LIVIVO - Search results -

Search results

Result 1 - 10 of total 123

Search options

Article: Chemical and enzymatic oxidative coupling of 5-hydroxy-N,N-dimethyltryptamine with amines.

Babin, F / Huynh-Dinh, T

1987 Volume 30, Issue 7, Page(s) 1239–1241

Abstract: As part of a program aiming to obtain a covalent labeling of serotoninergic receptors we have studied the oxidative coupling of serotonin derivatives with amino compounds. The oxidation of bufotenine (2) by MnO2 and human ceruloplasmin followed by the ... ...

Abstract	As part of a program aiming to obtain a covalent labeling of serotoninergic receptors we have studied the oxidative coupling of serotonin derivatives with amino compounds. The oxidation of bufotenine (2) by MnO2 and human ceruloplasmin followed by the Michael type addition with dansylcadaverine and dansyllysine gave a fluorescent adduct identified as fused oxazole structure 4.
MeSH term(s)	Bufotenin ; Cadaverine/analogs & derivatives ; Ceruloplasmin/pharmacology ; Manganese/pharmacology ; Manganese Compounds ; Oxidation-Reduction ; Oxides ; Receptors, Serotonin/analysis ; Serotonin/analogs & derivatives
Chemical Substances	Manganese Compounds ; Oxides ; Receptors, Serotonin ; Bufotenin (0A31347TZK) ; Serotonin (333DO1RDJY) ; Manganese (42Z2K6ZL8P) ; Ceruloplasmin (EC 1.16.3.1) ; monodansylcadaverine (I9N81SC5HD) ; Cadaverine (L90BEN6OLL) ; manganese dioxide (TF219GU161)
Language	English
Publishing date	1987-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/jm00390a020
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 151: 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)
Zs.MB 1: Show issues

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: Structure of the d(CGCCCGCGGGCG) dodecamer: a kinked A-DNA molecule showing some B-DNA features.

Malinina, L / Fernandez, L G / Huynh-Dinh, T / Subirana, J A

Journal of molecular biology

1999 Volume 285, Issue 4, Page(s) 1679–1690

Abstract: We have determined the structure of the dodecamer duplex d(CGCCCGCGGGCG)2. A careful use of the molecular replacement programme AMoRe has been essential in order to solve the structure. This dodecamer shows a unique conformation, quite different from all ...

Abstract	We have determined the structure of the dodecamer duplex d(CGCCCGCGGGCG)2. A careful use of the molecular replacement programme AMoRe has been essential in order to solve the structure. This dodecamer shows a unique conformation, quite different from all the previously studied oligonucleotide duplexes: the central octamer has an A conformation, but with a sharp 65 degrees kink in the centre; the terminal base-steps have a B-like conformation; the major groove is completely closed in the centre, a hollow molecule is thus found. The results obtained confirm the high degree of variability of DNA structure. A new type of kink and an intermediate A/B double-helical conformation have been found. Such intermediate conformation differs from those described in DNA polymerase complexes.
MeSH term(s)	Base Pairing ; Base Sequence ; Crystallography, X-Ray ; DNA/chemistry ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry
Chemical Substances	Oligodeoxyribonucleotides ; DNA (9007-49-2)
Language	English
Publishing date	1999-01-29
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1006/jmbi.1998.2424
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 867: 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: The structure of the most studied DNA fragment changes under the influence of ions: a new packing of d(CGCGAATTCGCG).

Liu, J / Malinina, L / Huynh-Dinh, T / Subirana, J A

FEBS letters

1998 Volume 438, Issue 3, Page(s) 211–214

Abstract: The title oligonucleotide and many related dodecamers have been extensively studied alone and as DNA-drug complexes. In practically all cases they were found to crystallize in the same space group, stabilized by interactions among the terminal guanine ... ...

