Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis.
about
Protein folding and quality control in the ERProtein homeostasis as a therapeutic target for diseases of protein conformationChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyNew therapeutic approaches for Krabbe disease: The potential of pharmacological chaperonesConformational analysis of misfolded protein aggregation by FRET and live-cell imaging techniquesN-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CyclePrion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress.Using pharmacological chaperones to restore proteostasisIdentification and functional clustering of genes regulating muscle protein degradation from amongst the known C. elegans muscle mutants.Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.Therapeutic approaches for lysosomal storage diseasesSmall molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise.The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments.Remodeling the proteostasis network to rescue glucocerebrosidase variants by inhibiting ER-associated degradation and enhancing ER folding.Measuring steady-state and dynamic endoplasmic reticulum and Golgi Zn2+ with genetically encoded sensors.Endoplasmic reticulum Ca(2+) handling in excitable cells in health and diseaseNematotoxicity of Marasmius oreades agglutinin (MOA) depends on glycolipid binding and cysteine protease activity.Defects in calcium homeostasis and mitochondria can be reversed in Pompe disease.Ryanodine receptor antagonists adapt NPC1 proteostasis to ameliorate lipid storage in Niemann-Pick type C disease fibroblastsN-glycosylation of enhanced aromatic sequons to increase glycoprotein stabilityResurrecting the protein fold for disease interventionPharmacological small molecules for the treatment of lysosomal storage disorders.Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseasesThe pathophysiology of GD - current understanding and rationale for existing and emerging therapeutic approaches.Endoplasmic-reticulum calcium depletion and disease.Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.Gaucher disease paradigm: from ERAD to comorbidity.Targeting endoplasmic reticulum stress in metabolic disease.Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases.Endoplasmic reticulum and lysosomal Ca²⁺ stores are remodelled in GBA1-linked Parkinson disease patient fibroblasts.New Directions in Gaucher Disease.FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts.Modulating ryanodine receptors with dantrolene attenuates neuronopathic phenotype in Gaucher disease mice.Regulating Secretory Proteostasis through the Unfolded Protein Response: From Function to Therapy.Chemical chaperones assist intracellular folding to buffer mutational variations.Connecting Ca2+ and lysosomes to Parkinson disease.Endoplasmic Reticulum Malfunction in the Nervous System.ERdj3 is an endoplasmic reticulum degradation factor for mutant glucocerebrosidase variants linked to Gaucher's disease.
P2860
Q26823157-A7C5CAFF-7081-4A2D-8F65-FB8225024159Q27003283-8DD03FE1-AECE-4966-AE7C-9E343AA96208Q27004511-F695F0FF-780A-4529-ABAA-244F748B5F51Q27015793-03132B23-0B20-4779-816A-7EB1340FC6E3Q28068142-014B6112-8218-4BE1-97DC-B8BBE485B0F2Q28083085-DA91669A-1265-4D8E-A492-82A96E15A82DQ28085581-D1240B4C-1ADB-4685-8C4E-67DD0B748159Q33786940-BEBE7D59-E804-48DD-B4B1-59287128ACBEQ33804655-CF76E864-1C28-42EF-8D48-81871DE645F8Q34042815-398DEB67-B5F2-42CC-84E6-E74E997F0F67Q34249680-8877BD7E-972B-48C2-9EC8-0DE176D71AD7Q34311420-B6FA1C62-9CCA-4A0E-A023-D5B01E7C782CQ34338604-B973BC4D-8532-40D9-B566-E20AB440AA51Q34512555-1DE30336-3061-40AA-B1C9-2CE8D7218A8EQ34684657-66F97654-8BC9-4D34-A1C1-05D525681075Q34688803-E538CE6F-1A38-4B0F-A92C-F74EBBB2D609Q34938458-9E055AE9-C651-4FC8-941C-40083277DC11Q35122788-52E9C835-B9DB-48B7-94D7-903CE3C84F5CQ35182822-712320FB-1B89-4438-9AF9-88717B445DCEQ35853122-DBBDA5A9-EA29-485F-8922-9230E7A86902Q36062024-9A7026A6-F759-4E06-B7BA-2E3F8A16AB7AQ36515262-5D432593-6D68-4C25-B6D0-392852ADF3CCQ36857284-06418193-6EED-49EF-BCC1-52AA921BCEDBQ37799818-FCA2F571-4B40-46B1-9AD1-31C7F7205840Q37819121-990CC542-0BF6-4373-8322-B07705EAC8E8Q37827416-F6FFA168-E52C-46FA-A192-B4ACDBDB5589Q37858336-EDA2E2D1-791D-42CA-AAD2-B9CA4DBE4ACDQ37987587-E4F47517-FB2E-446A-BC09-98F7D427D526Q38012690-27C208C4-53BB-43D5-98E6-58F6406D1DF1Q38074493-23972ECA-474B-437D-B843-E0FDE032DEA5Q38195215-3061E344-7FDB-4C67-A629-0B2C1E4DE882Q38389995-B243D86D-3B74-4B58-BBED-96F6F3FD891DQ38905996-2BEFEE3D-9623-44C7-8AF7-5F5FEB4C5C56Q39190061-ADAB0714-FD30-47F6-A39D-5675D098285BQ39364713-65A33E65-50B1-441B-A8A5-70FE901D76E2Q39396098-3222542D-BFC7-4484-9F66-45D39E811EA1Q41971592-5C6433AD-591E-4974-95BF-9434A117C8DEQ42255446-37BDE92D-586C-4D6A-8E77-9803C2010EB5Q42290598-B50E0BB7-6238-4952-B9BB-677B596FE008Q42801910-26240E18-66A3-4A60-9312-2600909EFC91
P2860
Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis.
@en
type
label
Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis.
@en
prefLabel
Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis.
@en
P2860
P356
P1476
Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis
@en
P2093
Amy E Palmer
Derrick Sek Tong Ong
P2860
P2888
P304
P356
10.1038/NCHEMBIO.368
P577
2010-05-09T00:00:00Z