression ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Fab Fragments/genetics ; Immunoglobulin Fab Fragments/metabolism ; Influenza A virus/chemistry ; Influenza A virus/genetics ; Influenza A virus/immunology ; Molecular Docking Simulation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sf9 Cells ; Spodoptera
Chemical Substances	Antibodies, Neutralizing ; Hemagglutinin Glycoproteins, Influenza Virus ; Immunoglobulin Fab Fragments ; Recombinant Proteins
Language	English
Publishing date	2019-02-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.3000139
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6193: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Radioprotective effects produced by the condensation of plasmid DNA with avidin and biotinylated gold nanoparticles.

Perry, Christopher C / Urata, Sarah M / Lee, Melissa / Aguilera, Joe A / Milligan, Jamie R

Radiation and environmental biophysics

2012 Volume 51, Issue 4, Page(s) 457–468

Abstract: The treatment of aqueous solutions of plasmid DNA with the protein avidin results in significant changes in physical, chemical, and biochemical properties. These effects include increased light scattering, formation of micron-sized particles containing ... ...

Abstract	The treatment of aqueous solutions of plasmid DNA with the protein avidin results in significant changes in physical, chemical, and biochemical properties. These effects include increased light scattering, formation of micron-sized particles containing both DNA and protein, and plasmid protection against thermal denaturation, radical attack, and nuclease digestion. All of these changes are consistent with condensation of the plasmid by avidin. Avidin can be displaced from the plasmid at higher ionic strengths. Avidin is not displaced from the plasmid by an excess of a tetra-arginine ligand, nor by the presence of biotin. Therefore, this system offers the opportunity to reversibly bind biotin-labeled species to a condensed DNA-protein complex. An example application is the use of biotinylated gold nanoparticles. This system offers the ability to examine in better detail the chemical mechanisms involved in important radiobiological effects. Examples include protein modulation of radiation damage to DNA, and radiosensitization by gold nanoparticles.
MeSH term(s)	Avidin/chemistry ; Biotin/chemistry ; Cesium Radioisotopes ; DNA/chemistry ; DNA/radiation effects ; DNA Damage ; Gold/chemistry ; Metal Nanoparticles/chemistry ; Plasmids ; Radiation-Protective Agents/chemistry
Chemical Substances	Cesium Radioisotopes ; Radiation-Protective Agents ; Avidin (1405-69-2) ; Biotin (6SO6U10H04) ; Gold (7440-57-5) ; DNA (9007-49-2)
Language	English
Publishing date	2012-07-24
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	124987-3
ISSN	1432-2099 ; 0301-634X
ISSN (online)	1432-2099
ISSN	0301-634X
DOI	10.1007/s00411-012-0429-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 120: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Free terminal amines in DNA-binding peptides alter the product distribution from guanine radicals produced by single electron oxidation.

Konigsfeld, Katie M / Lee, Melissa / Urata, Sarah M / Aguilera, Joe A / Milligan, Jamie R

International journal of radiation biology

2012 Volume 88, Issue 3, Page(s) 230–238

Abstract: Purpose: Electron deficient guanine radical species are major intermediates produced in DNA by the direct effect of ionizing irradiation. There is evidence that they react with amine groups in closely bound ligands to form covalent crosslinks. Crosslink ...