Abstract	The title oligonucleotide and many related dodecamers have been extensively studied alone and as DNA-drug complexes. In practically all cases they were found to crystallize in the same space group, stabilized by interactions among the terminal guanine bases. Here we report new packing interactions (R3) in the presence of Ca2+. The oligonucleotides interact by placing their terminal guanines in the narrow groove of a neighbor molecule, an interaction which had never been found in dodecamers.
MeSH term(s)	Base Sequence ; Binding Sites ; Calcium ; Crystallography, X-Ray ; DNA/chemistry ; Guanine ; Models, Molecular ; Oligodeoxyribonucleotides/chemistry ; Pharmaceutical Preparations
Chemical Substances	Oligodeoxyribonucleotides ; Pharmaceutical Preparations ; Guanine (5Z93L87A1R) ; DNA (9007-49-2) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1998-11-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/s0014-5793(98)01295-2
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 282: 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: Solution conformation of an RNA--DNA hybrid duplex containing a pyrimidine RNA strand and a purine DNA strand.

Hantz, E / Larue, V / Ladam, P / Le Moyec, L / Gouyette, C / Huynh Dinh, T

International journal of biological macromolecules

2001 Volume 28, Issue 4, Page(s) 273–284

Abstract: RNA--DNA hybrid duplexes are involved in transcription, replication and reverse transcription of nucleic acids. Information on such duplexes may shed some light on the mechanism of these processes. For this purpose, the influence of base composition on ... ...

Abstract	RNA--DNA hybrid duplexes are involved in transcription, replication and reverse transcription of nucleic acids. Information on such duplexes may shed some light on the mechanism of these processes. For this purpose, the influence of base composition on the structure of a polypyrimidine--polypurine RNA--DNA duplex r(cucuccuucucuu). d(GAGAGGAAGAGAA) has been studied using 1H, 31P and 13C NMR experiments, molecular modeling (JUMNA program) and NOE back-calculation methods. The resulting structure of the 13-mer hybrid duplex shows that the RNA strand is in the expected A-type conformation while the DNA strand is in a very flexible conformation. In the DNA strand, the desoxyribose sugars retain the C2'-endo B-type conformation. The duplex helical parameters (such as inclination, twist and displacement of the bases) are close to the A-type conformation. No bending was observed for the global axis curvature. The major groove width is close to the B-form value and the minor groove width is intermediate between standard values for A and B-forms. These results are in favour of the independence of minor groove size (where RNase H interacts) and the base composition of the hybrid duplexes.
MeSH term(s)	DNA/chemistry ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Nucleic Acid Conformation ; Nucleic Acid Heteroduplexes/chemistry ; Protons ; Purines/chemistry ; Pyrimidines/chemistry ; RNA/chemistry ; Solutions
Chemical Substances	Nucleic Acid Heteroduplexes ; Protons ; Purines ; Pyrimidines ; Solutions ; RNA (63231-63-0) ; DNA (9007-49-2) ; pyrimidine (K8CXK5Q32L) ; purine (W60KTZ3IZY)
Language	English
Publishing date	2001-08-03
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/s0141-8130(01)00123-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 2374: 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: Parallel and antiparallel GG.C base triplets in purpur.pyr triple helices formed with (GA) third strands.

Liquier, J / Geinguenaud, F / Huynh-Dinh, T / Gouyette, C / Khomyakova, E / Taillandier, E

Journal of biomolecular structure & dynamics

2001 Volume 19, Issue 3, Page(s) 527–534

Abstract: Triple helices with G*G.C and A*A.T base triplets with third GA strands either parallel or antiparallel with respect to the homologous duplex strand have been formed in presence of Na (+) or Mg(2+) counterions. Antiparallel triplexes are more stable and ... ...

Abstract	Triple helices with GG.C and AA.T base triplets with third GA strands either parallel or antiparallel with respect to the homologous duplex strand have been formed in presence of Na (+) or Mg(2+) counterions. Antiparallel triplexes are more stable and can be obtained even in presence of only monovalent Na(+) counterions. A biphasic melting has been observed, reflecting third strand separation around 20 degrees C followed by the duplex -> coil transition around 63 degrees C. Parallel triplexes are far less stable than the antiparallel ones. Their formation requires divalent ions and is observed at low temperature and in high concentration conditions. Different FTIR signatures of G*G.C triplets in parallel and antiparallel triple helices with GA rich third strands have been obtained allowing the identification of such base triplets in triplexes formed by nucleic acids with heterogeneous compositions. Only S-type sugars are found in the antiparallel triplex while some N-type sugar conformation is detected in the parallel triplex.
MeSH term(s)	Adenine/chemistry ; Base Sequence ; Carbohydrate Conformation ; Cations, Divalent ; Cytosine/chemistry ; DNA/chemistry ; Guanine/chemistry ; Magnesium/chemistry ; Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Oligonucleotides/chemistry ; Purines/chemistry ; Pyrimidines/chemistry ; Sodium/chemistry ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Temperature ; Trinucleotide Repeats
Chemical Substances	Cations, Divalent ; Oligonucleotides ; Purines ; Pyrimidines ; triplex DNA ; Guanine (5Z93L87A1R) ; Cytosine (8J337D1HZY) ; DNA (9007-49-2) ; Sodium (9NEZ333N27) ; Magnesium (I38ZP9992A) ; Adenine (JAC85A2161)
Language	English
Publishing date	2001-12
Publishing country	England
Document type	Journal Article
ZDB-ID	49157-3
ISSN	1538-0254 ; 0739-1102
ISSN (online)	1538-0254
ISSN	0739-1102
DOI	10.1080/07391102.2001.10506760
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2093: 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: Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.

