about
Matrix metalloproteinase interactions with collagen and elastinBinding Isotherms and Time Courses Readily from Magnetic ResonanceNMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigensStructure of the UGAGAU hexaloop that braces Bacillus RNase P for actionStructural Basis for a Lethal Mutation in U6 RNA † , ‡Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplingsNMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphataseSolution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and TumorsIncreased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3.Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation.Path to Collagenolysis: COLLAGEN V TRIPLE-HELIX MODEL BOUND PRODUCTIVELY AND IN ENCOUNTERS BY MATRIX METALLOPROTEINASE-12.TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria.Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.Nuclear magnetic resonance captures the elusive.An examination of the proteolytic activity for bovine pregnancy-associated glycoproteins 2 and 12.Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.Entropy increases from different sources support the high-affinity binding of the N-terminal inhibitory domains of tissue inhibitors of metalloproteinases to the catalytic domains of matrix metalloproteinases-1 and -3.Phosphorylation in the catalytic cleft stabilizes and attracts domains of a phosphohexomutaseNoninvasive Recognition and Biomarkers of Early Allergic Asthma in Cats Using Multivariate Statistical Analysis of NMR Spectra of Exhaled Breath CondensateSolution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.Peripheral membrane associations of matrix metalloproteinases.Mechanistic insights into phosphoprotein-binding FHA domains.The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface.Multiple Ligand-Bound States of a Phosphohexomutase Revealed by Principal Component Analysis of NMR Peak Shifts.Transient collagen triple helix binding to a key metalloproteinase in invasion and development.Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.Breaking the covalent connection: Chain connectivity and the catalytic reaction of PMM/PGM.1H, 13C, and 15N peak assignments and secondary structure of human macrophage metalloelastase (MMP-12) in its inhibitor-free state.Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in ps to ns and micros to ms.Eukaryotic cyclophilin as a molecular switch for effector activation.Hsc70 contacts helix III of the J domain from polyomavirus T antigens: addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb.1H, 13C and 15N resonance assignments of the kinase-interacting FHA domain of Arabidopsis thaliana kinase-associated protein phosphatase.Phenotypic and genetic characterization of cytochrome c2 deficient mutants of Rhodobacter sphaeroidesFolding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in E. coliAssignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experimentsTissue inhibitor of metalloproteinases-1 undergoes microsecond to millisecond motions at sites of matrix metalloproteinase-induced fit1H, 13C and 15N resonance assignments and secondary structure of the N-terminal domain of human tissue inhibitor of metalloproteinases-1
P50
Q26996437-7FF47A38-2DA8-4788-8157-09A53B97FDA2Q27301803-C85916E5-2486-4172-99EB-6EAE3AA6B969Q27626634-A4DAD869-17E2-4906-AF52-69F5CA625F67Q27638693-6AF5391D-2557-4DDF-8A6F-DBE291520549Q27640473-DAF234AF-6A0A-4062-818F-CEEC89E96136Q27641535-D408DF2E-B125-4AB1-835B-7611C545A2E9Q27642196-51E1E40A-1089-4EE6-84C6-F9F87F819428Q27676714-2E27FDBA-72C8-435E-AE8F-7303718874B8Q28607761-80355AA2-0670-4E9E-BFFC-4A44B28100FFQ30164834-672317FA-740B-4A06-B8B2-EA6A52E1E0C0Q30504556-CB266F75-18AB-47FB-B215-E975CFC1AF71Q30739775-543975CA-1AF0-40F2-A965-22E09CB7B9D6Q32055899-F2971C63-6A48-4CCF-95F5-43BBA12CA237Q33581798-22630D9C-74A2-4942-9073-9CB5F2257FF2Q33777230-C243137A-3C11-4529-A60A-7F3E0AC68E4CQ34062354-D1D3DE7C-0C71-41BC-B8A3-CA45557D0118Q34265512-217BE8C8-FC45-4CC3-B312-53AF657C08F6Q34567081-98A551A4-4C51-495A-AE0C-EFB68981CDF4Q34947735-90D7D42C-178C-4853-AC06-E4601EE85092Q34996616-39A11F65-F8C4-4145-ACF6-BBD92236CD2DQ36169149-A0F8B9D9-88B3-45C8-A058-18B314CF40CAQ36279009-E94D0C45-CF3F-4915-8741-9A4DE2EB0C90Q36356192-8B542284-8904-4846-9D19-BE75BA222D0BQ37227501-C6F530A1-3AE7-41A9-9184-DDDCD8755A82Q37511686-FE67D6A1-87E1-4E99-B843-324398A1AFB0Q37525779-CDA7BA83-1FE6-4DFD-B7DC-101BA31CCA49Q41010274-4DB8232F-A297-412A-BD69-C0A74DCFB03BQ41480381-B4864AF5-58BE-4462-AFFF-57013AE5F3E5Q41877082-78BE9019-8C98-4F61-A0A2-FACD033BF9E7Q42739768-0F6EA14B-0592-40F0-943A-5BEB10EEDEA2Q42743136-F788DA59-69ED-4D7B-BFFC-86DD9CC01C0BQ44090252-C51CD01B-9B89-4281-89AF-3203C1A32E7DQ46595106-B9A4C4BD-FD9B-406F-898D-8687AE0BB13BQ50936384-336C6E4C-C528-43E1-BAC6-5B10A11BB07FQ52020013-4A14AD6D-2116-433F-AD84-209482FDFF2AQ69828827-86D99ECE-38E8-4CC4-9AEB-35FBF12DA0BEQ71034615-6544CF4C-17AA-4F2C-A38B-29ABF46B7A6DQ72609645-F407A09C-D6C9-4067-B5B3-6F94BB297FABQ74112953-2F8B223D-5D12-4F8D-91CE-912FD43FFB01Q78241512-F07470A2-B24A-4B3E-864E-31419D8C4D98
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Steven R Van Doren
@ast
Steven R Van Doren
@en
Steven R Van Doren
@es
Steven R Van Doren
@nl
Steven R Van Doren
@sl
type
label
Steven R Van Doren
@ast
Steven R Van Doren
@en
Steven R Van Doren
@es
Steven R Van Doren
@nl
Steven R Van Doren
@sl
prefLabel
Steven R Van Doren
@ast
Steven R Van Doren
@en
Steven R Van Doren
@es
Steven R Van Doren
@nl
Steven R Van Doren
@sl
P106
P1153
56017556500
P21
P31
P496
0000-0003-2838-4598