Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.

scientific article published in August 2001

Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1046/J.1432-1327.2001.02347.X
P698PubMed publication ID11488924
P5875ResearchGate publication ID11854204

P2093author name stringE Leclerc
S W Vetter
P2860cites workEvidence for a phosphorylation-induced conformational change in phospholamban cytoplasmic domain by CD analysisQ67547161
Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairsQ68541267
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X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutantsQ71799416
Calmodulin modulates protein 4.1 binding to human erythrocyte membranesQ72496807
Secondary structure induction in aqueous vs membrane-like environmentsQ73665023
Function of WW domains as phosphoserine- or phosphothreonine-binding modulesQ22008803
Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteinsQ22253239
Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53Q27620615
The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanismsQ27628846
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Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structureQ27730268
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The structural basis for 14-3-3:phosphopeptide binding specificityQ29547190
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The effects of phosphorylation on the structure and function of proteinsQ40832954
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Serine/threonine phosphorylation of calmodulin modulates its interaction with the binding domains of target enzymesQ41839796
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Phosphorylation of calmodulin alters its potency as an activator of target enzymesQ48451320
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New clues to how proteins link up to run the cell.Q54192758
Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholine.Q54594737
Color test for detection of free terminal amino groups in the solid-phase synthesis of peptidesQ56390180
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P433issue15
P407language of work or nameEnglishQ1860
P921main subjectphosphorylationQ242736
P304page(s)4292-4299
P577publication date2001-08-01
P1433published inFEBS JournalQ1388041
P1476titlePhosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.
P478volume268

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cites work (P2860)
Q36913682Calcium in red blood cells-a perilous balance
Q22061744Dynamic α-helices: Conformations that do not conform
Q33558181Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor
Q27640451Structural basis for endothelial nitric oxide synthase binding to calmodulin
Q28776125The importance of intrinsic disorder for protein phosphorylation

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