Mousson, F / Beswick, V / Coïc, Y M / Huynh-Dinh, T / Sanson, A / Neumann, J M

FEBS letters

2001 Volume 505, Issue 3, Page(s) 431–435

Abstract: PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively charged. The conformational coupling between the transmembrane span and the cytoplasmic domain of PMP1 was investigated from 1H- ... ...

Abstract	PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively charged. The conformational coupling between the transmembrane span and the cytoplasmic domain of PMP1 was investigated from 1H-nuclear magnetic resonance data of two synthetic fragments: F9-F38, i.e. 80% of the whole sequence, and Y25-F38, the isolated cytoplasmic domain. Highly disordered in aqueous solution, the Y25-F38 peptide adopts a well-defined conformation in the presence of dodecylphosphocholine micelles. Compared with the long PMP1 fragment, this structure exhibits both native and non-native elements. Our results make it possible to assess the influence of a hydrophobic anchor on the intrinsic conformational propensity of a cytoplasmic domain.
MeSH term(s)	Amino Acid Sequence ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Micelles ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Proteolipids/chemistry ; Proteolipids/metabolism ; Protons
Chemical Substances	Membrane Proteins ; Micelles ; Proteolipids ; Protons
Language	English
Publishing date	2001-09-21
Publishing country	England
Document type	Journal Article
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/s0014-5793(01)02864-2
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 282: 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: Comparison between CUUG and UUCG tetraloops: thermodynamic stability and structural features analyzed by UV absorption and vibrational spectroscopy.

Baumruk, V / Gouyette, C / Huynh-Dinh, T / Sun, J S / Ghomi, M

Nucleic acids research

2001 Volume 29, Issue 19, Page(s) 4089–4096

Abstract: CUUG loop is one of the most frequently occurring tetraloops in bacterial 16S rRNA. This tetraloop has a high thermodynamic stability as proved by previous UV absorption and NMR experiments. Here, we present our results concerning the thermodynamic and ... ...

Abstract	CUUG loop is one of the most frequently occurring tetraloops in bacterial 16S rRNA. This tetraloop has a high thermodynamic stability as proved by previous UV absorption and NMR experiments. Here, we present our results concerning the thermodynamic and structural features of the 10mer 5'-r(GCG-CUUG-CGC)-3', forming a highly stable CUUG tetraloop hairpin in aqueous solution, by means of several optical techniques (UV and FT-IR absorption, Raman scattering). UV melting profile of this decamer provides a high melting temperature (60.7 degrees C). A set of Raman spectra recorded at different temperatures allowed us to analyze the order-to-disorder (hairpin-to-random coil) transition. Assignment of vibrational markers led us to confirm the particular nucleoside conformation, and to get information on the base stacking and base pairing in the hairpin structure. Moreover, comparison of the data obtained from two highly stable CUUG and UUCG tetraloops containing the same nucleotides but in a different order permitted an overall discussion of their structural features on the basis of Raman marker evidences.
MeSH term(s)	Nucleic Acid Conformation ; Nucleic Acid Denaturation ; RNA Stability ; RNA, Bacterial/chemistry ; RNA, Bacterial/metabolism ; RNA, Ribosomal, 16S/chemistry ; RNA, Ribosomal, 16S/metabolism ; Spectrophotometry, Ultraviolet ; Spectroscopy, Fourier Transform Infrared ; Spectrum Analysis, Raman/methods ; Thermodynamics
Chemical Substances	RNA, Bacterial ; RNA, Ribosomal, 16S
Language	English
Publishing date	2001-09-25
Publishing country	England
Document type	Comparative Study ; Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/29.19.4089
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1067: 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: Nickel-guanine interactions in DNA: crystal structure of nickel-d[CGTGTACACG]2.

