Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
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A screen for nigericin-resistant yeast mutants revealed genes controlling mitochondrial volume and mitochondrial cation homeostasis.TMalphaDB and TMbetaDB: web servers to study the structural role of sequence motifs in α-helix and β-barrel domains of membrane proteins.Ser/Thr motifs in transmembrane proteins: conservation patterns and effects on local protein structure and dynamicsHelix kinks are equally prevalent in soluble and membrane proteins.Identification of local variations within secondary structures of proteins.TMKink: a method to predict transmembrane helix kinks.Ion conduction and conformational flexibility of a bacterial voltage-gated sodium channel.hCB2 ligand-interaction landscape: cysteine residues critical to biarylpyrazole antagonist binding motif and receptor modulation.Elucidation of structural elements for selectivity across monoamine transporters: novel 2-[(diphenylmethyl)sulfinyl]acetamide (modafinil) analoguesNon-specific binding and general cross-reactivity of Y receptor agonists are correlated and should importantly depend on their acidic sectors.The role of Cysteine 6.47 in class A GPCRsMolecular dynamics and mutational analysis of a channelopathy mutation in the IIS6 helix of Ca V 1.2.In Vivo Analysis of Infectivity, Fusogenicity, and Incorporation of a Mutagenic Viral Glycoprotein Library Reveals Determinants for Virus IncorporationToward high-resolution prediction and design of transmembrane helical protein structuresSystematic Analysis and Prediction of In Situ Cross Talk of O-GlcNAcylation and Phosphorylation.Solving the membrane protein folding problem.Characterizing the Murine Leukemia Virus Envelope Glycoprotein Membrane-Spanning Domain for Its Roles in Interface Alignment and FusogenicityMultiple approaches converge on the structure of the integrin alphaIIb/beta3 transmembrane heterodimer.Pharmacological modulation of chemokine receptor function.Impact of helix irregularities on sequence alignment and homology modeling of G protein-coupled receptors.Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helixGPCR-SSFE 2.0-a fragment-based molecular modeling web tool for Class A G-protein coupled receptors.Different structural requirements for the constitutive and the agonist-induced activities of the beta2-adrenergic receptor.Structural and thermodynamic basis of proline-induced transmembrane complex stabilization.Conserved extracellular cysteine residues and cytoplasmic loop-loop interplay are required for functionality of the heptahelical MLO proteinTryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.Toward the three-dimensional structure and lysophosphatidic acid binding characteristics of the LPA(4)/p2y(9)/GPR23 receptor: a homology modeling study.Structure and function of yeast and fungal Na+ /H+ antiporters.Methods for the Development of In Silico GPCR Models.HELANAL-Plus: a web server for analysis of helix geometry in protein structures.Helix 8 of the viral chemokine receptor ORF74 directs chemokine binding.In Silico Veritas: The Pitfalls and Challenges of Predicting GPCR-Ligand InteractionsThe Approach of Conformational Chimeras to Model the Role of Proline-Containing Helices on GPCR Mobility: the Fertile Case of Cys-LTR1
P2860
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P2860
Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
@en
type
label
Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
@en
prefLabel
Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
@en
P2093
P2860
P1433
P1476
Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
@en
P2093
Cedric Govaerts
Juan Antonio Ballesteros
Mireia Olivella
Xavier Deupi
P2860
P304
P356
10.1016/S0006-3495(04)74088-6
P407
P433
P577
2004-01-01T00:00:00Z