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The three-dimensional structure of CsmA: a small antenna protein from the green sulfur bacterium Chlorobium tepidumA vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylationMutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilizationFast mapping of global protein folding states by multivariate NMR: a GPS for proteins.Incorporation of antimicrobial peptides into membranes: a combined liquid-state NMR and molecular dynamics study of alamethicin in DMPC/DHPC bicelles.Conformational flexibility of alpha-lactalbumin related to its membrane binding capacity.The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues.Phenylalanine hydroxylase misfolding and pharmacological chaperones.Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp.Linking genotypes database with locus-specific database and genotype-phenotype correlation in phenylketonuriaPharmacological Chaperoning: A Potential Treatment for PMM2-CDG.Pharmacological chaperones as a potential therapeutic option in methylmalonic aciduria cblB type.Pharmacological Chaperones that Protect Tetrahydrobiopterin Dependent Aromatic Amino Acid Hydroxylases Through Different Mechanisms.In situ solid-state NMR spectroscopy of protein in heterogeneous membranes: the baseplate antenna complex of Chlorobaculum tepidum.Screening and evaluation of small organic molecules as ClpB inhibitors and potential antimicrobials.Erratum to "Discovery of compounds that protect tyrosine hydroxylase activity through different mechanisms" [Biochim. Biophys. Acta 1854/9 (2015) 1078-1089].Discovery of compounds that protect tyrosine hydroxylase activity through different mechanisms.The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy.Discovery of a Specific Inhibitor of Pyomelanin Synthesis in Legionella pneumophilaSDS-Facilitated In vitro Formation of a Transmembrane B-Type Cytochrome Is Mediated by Changes in Local pHNMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding regionThe Arabidopsis (ASHH2) CW domain binds monomethylated K4 of the histone H3 tail through conformational selectionQuantification of Polyphenols in Seaweeds: A Case Study of Ulva intestinalisAnionic hafnium species: an active catalytic intermediate for the coupling of epoxides with CO2?
P50
Q27651324-E1AB3938-53CE-4D2D-8137-603A695FE585Q27678995-785DDBDD-4A7F-4847-8F02-3852110E6030Q27680374-C9099E7C-CFDE-433C-9DB7-4A8929431ADEQ30981802-A000F12C-C440-4A20-8916-DFB86211B62BQ33430435-2DB8EBA6-9551-402B-9635-F455937A77D8Q34421039-F38B4955-2E45-4FED-AA31-029EE40897D4Q34493802-C477EEA6-6020-42FB-B3A2-FC437E485B08Q34556955-CCC9E9A4-58F7-4BCF-8169-DB9ADDF4F808Q34568257-D25603BF-6F43-4AC4-9AE2-6FA2D336865FQ35079956-AD5611F0-D9BC-4FC3-9D2A-4A32499AF15FQ36172720-2F0EEB47-2D74-4CC7-97C3-497F57545D71Q37111958-209EB26D-F934-4AF7-9AB2-85CC762C81A5Q38764990-C0CC554B-9FCC-4A31-8335-2252333D7227Q47640191-6C74C00B-2398-40AD-B5A4-1F924642A172Q47739500-87C396AC-ABF7-4D9E-8BEA-2D571933C1DFQ50129112-D8248425-E41B-4389-9345-2DA474BFB23AQ50445869-8D8225E8-6664-42CA-BCA7-829032385630Q50542090-FC22063B-2652-44A2-A220-9C4A43455682Q57235348-B54901AA-5B0D-418B-9D2F-D2468D26A0D1Q57823070-82886C6A-8474-45D1-8490-E610D5CFB919Q80099176-1E87216E-01A7-49F7-B277-DFFD9740B610Q89829029-B996E5FD-71F8-4880-B095-EA2792233FF0Q91807787-9411E226-0A79-42C5-A7DC-11FB1BA62B26Q92532398-398E7B87-C866-49A6-8817-CA2D6FA58DCB
P50
description
Noors onderzoeker
@nl
researcher, ORCID id # 0000-0003-0346-3986
@en
name
Jarl Underhaug
@ast
Jarl Underhaug
@en
Jarl Underhaug
@es
Jarl Underhaug
@nl
Jarl Underhaug
@sl
type
label
Jarl Underhaug
@ast
Jarl Underhaug
@en
Jarl Underhaug
@es
Jarl Underhaug
@nl
Jarl Underhaug
@sl
prefLabel
Jarl Underhaug
@ast
Jarl Underhaug
@en
Jarl Underhaug
@es
Jarl Underhaug
@nl
Jarl Underhaug
@sl
P106
P21
P27
P31
P496
0000-0003-0346-3986