Abrescia, Nicola A / Huynh-Dinh, Tam / Subirana, Juan A

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

2002 Volume 7, Issue 1-2, Page(s) 195–199

Abstract: The aim of this study was to clarify whether Ni2+ ions could bind to guanine bases in a standard B-DNA duplex and eventually induce a B-->Z transition. We have determined by X-ray crystallography at 3.1 A resolution the structure of the alternating ... ...

Abstract	The aim of this study was to clarify whether Ni2+ ions could bind to guanine bases in a standard B-DNA duplex and eventually induce a B-->Z transition. We have determined by X-ray crystallography at 3.1 A resolution the structure of the alternating deoxynucleotide d(CGTGTACACG), which contains both internal and terminal guanines. The duplex is in the B form. It is shown that nickel ions bind selectively to the N7 atom of guanine 10, which is in an extra-helical position, and guanine 2, which is in the terminal position of the duplex. It does not bind to guanine 4, which lies within a standard B-DNA tract. This simple but unambiguous result proves that nickel ions select between different guanines via steric accessibility. Guanine-Ni2+-guanine bridges among symmetry-related duplexes have also been found. These bridges may explain why Ni2+ ions may act either as a precipitant or a renaturing agent for DNA under certain conditions. The biochemical interaction of nickel with DNA can thus be related to its capacity to specifically bind to B-DNA regions with exposed guanines. Also, from the structural point of view, we have found a terminal cytosine, which forms a C.G:C reverse-Hoogsteen triple structure with a base pair of a neighbor duplex. This type of triplet is seldom found and is here described for the first time for a DNA structure.
MeSH term(s)	Crystallography, X-Ray/methods ; Cytosine/chemistry ; DNA/chemistry ; DNA/metabolism ; Guanine/chemistry ; Models, Molecular ; Nickel/chemistry ; Nucleic Acid Conformation ; Nucleic Acid Renaturation/physiology ; Oligodeoxyribonucleotides/chemical synthesis ; Oligodeoxyribonucleotides/chemistry
Chemical Substances	Oligodeoxyribonucleotides ; Guanine (5Z93L87A1R) ; Nickel (7OV03QG267) ; Cytosine (8J337D1HZY) ; DNA (9007-49-2)
Language	English
Publishing date	2002-01
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1464026-0
ISSN	1432-1327 ; 0949-8257
ISSN (online)	1432-1327
ISSN	0949-8257
DOI	10.1007/s007750100286
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article: PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study.

Roux, M / Beswick, V / Coïc, Y M / Huynh-Dinh, T / Sanson, A / Neumann, J M

Biophysical journal

2000 Volume 79, Issue 5, Page(s) 2624–2631

Abstract: PMP1 is a 38-residue plasma membrane protein of the yeast Saccharomyces cerevisiae that regulates the activity of the H(+)-ATPase. The cytoplasmic domain conformation results in a specific interfacial distribution of five basic side chains, thought to ... ...

