Some like it hot: the structure and function of small heat-shock proteins.
about
Analysis and phylogeny of small heat shock proteins from marine viruses and their cyanobacteria hostNative aggregation as a cause of origin of temporary cellular structures needed for all forms of cellular activity, signaling and transformationsBinding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motifN-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperoneHeat shock proteins and resistance to desiccation in congeneric land snailsHsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiaeMultivalent fusion protein vaccine for lymphatic filariasisCharcot-Marie-Tooth disease and intracellular trafficPositive or negative involvement of heat shock proteins in multiple sclerosis pathogenesis: an overviewChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisInteraction of HSP20 with a viral RdRp changes its sub-cellular localization and distribution pattern in plants.Fusion of protein aggregates facilitates asymmetric damage segregationStructure and Functional Studies of the CS Domain of the Essential H/ACA Ribonucleoparticle Assembly Protein SHQ1Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersCrystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a GrooveN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneityAlternative bacterial two-component small heat shock protein systemsStructural Instability Tuning as a Regulatory Mechanism in Protein-Protein InteractionsChanges in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the -crystallin domainHigh-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria.Multiple chaperonins in bacteria--novel functions and non-canonical behaviorsIncreased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathyHold me tight: Role of the heat shock protein family of chaperones in cardiac diseasePolyphosphate is a primordial chaperoneBiochemical characterization and evaluation of a Brugia malayi small heat shock protein as a vaccine against lymphatic filariasisPhosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neuronsIn Vitro Structural and Functional Characterization of the Small Heat Shock Proteins (sHSP) of the Cyanophage S-ShM2 and Its Host, Synechococcus sp. WH7803The HSP70 chaperone machinery: J proteins as drivers of functional specificityMass spectrometry quantifies protein interactions--from molecular chaperones to membrane porins.Impaired Chaperone Activity of Human Heat Shock Protein Hsp27 Site-Specifically Modified with Argpyrimidine.Neural stem cell transplantation can ameliorate the phenotype of a mouse model of spinal muscular atrophy.The eye lens chaperone alpha-crystallin forms defined globular assemblies.A novel mechanism for small heat shock proteins to function as molecular chaperones.Pharmacological chaperone for α-crystallin partially restores transparency in cataract modelsConstruction of gender-enriched cDNA archives for adult Oesophagostomum dentatum by suppressive-subtractive hybridization and a microarray analysis of expressed sequence tags.Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthaseSite-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationSystems analysis of chaperone networks in the malarial parasite Plasmodium falciparum.
P2860
Q21132413-5AA211D8-8A2C-4CEA-B2C2-702EC4BF2BE0Q21245219-19BF54F9-9B28-4E89-B6C4-09DBF9EF2F35Q24305073-986F994B-6850-4BD9-924D-EA00331A3F6DQ24337796-4999C74F-6609-44B9-A6AE-5413C795A797Q24607745-948A8866-50BD-4D32-A815-02239CDF2072Q24610346-2D4A0E2D-3C99-4482-ADA9-B204333477F8Q24630552-33761873-7FF1-431E-8C7A-CE24492C5C91Q26824841-D9E017AA-28B9-454F-8D5C-471C912C6486Q27000682-A6528200-B364-4F20-877F-F32DD0DB4E69Q27004511-6DD052A2-2647-49BD-B729-DE3AB325F47BQ27308680-15C424FD-A784-40E1-956A-3A39A28660B5Q27314757-29FD1E7F-2726-4A14-A72F-FEE5B536FCADQ27652939-4971A8FF-F29D-45BD-9E42-CE7D0766B80FQ27664218-5616EFAA-0486-473B-A3FF-6E168F2898E9Q27666994-A7B2624F-2BF1-4782-B9E1-506CE285C6D2Q27667422-4F29B0FD-E36B-4D68-9693-EF172D57C0EAQ27675261-47A9C344-36E0-4750-92F7-6D229A300A3AQ27676032-6A445683-C305-4B3F-A512-81F16B31346DQ27677069-B79D6554-6EB7-40B8-A4B5-69496275C1F1Q27677103-3272B780-7589-48DA-A070-EF3CAC09B193Q27679512-C69E2547-2BD3-474F-9BEA-2D5F3298F4A0Q27939210-78E8A493-4458-4CC0-B5B3-921B5EA09EF0Q28084087-06B8EAAD-4FFC-4E0C-ABD3-F3D14D7C0232Q28115297-7B26DF89-1EB1-458D-A863-EA732A40784EQ28296634-B9E55AFA-D872-45EC-91CF-0B853221D980Q28307913-E4A1D294-9714-4473-8D15-946E32852537Q28482148-C1093298-008F-4EF0-932A-BC5BF89F58A4Q28573943-3E6DBC90-59FD-4870-AF68-E04A5009CBFEQ28829851-96CEF9B6-9FAC-4733-8165-82DFD04C15A4Q29616140-8827409B-DFA3-4917-BB5B-B2A2CD7F2071Q30368236-587136D8-40CC-45DB-AFC1-3EC0840B8C62Q30390809-A2AFD31E-3AE3-4801-937D-C491BBAEFB55Q30483218-A44DB029-4B86-46CC-B134-F7E024F26274Q30489512-4F35EA13-1CE7-4C9E-A06F-9BAF6CC4E756Q30625248-790D020B-62F8-4307-BFD6-AAB4B58D68C2Q30700509-8501C96F-4B48-41D2-8858-892C4615AAA9Q33232158-E1FE2785-31B6-4EF5-92B7-7F8B6F43BA3DQ33287601-4666FE72-2B59-4F6B-808B-BF68DFC5E0C4Q33302904-3B328987-D79C-456C-AD7D-E88DDA98D589Q33302931-14E301A4-DD14-48C9-8A02-637222B22F43
P2860
Some like it hot: the structure and function of small heat-shock proteins.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Some like it hot: the structure and function of small heat-shock proteins.
@ast
Some like it hot: the structure and function of small heat-shock proteins.
@en
type
label
Some like it hot: the structure and function of small heat-shock proteins.
@ast
Some like it hot: the structure and function of small heat-shock proteins.
@en
prefLabel
Some like it hot: the structure and function of small heat-shock proteins.
@ast
Some like it hot: the structure and function of small heat-shock proteins.
@en
P2093
P356
P1476
Some like it hot: the structure and function of small heat-shock proteins
@en
P2093
Daniel Weinfurtner
Johannes Buchner
Martin Haslbeck
P2888
P304
P356
10.1038/NSMB993
P577
2005-10-01T00:00:00Z