The role of initial oligomers in amyloid fibril formation by human stefin B.

scientific article published on 05 September 2013

The role of initial oligomers in amyloid fibril formation by human stefin B. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.3390/IJMS140918362
P932PMC publication ID3794784
P698PubMed publication ID24013380
P5875ResearchGate publication ID256469196

P50authorAndrej VilfanQ37383471
Julia SmirnovaQ61330948
Andra NoormägiQ64681520
Ajda Taler-VerčičQ82499105
Tiina KirsipuuQ85648484
Rosemary A StaniforthQ97561630
P2093author name stringPeep Palumaa
Eva Zerovnik
Miha Skarabot
Mira Polajnar
Merlin Friedemann
Magda Tušek Znidarič
Matjaž Zganec
P2860cites workCalorimetric measurements of thermal denaturation of stefins A and B. Comparison to predicted thermodynamics of stefin-B unfoldingQ41815677
Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometryQ41932531
Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions.Q42428466
In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1.Q43057871
Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synucleinQ43256880
Size and morphology of toxic oligomers of amyloidogenic proteins: a case study of human stefin B.Q43477001
Native protein MS and ion mobility large flying proteins with ESI.Q43512452
Human stefin B readily forms amyloid fibrils in vitroQ43875211
Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometryQ44022725
Evidence for non-isostructural replacement of Zn(2+) with Cd(2+) in the beta-domain of brain-specific metallothionein-3.Q44130963
The Alzheimer's amyloid-β(1-42) peptide forms off-pathway oligomers and fibrils that are distinguished structurally by intermolecular organizationQ44432291
Alzheimer's disease Abeta peptide fragment 10-30 forms a spectrum of metastable oligomers with marked preference for N to N and C to C monomer termini proximityQ45151322
Organization of nucleobase-functionalized beta-peptides investigated by soft electrospray ionization mass spectrometryQ45796943
Essential role of Pro 74 in stefin B amyloid-fibril formation: dual action of cyclophilin A on the processQ46098256
Development of the structural core and of conformational heterogeneity during the conversion of oligomers of the mouse prion protein to worm-like amyloid fibrilsQ46102603
Protein aggregation as a possible cause for pathology in a subset of familial Unverricht-Lundborg diseaseQ46393959
The mechanism of amyloid-fibril formation by stefin B: temperature and protein concentration dependence of the rates.Q46476689
Interaction of human stefin B in the prefibrillar oligomeric form with membranes. Correlation with cellular toxicityQ46545728
Interaction with model membranes and pore formation by human stefin B: studying the native and prefibrillar statesQ46657445
Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein.Q46894359
Compactness of the molten globule in comparison to unfolded states as observed by size-exclusion chromatographyQ47366397
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometryQ47708702
Different propensity to form amyloid fibrils by two homologous proteins-Human stefins A and B: searching for an explanation.Q47867012
Abnormal distribution of cathepsin proteinases and endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam, and senile dementia and in the agedQ48380704
Cloning a synthetic gene for human stefin B and its expression in E. coliQ22254878
The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interactionQ24556546
Stepwise evolution of protein native structure with electrospray into the gas phase, 10(-12) to 10(2) sQ24653770
Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamilyQ27634658
Essential role of proline isomerization in stefin B tetramer formationQ27643513
Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1)Q28115575
Cysteine proteinase inhibitors stefin A, stefin B, and cystatin C in sera from patients with colorectal cancer: relation to prognosisQ28145435
Novel cystatin B mutation and diagnostic PCR assay in an Unverricht-Lundborg progressive myoclonus epilepsy patientQ28252321
Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1)Q28275721
The cystatins: Protein inhibitors of cysteine proteinasesQ28283958
Cystatin B deficiency sensitizes neurons to oxidative stress in progressive myoclonus epilepsy, EPM1Q28582306
Influence of partial unfolding and aggregation of human stefin B (cystatin B) EPM1 mutants G50E and Q71P on selective cleavages by cathepsins B and S.Q30426489
MEROPS: the peptidase database.Q31033155
Role of small oligomers on the amyloidogenic aggregation free-energy landscapeQ33570944
Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells.Q33661328
Unverricht-Lundborg disease with cystatin B gene abnormalitiesQ34111631
Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometryQ34173720
Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: distinguishing two-state from multi-state transitionsQ34468020
Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulatorsQ34754105
Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegenerationQ35795163
Protein folding mechanisms studied by time-resolved electrospray mass spectrometryQ36417077
Differences in aggregation properties of three site-specific mutants of recombinant human stefin B.Q36526184
Cystatins: biochemical and structural properties, and medical relevanceQ37175525
Structure-neurotoxicity relationships of amyloid beta-protein oligomersQ37329557
Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity.Q38033158
Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assemblyQ38051908
Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assemblyQ38272762
Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo.Q40071241
Studying noncovalent protein complexes by electrospray ionization mass spectrometryQ41671168
Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry.Q52855180
Comparative ESI-MS study of ∼2.2 MDa native hemocyanins from deep-sea and shore crabs: from protein oligomeric state to biotopeQ57088033
Quadrupole time-of-flight mass spectrometry of the native hemocyanin of the deep-sea crab Bythograea thermydronQ57088062
Similar toxicity of the oligomeric molten globule state and the prefibrillar oligomersQ57186606
Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditionsQ57220352
The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrumentQ57666433
Amyloid fibril formation by human stefin B: influence of pH and TFE on fibril growth and morphologyQ58179795
Differences in the effects of TFE on the folding pathways of human stefins A and BQ60214193
On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phasesQ60214202
On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate statesQ60214206
Intermediates in denaturation of a small globular protein, recombinant human stefin BQ68111939
Protein inhibitors of cysteine proteinases. I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytesQ71248338
Amyloid fibril formation by human stefin B in vitro: immunogold labelling and comparison to stefin AQ74438034
Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometryQ78786937
Ion mobility separation coupled with MS detects two structural states of Alzheimer's disease Aβ1-40 peptide oligomersQ83211046
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue9
P407language of work or nameEnglishQ1860
P304page(s)18362-18384
P577publication date2013-09-05
P1433published inInternational Journal of Molecular SciencesQ3153277
P1476titleThe role of initial oligomers in amyloid fibril formation by human stefin B
P478volume14

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cites work (P2860)
Q55276020Inhibition of Protein Aggregation by Several Antioxidants.
Q61813190Possible Mechanisms by which Stefin B could Regulate Proteostasis and Oxidative Stress
Q42105214Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation
Q92694063Prolines Affect the Nucleation Phase of Amyloid Fibrillation Reaction; Mutational Analysis of Human Stefin B
Q39438003Putative alternative functions of human stefin B (cystatin B): binding to amyloid-beta, membranes, and copper

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