Ligand binding modulates the mechanical stability of dihydrofolate reductase.
about
Exploring novel strategies for AIDS protozoal pathogens: α-helix mimetics targeting a key allosteric protein–protein interaction in C. hominis thymidylate synthase-dihydrofolate reductase (TS-DHFR)Enhanced degradation of dihydrofolate reductase through inhibition of NAD kinase by nicotinamide analogsNanomechanics of the cadherin ectodomain: "canalization" by Ca2+ binding results in a new mechanical element.A functional single-molecule binding assay via force spectroscopyLigand binding and circular permutation modify residue interaction network in DHFR.Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA.Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium.Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrinInhibitor binding increases the mechanical stability of staphylococcal nucleaseDependence of proteasome processing rate on substrate unfoldingCa2+ binding enhanced mechanical stability of an archaeal crystallin.A novel strategy for utilizing voice coil servoactuators in tensile tests of low volume protein hydrogels.Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilizationSingle-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability.Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Sequence- and species-dependence of proteasomal processivity.Mechanical biochemistry of proteins one molecule at a time.Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains.Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins.Conformational plasticity of the essential membrane-associated mannosyltransferase PimA from mycobacteria.Force spectroscopy studies on protein-ligand interactions: a single protein mechanics perspective.Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.Ligand-modulated parallel mechanical unfolding pathways of maltose-binding proteins.Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Force Spectroscopy of the Plasmodium falciparum Vaccine Candidate Circumsporozoite Protein Suggests a Mechanically Pliable Repeat Region.Single-molecule studies on PolySUMO proteins reveal their mechanical flexibilitySmall peptide binding stiffens the ubiquitin-like protein SUMO1.Secondary structure, mechanical stability, and location of transition state of proteinsFingerprinting DHFR in single-molecule AFM studies.The effect of protein complexation on the mechanical stability of Im9.Prying open single GroES ring complexes by force reveals cooperativity across domains.Tailoring protein nanomechanics with chemical reactivity.Enhancing the mechanical stability of proteins through a cocktail approach.Experimental measurement of binding energy, selectivity, and allostery using fluctuation theorems.Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Nicotinamide Phosphoribosyltransferase Deficiency Potentiates the Anti-proliferative Activity of Methotrexate through Enhanced Depletion of Intracellular ATP.Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.
P2860
Q27680861-FEA06838-54B2-47F7-9621-3364BA36DFD1Q28280315-F9A994F4-9F0A-449D-94AC-69A21EFEAAF5Q30427814-58703905-272B-49A9-A75A-7FEE94E932C3Q30496546-597BE0A5-3238-4872-BDA7-8FC95DDAC445Q33287881-33EDDE6F-93ED-4117-9879-C9006F4BA707Q34473855-422D6BEE-5AA8-4DB0-8226-2DCFC5E24AF1Q34504511-64F72CFC-F05A-4242-90C1-5DD3AA32CE90Q34557983-30E02185-57F1-4278-8745-437627E1CAC4Q34568116-479D1E88-0DF7-41A3-ABBE-11F9834ED402Q34978877-0F76AA62-E3FC-4381-999C-77E8D64D77C1Q35146699-C5E99EBB-C8C4-4BA0-ADFC-89381A04D6D2Q35569612-737148ED-B784-4251-967C-111BB112F67CQ35743849-3EAD1ADC-5D56-49D6-B33C-B15D43374976Q35839557-CFA71FF6-D722-429D-B069-5A6338047FE4Q35926219-A4F4972D-4A7B-4D7A-A7A8-DE120268B74BQ36177085-2BD11FA9-3933-4EAD-B41D-D37E9DBF5F12Q36740326-22480774-5BF4-4240-95F5-80E3C8C09E6EQ36783698-86FB3A85-8BBE-4092-AAED-9BA7BCA3C387Q36837541-9B20B82D-2311-4B38-82C5-B906445D7BB5Q37226219-C3D33C62-D30A-4090-A6A1-7EA87856805DQ38205675-7718692A-D015-4839-87C5-DA3A711409DBQ38334135-8980E166-9C07-4A0C-B8D3-BB0FD82654D5Q38334433-5B04D37B-FD1F-43BD-9D30-4B1F9E65E237Q38699291-6681A76C-BD4D-4ECF-A370-AD6B0E6EDC1DQ38777070-B125A6CC-865B-42D2-95FA-313AEF789CACQ40912791-75AAF3E8-51F7-48C5-AD0F-A1E30401CEEEQ41550756-02C80791-1B9F-4C81-8FB4-FC057016A330Q41678915-47C83101-FCB2-4735-ACE2-938193E26578Q41808561-E53B0AB6-CFD5-40EF-BA1F-99D7C9C58B9DQ41821044-06BCD447-1705-4B63-B59C-592A57E750EFQ42183206-1A29BB17-A3FF-498F-B774-28CA22E46284Q42208779-18021863-C6BC-49AE-AEE2-0929EDE4AA8FQ42712667-1E77D709-6402-40D8-B12F-6AAA1BAFCC93Q47994680-3C32DD28-98BF-4FE6-A299-104A4ED3A5BDQ48042718-32896C64-F4B2-44B4-B3CF-1535ECFD9D10Q50053714-514A5622-A6CC-4FD1-984B-72A99005887FQ54422222-24380E28-F25D-42D3-9374-60A7AFCA3525
P2860
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@ast
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@en
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@nl
type
label
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@ast
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@en
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@nl
prefLabel
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@ast
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@en
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
@nl
P2093
P2860
P1433
P1476
Ligand binding modulates the mechanical stability of dihydrofolate reductase
@en
P2093
Carmen L Badilla
Julio M Fernandez
P2860
P304
P356
10.1529/BIOPHYSJ.105.062034
P407
P577
2005-08-12T00:00:00Z