نتائج البحث

Molecular dynamics simulation of the opposite-base preference and interactions in the active site of formamidopyrimidine-DNA glycosylase.

• Authors : Popov AV; SB RAS Institute of Chemical Biology and Fundamental Medicine, 8 Lavrentieva Ave., Novosibirsk, 630090, Russia.; Endutkin AV

Subjects: Molecular Dynamics Simulation*; DNA/DNA/DNA/*metabolism ; DNA-Formamidopyrimidine Glycosylase/DNA-Formamidopyrimidine Glycosylase/DNA-Formamidopyrimidine Glycosylase/*chemistry

• Source: BMC structural biology [BMC Struct Biol] 2017 May 08; Vol. 17 (1), pp. 5. Date of Electronic Publication: 2017 May 08.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان

Disturbance of DNA conformation by the binding of testosterone-based platinum drugs via groove-face and intercalative interactions: a molecular dynamics simulation study.

• Authors : Cui S; Key Laboratory of Theoretical and Computational Photochemistry of Ministry of Education, College of Chemistry, Beijing Normal University, Beijing 100875, PR China.; Wang Y

Subjects: Molecular Dynamics Simulation*; DNA/DNA/DNA/*metabolism ; Intercalating Agents/Intercalating Agents/Intercalating Agents/*metabolism

• Source: BMC structural biology [BMC Struct Biol] 2013 Mar 22; Vol. 13, pp. 4. Date of Electronic Publication: 2013 Mar 22.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان

A mutational analysis and molecular dynamics simulation of quinolone resistance proteins QnrA1 and QnrC from Proteus mirabilis

• Authors : Xiaogang Xu; Qinglan Guo; Minghua Wang

Subjects: Models, Molecular; 0301 basic medicine; Base Sequence

• Source: BMC Struct Biol

تفاصيل العنوان

Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between 'open' and 'closed' conformations and suggests specific for eEF1A1 affinity for Ca2+-calmodulin

• Authors : Dmitry S. Kanibolotsky; Catherine M. Abbott; Oleksandra V. Novosylna

Subjects: Models, Molecular; 0303 health sciences; Binding Sites

• Source: BMC Struct BiolKanibolotsky, D S, Novosyl'na, O V, Abbott, C M, Negrutskii, B S & El'skaya, A V 2008, ' Multiple molecular dynamics

تفاصيل العنوان

Molecular dynamics simulation of human LOX-1 provides anexplanation for the lack of OxLDL binding to the Trp150Ala mutant.

• Authors : Falconi, Mattia¹ ; Biocca, Silvia² ; Novelli, Giuseppe³

• Source: BMC Structural Biology. 2007, Vol. 7, p73-83. 11p.

تفاصيل العنوان

Destabilization of the TWIST1/E12 complex dimerization following the R154P point-mutation of TWIST1: an in silico approach.

• Authors : Bouard C; Inserm UMR-S1052, Centre de Recherche en Cancérologie de Lyon, Lyon, 69373, France.; CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, Lyon, 69373, France.

Subjects: Molecular Dynamics Simulation* ; Point Mutation*; Nuclear Proteins/Nuclear Proteins/Nuclear Proteins/*chemistry

• Source: BMC structural biology [BMC Struct Biol] 2017 May 18; Vol. 17 (1), pp. 6. Date of Electronic Publication: 2017 May 18.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان

Localization of putative binding sites for cyclic guanosine monophosphate and the anti-cancer drug 5-fluoro-2'-deoxyuridine-5'-monophosphate on ABCC11 in silico models.

• Authors : Honorat M; INSERM, UMR-S1052, Centre de Recherche en Cancérologie de Lyon, Lyon F-69008, France.; Terreux R

Subjects: Molecular Dynamics Simulation*; ATP-Binding Cassette Transporters/ATP-Binding Cassette Transporters/ATP-Binding Cassette Transporters/*metabolism ; Antineoplastic Agents/Antineoplastic Agents/Antineoplastic Agents/*metabolism

• Source: BMC structural biology [BMC Struct Biol] 2013 May 06; Vol. 13, pp. 7. Date of Electronic Publication: 2013 May 06.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان

Modeling holo-ACP:DH and holo-ACP:KR complexes of modular polyketide synthases: a docking and molecular dynamics study.

• Authors : Anand S; Bioinformatics Center, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.; Mohanty D

Subjects: Molecular Docking Simulation* ; Molecular Dynamics Simulation*; Acyl Carrier Protein/Acyl Carrier Protein/Acyl Carrier Protein/*chemistry

• Source: BMC structural biology [BMC Struct Biol] 2012 May 28; Vol. 12, pp. 10. Date of Electronic Publication: 2012 May 28.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان

The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulations.

• Authors : Duclert-Savatier N; Institut Pasteur, CNRS URA 2185, Unité de Bioinformatique Structurale, 25-28 rue du Dr Roux, F-75724 Paris Cedex 15, France.; Martínez L

Subjects: Molecular Dynamics Simulation* ; Nuclear Magnetic Resonance, Biomolecular* ; Protein Unfolding*

• Source: BMC structural biology [BMC Struct Biol] 2011 Nov 24; Vol. 11, pp. 46. Date of Electronic Publication: 2011 Nov 24.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان

Hydration studies on the archaeal protein Sso7d using NMR measurements and MD simulations.

• Authors : Bernini A; Dipartimento di Biotecnologie, Università degli Studi di Siena, via Fiorentina 1, Siena, Italy.; Spiga O

Subjects: Molecular Dynamics Simulation*; Archaeal Proteins/Archaeal Proteins/Archaeal Proteins/*chemistry ; DNA-Binding Proteins/DNA-Binding Proteins/DNA-Binding Proteins/*chemistry

• Source: BMC structural biology [BMC Struct Biol] 2011 Oct 21; Vol. 11, pp. 44. Date of Electronic Publication: 2011 Oct 21.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

تفاصيل العنوان