Abstract	Purpose: Electron deficient guanine radical species are major intermediates produced in DNA by the direct effect of ionizing irradiation. There is evidence that they react with amine groups in closely bound ligands to form covalent crosslinks. Crosslink formation is very poorly characterized in terms of quantitative rate and yield data. We sought to address this issue by using oligo-arginine ligands to model the close association of DNA and its binding proteins in chromatin. Materials and methods: Guanine radicals were prepared in plasmid DNA by single electron oxidation. The product distribution derived from them was assayed by strand break formation after four different post-irradiation incubations. Results: We compared the yields of DNA damage produced in the presence of four ligands in which neither, one, or both of the amino and carboxylate termini were blocked with amides. Free carboxylate groups were unreactive. Significantly higher yields of heat labile sites were observed when the amino terminus was unblocked. The rate of the reaction was characterized by diluting the unblocked amino group with its amide blocked derivative. Conclusion: These observations provide a means to develop quantitative estimates for the yields in which these labile sites are formed in chromatin by exposure to ionizing irradiation.
MeSH term(s)	Amines/metabolism ; Chromatin/metabolism ; DNA/chemistry ; DNA/genetics ; DNA/metabolism ; DNA Breaks, Single-Stranded/radiation effects ; Electron Transport/radiation effects ; Free Radicals/metabolism ; Guanine/metabolism ; Ligands ; Oligopeptides/chemistry ; Oligopeptides/metabolism ; Plasmids/metabolism
Chemical Substances	Amines ; Chromatin ; Free Radicals ; Ligands ; Oligopeptides ; Guanine (5Z93L87A1R) ; DNA (9007-49-2)
Language	English
Publishing date	2012-03
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3065-x
ISSN	1362-3095 ; 0020-7616 ; 0955-3002
ISSN (online)	1362-3095
ISSN	0020-7616 ; 0955-3002
DOI	10.3109/09553002.2012.643853
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ue I Zs.280: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Identification of ebselen as a potent inhibitor of insulin degrading enzyme by a drug repurposing screening.

Leroux, Florence / Bosc, Damien / Beghyn, Terence / Hermant, Paul / Warenghem, Sandrine / Landry, Valérie / Pottiez, Virginie / Guillaume, Valentin / Charton, Julie / Herledan, Adrien / Urata, Sarah / Liang, Wenguang / Sheng, Li / Tang, Wei-Jen / Deprez, Benoit / Deprez-Poulain, Rebecca

European journal of medicinal chemistry

2019 Volume 179, Page(s) 557–566

Abstract: Insulin-degrading enzyme, IDE, is a metalloprotease implicated in the metabolism of key peptides such as insulin, glucagon, β-amyloid peptide. Recent studies have pointed out its broader role in the cell physiology. In order to identify new drug-like ... ...

Abstract	Insulin-degrading enzyme, IDE, is a metalloprotease implicated in the metabolism of key peptides such as insulin, glucagon, β-amyloid peptide. Recent studies have pointed out its broader role in the cell physiology. In order to identify new drug-like inhibitors of IDE with optimal pharmacokinetic properties to probe its multiple roles, we ran a high-throughput drug repurposing screening. Ebselen, cefmetazole and rabeprazole were identified as reversible inhibitors of IDE. Ebselen is the most potent inhibitor (IC
MeSH term(s)	Azoles/chemistry ; Azoles/pharmacology ; Biocatalysis ; Dose-Response Relationship, Drug ; Drug Evaluation, Preclinical ; Drug Repositioning ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; High-Throughput Screening Assays ; Humans ; Insulysin/antagonists & inhibitors ; Insulysin/metabolism ; Molecular Structure ; Organoselenium Compounds/chemistry ; Organoselenium Compounds/pharmacology ; Structure-Activity Relationship
Chemical Substances	Azoles ; Enzyme Inhibitors ; Organoselenium Compounds ; ebselen (40X2P7DPGH) ; Insulysin (EC 3.4.24.56)
Language	English
Publishing date	2019-06-24
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2019.06.057
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.B 784: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: An atlas of healthy and injured cell states and niches in the human kidney.

