Hormone binding globulins undergo serpin conformational change in inflammation.
about
Binding of retinoic acid by the inhibitory serpin protein C inhibitorStructural mechanism for the carriage and release of thyroxine in the blood.Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemiaPhysical mapping of four serpin genes: alpha 1-antitrypsin, alpha 1-antichymotrypsin, corticosteroid-binding globulin, and protein C inhibitor, within a 280-kb region on chromosome I4q32.1An overview of the serpin superfamilyScience review: mechanisms of impaired adrenal function in sepsis and molecular actions of glucocorticoidsThe role of glucocorticoid action in the pathophysiology of the Metabolic SyndromeThe Role of ACTH and Corticosteroids for Sepsis and Septic Shock: An UpdateInteractions causing the kinetic trap in serpin protein foldingStructure of native protein C inhibitor provides insight into its multiple functionsCorticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered releaseAllosteric Modulation of Hormone Release from Thyroxine and Corticosteroid-binding GlobulinsCorticosteroid-Binding Globulin: Structure-Function Implications from Species DifferencesHyporesponsiveness to glucocorticoids in mice genetically deficient for the corticosteroid binding globulinTowards engineering hormone-binding globulins as drug delivery agentsRegulation of DNA synthesis and the cell cycle in human prostate cancer cells and lymphocytes by ovine uterine serpin.Expression of biologically active human corticosteroid binding globulin by insect cells: acquisition of function requires glycosylation and transportMeasurement of tissue cortisol levels in patients with severe burns: a preliminary investigation.Serine Protease Inhibitors in Ticks: An Overview of Their Role in Tick Biology and Tick-Borne Pathogen Transmission.MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member.Pseudomonas aeruginosa elastase disrupts the cortisol-binding activity of corticosteroid-binding globulin.Regulation of protein function by native metastabilityMolecular basis for the properties of the thyroxine-binding globulin-slow variant in American blacks.S-glutathionylated serine proteinase inhibitors as plasma biomarkers in assessing response to redox-modulating drugsC1 inhibitor hinge region mutations produce dysfunction by different mechanisms.How changes in affinity of corticosteroid-binding globulin modulate free cortisol concentration.Association between chronic fatigue syndrome and the corticosteroid-binding globulin gene ALA SER224 polymorphism.Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick Ixodes ricinusModulation in Wistar rats of blood corticosterone compartmentation by sex and a cafeteria dietCorticosteroid-binding globulin gene polymorphisms: clinical implications and links to idiopathic chronic fatigue disorders.Evidence for estrogen-dependent uterine serpin (SERPINA14) expression during estrus in the bovine endometrial glandular epithelium and lumen.Functional implication of an Arg307Gly substitution in corticosteroid-binding globulin, a candidate gene for a quantitative trait locus associated with cortisol variability and obesity in pigTherapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.Clinical manifestations of highly prevalent corticosteroid-binding globulin mutations in a village in southern Italy.Structural insights into the unique inhibitory mechanism of the silkworm protease inhibitor serpin18.Exploration of the Hypothalamic-Pituitary-Adrenal Axis to Improve Animal Welfare by Means of Genetic Selection: Lessons from the South African MerinoThe genome of Strongyloides spp. gives insights into protein families with a putative role in nematode parasitism.Characterization and expression profiling of serine protease inhibitors in the diamondback moth, Plutella xylostella (Lepidoptera: Plutellidae).Non-invasive reproductive and stress endocrinology in amphibian conservation physiology.Proteolytic activation transforms heparin cofactor II into a host defense molecule
P2860
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P2860
Hormone binding globulins undergo serpin conformational change in inflammation.
description
1988 nî lūn-bûn
@nan
1988 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Hormone binding globulins undergo serpin conformational change in inflammation.
@ast
Hormone binding globulins undergo serpin conformational change in inflammation.
@en
Hormone binding globulins undergo serpin conformational change in inflammation.
@nl
type
label
Hormone binding globulins undergo serpin conformational change in inflammation.
@ast
Hormone binding globulins undergo serpin conformational change in inflammation.
@en
Hormone binding globulins undergo serpin conformational change in inflammation.
@nl
prefLabel
Hormone binding globulins undergo serpin conformational change in inflammation.
@ast
Hormone binding globulins undergo serpin conformational change in inflammation.
@en
Hormone binding globulins undergo serpin conformational change in inflammation.
@nl
P2093
P356
P1433
P1476
Hormone binding globulins undergo serpin conformational change in inflammation.
@en
P2093
Carrell RW
Pemberton PA
P2888
P304
P356
10.1038/336257A0
P407
P50
P577
1988-11-01T00:00:00Z
P6179
1006536711