Abstract	PMP1 is a 38-residue plasma membrane protein of the yeast Saccharomyces cerevisiae that regulates the activity of the H(+)-ATPase. The cytoplasmic domain conformation results in a specific interfacial distribution of five basic side chains, thought to strongly interact with anionic phospholipids. We have used the PMP1 18-38 fragment to carry out a deuterium nuclear magnetic resonance ((2)H-NMR) study for investigating the interactions between the PMP1 cytoplasmic domain and phosphatidylserines. For this purpose, mixed bilayers of 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphoserine (POPS) were used as model membranes (POPC/POPS 5:1, m/m). Spectra of headgroup- and chain-deuterated POPC and POPS phospholipids, POPC-d4, POPC-d31, POPS-d3, and POPS-d31, were recorded at different temperatures and for various concentrations of the PMP1 fragment. Data obtained from POPS deuterons revealed the formation of specific peptide-POPS complexes giving rise to a slow exchange between free and bound PS lipids, scarcely observed in solid-state NMR studies of lipid-peptide/protein interactions. The stoichiometry of the complex (8 POPS per peptide) was determined and its significance is discussed. The data obtained with headgroup-deuterated POPC were rationalized with a model that integrates the electrostatic perturbation induced by the cationic peptide on the negatively charged membrane interface, and a "spacer" effect due to the intercalation of POPS/PMP1f complexes between choline headgroups.
MeSH term(s)	Amino Acid Sequence ; Biophysical Phenomena ; Biophysics ; Deuterium ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Chemical ; Molecular Sequence Data ; Nerve Tissue Proteins ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Phosphatidylcholines/chemistry ; Phosphatidylcholines/metabolism ; Phosphatidylethanolamines/chemistry ; Phosphatidylethanolamines/metabolism ; Protein Binding ; Proteolipids/chemistry ; Proteolipids/metabolism ; Proton-Translocating ATPases ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins ; Static Electricity
Chemical Substances	Fungal Proteins ; Lipid Bilayers ; Macromolecular Substances ; Membrane Proteins ; Nerve Tissue Proteins ; PMP1 protein, S cerevisiae ; Peptide Fragments ; Phosphatidylcholines ; Phosphatidylethanolamines ; Proteolipids ; Saccharomyces cerevisiae Proteins ; 1-palmitoyl-2-oleoylphosphatidylethanolamine (10015-88-0) ; Deuterium (AR09D82C7G) ; Proton-Translocating ATPases (EC 3.6.3.14) ; 1-palmitoyl-2-oleoylphosphatidylcholine (TE895536Y5)
Language	English
Publishing date	2000-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/S0006-3495(00)76501-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

In stock of ZB MED Cologne/Königswinter

Zs.A 235: 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.MO 2: Show issues

Order via subito

Details ▾

Article ; Online: Targeting of Pu.Py Duplexes by GA and GT Rich Oligonucleotides on Microchip and in Solution.

Khomyakova, E / Liquier, J / Huynh-Dinh, T / Florentiev, V / Mirzabekov, A / Taillandier, E

Journal of biomolecular structure & dynamics

2000 Volume 17 Suppl 1, Page(s) 227–235

Abstract: Abstract Formation of triple helices with GA and GT third strands has been studied. Besides the usual investigation techniques common for characterizing triple helical formation (CD spectroscopy, gel shift mobility assay, chemical probing and S1 ... ...

Abstract	Abstract Formation of triple helices with GA and GT third strands has been studied. Besides the usual investigation techniques common for characterizing triple helical formation (CD spectroscopy, gel shift mobility assay, chemical probing and S1 nuclease footprinting) we have used a new technique in which targeting of polypurine sequences in duplexes was demonstrated on oligonucleotide microchips. This technique is very successful to quickly test a large number of potential triple helix formation. In this work we used oligonucleotide microairay to study the specificity of DNA duplex recognition by GA and GT strands. Generic 6-mer microchip containing all possible 4(6) = 4,096 single-stranded hexadeoxyribonucleotides immobilized within individual gel pads was applied. To study formation of intermolecular triple helices on the generic microchip, a number of Pu.Py duplexes were formed by hybridization of the mixture of purine octadeoxyribonucleotides on the microchip followed by targeting of the duplexes by GA or GT third strands. Melting behavior of the formed structures was investigated using fluorescence measurements under microscope. In solution we present the results obtained for GT triplexes and discuss the characteristics of the CD spectra. Results obtained by S1 nuclease footprinting, KMnO(4) and DMS chemical probing are consistent with the spectroscopic data reflecting triplex structure formation.
MeSH term(s)	Base Sequence ; DNA/chemistry ; Nucleic Acid Conformation ; Oligonucleotides
Chemical Substances	Oligonucleotides ; DNA (9007-49-2)
Language	English
Publishing date	2000
Publishing country	England
Document type	Journal Article
ZDB-ID	49157-3
ISSN	1538-0254 ; 0739-1102
ISSN (online)	1538-0254
ISSN	0739-1102
DOI	10.1080/07391102.2000.10506626
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2093: 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

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

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

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

Full text online

More links

Kategorien

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