about
Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme proteinThe RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundaryAssociation of a Novel ACTA1 Mutation With a Dominant Progressive Scapuloperoneal Myopathy in an Extended FamilyCrystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptorVimentin coil 1A-A molecular switch involved in the initiation of filament elongationThe Pentameric Channel of COMPcc in Complex with Different Fatty AcidsStructural elucidation of full-length nidogen and the laminin-nidogen complex in solutionStructural decoding of netrin-4 reveals a regulatory function towards mature basement membranesStructural insights into mutations of cystathionine beta-synthase.Biophysical analysis of a lethal laminin alpha-1 mutation reveals altered self-interaction.Biophysical Characterization of G-Quadruplex Recognition in the PITX1 mRNA by the Specificity Domain of the Helicase RHAU.Binding of G-quadruplexes to the N-terminal recognition domain of the RNA helicase associated with AU-rich element (RHAU).Recessive and dominant mutations in COL12A1 cause a novel EDS/myopathy overlap syndrome in humans and mice.RNA Helicase Associated with AU-rich Element (RHAU/DHX36) Interacts with the 3'-Tail of the Long Non-coding RNA BC200 (BCYRN1).Platinum (IV) coiled coil nanotubes selectively kill human glioblastoma cells.Collagen XXII binds to collagen-binding integrins via the novel motifs GLQGER and GFKGER.Inhibition of glycosylation on a camelid antibody uniquely affects its FcγRI binding activity.T-shaped arrangement of the recombinant agrin G3-IgG Fc protein.Dramatic and concerted conformational changes enable rhodocetin to block α2β1 integrin selectively.Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli.Correction: Dramatic and concerted conformational changes enable rhodocetin to block α2β1 integrin selectively.The many types of interhelical ionic interactions in coiled coils - an overview.Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements.Nanoscale Assembly of High-Mobility Group AT-Hook 2 Protein with DNA Replication Fork.Archaea S-layer nanotube from a "black smoker" in complex with cyclo-octasulfur (S8 ) rings.Impact of G-quadruplex loop conformation in the PITX1 mRNA on protein and small molecule interaction.Statistical analysis of intrahelical ionic interactions in alpha-helices and coiled coils.Interaction studies of a protein and carbohydrate system using an integrated approach: a case study of the miniagrin-heparin system.Structure and hydrodynamics of a DNA G-quadruplex with a cytosine bulge.QM and QM/MM studies of uranyl fluorides in the gas and aqueous phases and in the hydrophobic cavities of tetrabrachionEvidence for self-association of a miniaturized version of agrin from hydrodynamic and small-angle X-ray scattering measurements
P50
Q24291509-22F61C38-1307-4745-9D03-B4601027B048Q24301714-405763CE-EF6A-4F59-BE66-9DB9F701F590Q27345132-3210623B-B61A-4658-8455-75CF1A9E7A70Q27625317-2BA443E6-1FC5-4966-B560-853C09E41DC6Q27655410-656CB807-B657-42CA-9366-E7F2399629ECQ27675015-5A5AA2C8-0BAA-4C47-BD3F-73AFB8904A96Q28506868-909BE335-3893-4366-B9B2-AB586061D34AQ30831014-8C9840FC-BDE3-4AB6-AB8E-3B5FC53D9D07Q35103607-EEF6B95E-665F-451C-832A-475A00B89404Q35717335-9E2C094E-1D05-4AE8-A5FB-C9C2908F2F81Q35864127-DB1C599A-F004-4A17-AFEE-550633490B8FQ37368604-A07D722B-F2B1-4CAD-9FD3-602053373E60Q37685735-61FFE3A7-C3D4-4D31-9D79-84429D63F6A0Q38771426-0C540275-5984-4F6C-B930-42B6BA055090Q38909894-DAF9627A-222E-4574-AECB-D06DA24FE52AQ39034184-D41AEB5C-560F-47E3-9C66-F74C74110CC5Q39308046-627E5910-98F2-421D-98ED-135F1CF4502AQ39568467-76D82334-1FBD-453B-8D0E-3F4FF6908675Q41006227-AAE25E8B-1C36-44E4-910D-B70CF2E051CFQ42182765-C189E46E-AB56-48DB-9180-E42342B8F0DAQ42354759-A840495B-4A33-4226-ACB7-373AE4088DB8Q43544891-5A661934-54C4-4470-952C-E7CA158B0784Q45761839-FA1256CB-EBDB-412F-843A-B8FB1729FCDCQ47270675-5A3A9CC1-9869-482D-BAA3-E6A91B9D71A0Q47773583-871DB446-8666-48A4-B8C9-EFF812AC6A7DQ51056416-AEFA457E-DB6D-4CA0-BF78-CD8CE37E201AQ51936419-6A19C2F2-BD92-4C0D-BC0E-9E56ED7E7B35Q52358048-33D2361A-3793-498A-9DFA-8A695EDEBD57Q55383307-260CD540-F214-4174-8129-235C10F9B6CFQ83579567-C4391C13-47D3-4713-8FD0-8FE86EC8450EQ84805512-91E37D9B-0561-4878-8B38-A3ABB3270759
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Markus Meier
@ast
Markus Meier
@en
Markus Meier
@es
Markus Meier
@nl
Markus Meier
@sl
type
label
Markus Meier
@ast
Markus Meier
@en
Markus Meier
@es
Markus Meier
@nl
Markus Meier
@sl
prefLabel
Markus Meier
@ast
Markus Meier
@en
Markus Meier
@es
Markus Meier
@nl
Markus Meier
@sl
P106
P21
P31
P496
0000-0003-1068-746X