Altered protein folding may be the molecular basis of most cases of cystic fibrosis.

Altered protein folding may be the molecular basis of most cases of cystic fibrosis.

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http://www.wikidata.org/entity/Q35344873
Enhancing the Potency of F508del Correction: A Multi-Layer Combinational Approach to Drug Discovery for Cystic Fibrosis.The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.Lumacaftor and ivacaftor in the management of patients with cystic fibrosis: current evidence and future prospects.Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809.Side chain and backbone contributions of Phe508 to CFTR folding.A missense mutation in the sodium phosphate co-transporter Slc34a1 impairs phosphate homeostasis.On the design of broad based screening assays to identify potential pharmacological chaperones of protein misfolding diseasesBiosynthesis and trafficking of the bile salt export pump, BSEP: therapeutic implications of BSEP mutations.Combating cystic fibrosis: in search for CF transmembrane conductance regulator (CFTR) modulators.Effect of nanomolar concentrations of sodium dodecyl sulfate, a catalytic inductor of alpha-helices, on human calcitonin incorporation and channel formation in planar lipid membranes.Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATPIntroduction to section IV: biophysical methods to approach CFTR structure.Effects of lovastatin on trafficking of cystic fibrosis transmembrane conductance regulator in human tracheal epithelium.Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutanta and rescues wild-type caveolin-3.Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the golgi complex.Effect of calcium ions on human calcitonin. Possible implications for bone resorption by osteoclasts.Cellular processing of the amyloidogenic cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type
P2860

Altered protein folding may be the molecular basis of most cases of cystic fibrosis.

Item
http://www.wikidata.org/entity/Q35344873
description
1992 nî lūn-bûn
@nan
1992 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@ast
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@en
type
label
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@ast
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@en
prefLabel
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@ast
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
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P1433
P1476
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
@en
P2093
P2860
P304
P31
P356
10.1016/0014-5793(92)81399-7
P407
P433
P478
P577
P5875
P698
P921