Lake, Blue B / Menon, Rajasree / Winfree, Seth / Hu, Qiwen / Melo Ferreira, Ricardo / Kalhor, Kian / Barwinska, Daria / Otto, Edgar A / Ferkowicz, Michael / Diep, Dinh / Plongthongkum, Nongluk / Knoten, Amanda / Urata, Sarah / Mariani, Laura H / Naik, Abhijit S / Eddy, Sean / Zhang, Bo / Wu, Yan / Salamon, Diane /

Williams, James C / Wang, Xin / Balderrama, Karol S / Hoover, Paul J / Murray, Evan / Marshall, Jamie L / Noel, Teia / Vijayan, Anitha / Hartman, Austin / Chen, Fei / Waikar, Sushrut S / Rosas, Sylvia E / Wilson, Francis P / Palevsky, Paul M / Kiryluk, Krzysztof / Sedor, John R / Toto, Robert D / Parikh, Chirag R / Kim, Eric H / Satija, Rahul / Greka, Anna / Macosko, Evan Z / Kharchenko, Peter V / Gaut, Joseph P / Hodgin, Jeffrey B / Eadon, Michael T / Dagher, Pierre C / El-Achkar, Tarek M / Zhang, Kun / Kretzler, Matthias / Jain, Sanjay

Nature

2023 Volume 619, Issue 7970, Page(s) 585–594

Abstract: Understanding kidney disease relies on defining the complexity of cell types and states, their associated molecular profiles and interactions within tissue ... ...

Abstract	Understanding kidney disease relies on defining the complexity of cell types and states, their associated molecular profiles and interactions within tissue neighbourhoods
MeSH term(s)	Humans ; Cell Nucleus/genetics ; Gene Expression Profiling ; Kidney/cytology ; Kidney/injuries ; Kidney/metabolism ; Kidney/pathology ; Kidney Diseases/metabolism ; Kidney Diseases/pathology ; Transcriptome/genetics ; Single-Cell Analysis ; Case-Control Studies ; Imaging, Three-Dimensional
Language	English
Publishing date	2023-07-19
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-05769-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Modeling the influence of histone proteins on the sensitivity of DNA to ionizing radiation.

Lee, Melissa / Urata, Sarah M / Aguilera, Joe A / Perry, Christopher C / Milligan, Jamie R

Radiation research

2011 Volume 177, Issue 2, Page(s) 152–163

Abstract: The DNA-binding proteins that are present in chromatin significantly affect the sensitivity of cells to ionizing radiation and to the radiation chemistry of DNA damage. The interaction between protein and DNA modifies the radiation chemistry of the ... ...

Abstract	The DNA-binding proteins that are present in chromatin significantly affect the sensitivity of cells to ionizing radiation and to the radiation chemistry of DNA damage. The interaction between protein and DNA modifies the radiation chemistry of the latter. To model these processes, we have examined the effects of ionizing radiation on the minichromosome form of SV40 (which contains histone proteins arranged in nucleosomes) and also on plasmid DNA in the presence of lysozyme. Although high concentrations of lysozyme can bring about an extensive radioprotection by condensation of the plasmid, at lower levels it still produces significant radioprotective effects under conditions where this associative phase separation does not take place. The presence of histones or of lysozyme decreases the yield of modified guanines produced by ionizing radiation. Comparison with previous observations made with oligopeptides suggests that the mechanism responsible is electron donation to guanyl radicals in the DNA by tryptophan and tyrosine residues in the proteins. However, there was no evidence for DNA-protein crosslink formation.
MeSH term(s)	Computer Simulation ; DNA/chemistry ; DNA/radiation effects ; DNA Damage ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/radiation effects ; Dose-Response Relationship, Radiation ; Histones/chemistry ; Histones/radiation effects ; Models, Chemical ; Muramidase/chemistry ; Muramidase/radiation effects ; Protein Binding/radiation effects ; Radiation Dosage ; Radiation Tolerance/radiation effects ; Radiation, Ionizing
Chemical Substances	DNA-Binding Proteins ; Histones ; DNA (9007-49-2) ; Muramidase (EC 3.2.1.17)
Language	English
Publishing date	2011-11-21
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	80322-4
ISSN	1938-5404 ; 0033-7587
ISSN (online)	1938-5404
ISSN	0033-7587
DOI	10.1667/rr2812.1
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ue I Zs.275: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito