A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations - Wikidata - awgldk - TriplyDB

A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

http://www.wikidata.org/entity/Q29547632

about

A kinetic model of trp-cage folding from multiple biased molecular dynamics simulations Evaluating the effects of cutoffs and treatment of long-range electrostatics in protein folding simulations A systematic framework for molecular dynamics simulations of protein post-translational modifications Mechanistic and structural insight into the functional dichotomy between IL-2 and IL-15 Unfolded-state dynamics and structure of protein L characterized by simulation and experiment SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease Molecular basis of reduced glucosylceramidase activity in the most common Gaucher disease mutant, N370S Further evidence for the likely completeness of the library of solved single domain protein structures Exploiting a natural conformational switch to engineer an interleukin-2 'superkine'A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease Discovery of small-molecule HIV-1 fusion and integrase inhibitors oleuropein and hydroxytyrosol: Part I. fusion [corrected] inhibition The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site Binding modes of CCR5-targetting HIV entry inhibitors: partial and full antagonists Structure and energy of a DNA dodecamer under tensile load A new anti conformation for N-(deoxyguanosin-8-yl)-2-acetylaminofluorene (AAF-dG) allows Watson-Crick pairing in the Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4).Computational analysis and prediction of the binding motif and protein interacting partners of the Abl SH3 domain.Local order in the unfolded state: conformational biases and nearest neighbor interactions SwissParam: A fast force field generation tool for small organic molecules Identification of Chalcones as Fasciola hepatica Cathepsin L Inhibitors Using a Comprehensive Experimental and Computational Approach Structure, dynamics, and interaction of Mycobacterium tuberculosis (Mtb) DprE1 and DprE2 examined by molecular modeling, simulation, and electrostatic studies Discovery of the elusive leptin in birds: identification of several 'missing links' in the evolution of leptin and its receptor Folding and Stabilization of Native-Sequence-Reversed Proteins.Dynamic Allostery of the Catabolite Activator Protein Revealed by Interatomic Forces Minimum free energy path of ligand-induced transition in adenylate kinase Conformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulations Molecular dynamics simulations of forced unbending of integrin α(v)β₃ Exploring the universe of protein structures beyond the Protein Data Bank Detection of functional modes in protein dynamics Non-Specific Blocking of miR-17-5p Guide Strand in Triple Negative Breast Cancer Cells by Amplifying Passenger Strand Activity Alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant GAGA-factors in the nucleus and nucleolus A novel, highly selective inhibitor of pestivirus replication that targets the viral RNA-dependent RNA polymerase.Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein Structural Insights into SraP-Mediated Staphylococcus aureus Adhesion to Host Cells Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1 Structural basis for the sequence-specific RNA-recognition mechanism of human CUG-BP1 RRM3 Structural and Thermodynamic Basis for Enhanced DNA Binding by a Promiscuous Mutant EcoRI Endonuclease Electrostatic contributions drive the interaction betweenStaphylococcus aureusprotein Efb-C and its complement target C3d Structure of L-Xylulose-5-Phosphate 3-Epimerase (UlaE) from the Anaerobic L-Ascorbate Utilization Pathway of Escherichia coli: Identification of a Novel Phosphate Binding Motif within a TIM Barrel Fold

P2860

Q21092563-90635595-3DEE-4A48-8A82-F3AC76065E6D Q21134160-642790FA-894E-471A-9074-C845235A2713 Q21145303-C9B9BCCB-8DCF-43A6-BDB1-C8A10C664507 Q24301975-8C979A65-20E9-4B67-B995-AD95C9613796 Q24596398-54F3636C-AE60-41F5-BF64-24A861C64F39 Q24611702-2D2323E0-1454-4040-BBDE-AC6CCE03CBAD Q24615365-F56A301A-2E10-4367-A7DF-CB8EEFFC74D1 Q24621867-8B2CDBAD-40B4-4DF2-A4FD-11137EDF7BFD Q24621878-C2D0C8D5-8C05-4911-A387-72264D502DCC Q24632192-EDA49DFF-0EED-41BC-A204-14ADE4DF3EC2 Q24633417-493DB777-56A9-4E14-8685-6F76EBB609BF Q24644512-1E545218-7C70-436B-99E8-926CE35AA29F Q24650711-2950C6A2-C4F0-4DD1-A4EA-98EDD30808DA Q24655859-AEDAAF67-DDE6-4413-84A7-0D6115477253 Q24658283-D852DCBB-24F6-4CC7-A684-324E18243409 Q24812957-127E9248-EF05-46B6-AB58-70FD51BCC656 Q25257140-A5301878-9F75-4E9F-B160-9A0A462AEAAD Q25257719-E3D5EEDD-BD18-41D8-986B-817A743F903F Q26851842-3D549336-6898-4FA6-82BE-B889D1C7C70F Q27136894-1B51ED1D-4C80-4004-AA1A-E64B26278D47 Q27303614-719D9E4F-F151-46B8-B6D2-7A6DDCAB8242 Q27311652-B4DDDF79-E0A0-4268-9704-A361A5E7C4BB Q27313624-5E7D0BE5-5B49-4BC9-ADFB-F7BDB41D7094 Q27318306-5C8AD801-75E9-4D45-881B-C7EF0BFE6421 Q27318433-70FE53F5-2888-43BB-B4BB-7366549F5DBA Q27330358-A0533952-32C8-47A9-B904-BAE7067B4D6D Q27333790-206F3589-6CF2-423B-BFD7-598B07377EE7 Q27334036-32098D9E-36F9-4AFF-8005-0D7644B173AA Q27334418-55AA83F1-F6D7-4255-B6C5-CE536452C725 Q27335384-C46C6609-7E93-4C54-B485-F2F3D5B175F8 Q27345210-606F1869-B963-47CA-9FFB-B0BD3DB683FF Q27437831-469E21FC-4F54-43F7-ABDC-568D368FB401 Q27472778-69B59C19-95A7-46DA-A312-E9C3D8D44C38 Q27644304-51D72EBE-0ED5-4845-A819-37F4C74D0E4A Q27644575-C57834F3-61AB-4680-940B-014EDBB2AC40 Q27644587-5951A68C-B3D7-422F-9091-9A678B741945 Q27646264-6B492D32-22E0-4812-B636-2B307735B41C Q27649010-A110686A-BCCD-4A96-8A50-301793FF001F Q27651460-C870C4F5-675F-4474-8AB5-FEDE3681D055 Q27652487-D3CA9925-C7A2-46B8-81B7-61ABCC0535C4

P2860

A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

http://www.wikidata.org/entity/Q29547632

description

2003 nî lūn-bûn

@nan

2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

A point-charge force field for ...... uantum mechanical calculations

@ast

A point-charge force field for ...... uantum mechanical calculations

@en

type

label

A point-charge force field for ...... uantum mechanical calculations

@ast

A point-charge force field for ...... uantum mechanical calculations

@en

prefLabel

A point-charge force field for ...... uantum mechanical calculations

@ast

A point-charge force field for ...... uantum mechanical calculations

@en

P1433

Q29547632-E2DDFA12-0E02-4086-95A9-3F7399496E33

P1476

Q29547632-423E45B7-6A0A-49FE-97D2-312023C69926

P2093

Q29547632-0D72D3B8-E050-43F3-B4C9-0D829E7E4917

Q29547632-1E07F918-BA05-48CC-9022-0EB6F7977477

Q29547632-1E59FE2F-DF22-4AE2-8268-0EF4DFAAB151

Q29547632-4AED2FDE-6E9F-4BDC-AB36-718A2CFF7422

Q29547632-870CFDA0-40FC-4DFF-A8AA-22DB66A7E6DE

Q29547632-A75422AB-245D-43CA-A41D-AC21FC30FC99

Q29547632-C0B42E59-3C5B-4429-80D5-50C368820FF0

Q29547632-D3CC9120-B3A3-42F6-A2EF-B2C97FE50AB8

Q29547632-F3E80F13-D88B-42F8-841A-F8007B0D2D56

Q29547632-FA31CAF0-1445-4BC5-878B-759916A87CE5

P304

Q29547632-7DD07190-C7B1-4A48-AAB4-64CA5D0057D1

P31

Q29547632-192DCFF8-907D-481A-A5A0-78F60C584E07

P3181

Q29547632-569A74BA-D6A9-464C-AD3A-443A27022E56

P356

Q29547632-26942DFF-FF30-4A28-88A7-050EE5F85012

P407

Q29547632-DE8BFB4F-37E5-4CE8-9E9F-52F0CF93BD02

P433

Q29547632-49B1B244-C6BB-42E1-8C78-E72D4B2C7981

P478

Q29547632-AF138D47-57E7-4B98-AB09-C5EAAC9BE921

P50

Q29547632-D2B00900-F98A-47FC-A1D5-5493F4283F9E

Q29547632-DB6CE8B5-ADB0-4831-BD18-72637BC5EE78

Q29547632-DE693968-1BC5-4795-8E4D-0661ECC0C9D6

P577

Q29547632-DEE6C0AD-E32F-4268-B11D-B0ED7B510924

P5875

Q29547632-5DBDE4D4-729E-4FE5-B6AF-2CCF4741E33D

P698

Q29547632-8E6C5A36-A841-4149-B599-A745510AAAEF

P3181

P356

P1433

Journal of Computational Chemistry

P1476

A point-charge force field for ...... uantum mechanical calculations

@en

P2093

Guoming Xiong

http://www.w3.org/2001/XMLSchema#string

James Caldwell

http://www.w3.org/2001/XMLSchema#string

Mathew C Lee

http://www.w3.org/2001/XMLSchema#string

Peter Kollman

http://www.w3.org/2001/XMLSchema#string

Piotr Cieplak

http://www.w3.org/2001/XMLSchema#string

Rong Yang

http://www.w3.org/2001/XMLSchema#string

Shibasish Chowdhury

http://www.w3.org/2001/XMLSchema#string

Taisung Lee

http://www.w3.org/2001/XMLSchema#string

Wei Zhang

http://www.w3.org/2001/XMLSchema#string

Yong Duan

http://www.w3.org/2001/XMLSchema#string

P304

1999-2012

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

210070

http://www.w3.org/2001/XMLSchema#string

P356

10.1002/JCC.10349

http://www.w3.org/2001/XMLSchema#string

P407

P433

16

http://www.w3.org/2001/XMLSchema#string

P478

24

http://www.w3.org/2001/XMLSchema#string

P50

P577

2003-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

9061783

http://www.w3.org/2001/XMLSchema#string

P698

14531054

http://www.w3.org/2001/XMLSchema#string