scholarly article | Q13442814 |
P50 | author | Andrej Vilfan | Q37383471 |
Julia Smirnova | Q61330948 | ||
Andra Noormägi | Q64681520 | ||
Ajda Taler-Verčič | Q82499105 | ||
Tiina Kirsipuu | Q85648484 | ||
Rosemary A Staniforth | Q97561630 | ||
P2093 | author name string | Peep Palumaa | |
Eva Zerovnik | |||
Miha Skarabot | |||
Mira Polajnar | |||
Merlin Friedemann | |||
Magda Tušek Znidarič | |||
Matjaž Zganec | |||
P2860 | cites work | Calorimetric measurements of thermal denaturation of stefins A and B. Comparison to predicted thermodynamics of stefin-B unfolding | Q41815677 |
Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry | Q41932531 | ||
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-synuclein | Q43256880 | ||
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 vitro | Q43875211 | ||
Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry | Q44022725 | ||
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 organization | Q44432291 | ||
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 proximity | Q45151322 | ||
Organization of nucleobase-functionalized beta-peptides investigated by soft electrospray ionization mass spectrometry | Q45796943 | ||
Essential role of Pro 74 in stefin B amyloid-fibril formation: dual action of cyclophilin A on the process | Q46098256 | ||
Development of the structural core and of conformational heterogeneity during the conversion of oligomers of the mouse prion protein to worm-like amyloid fibrils | Q46102603 | ||
Protein aggregation as a possible cause for pathology in a subset of familial Unverricht-Lundborg disease | Q46393959 | ||
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 toxicity | Q46545728 | ||
Interaction with model membranes and pore formation by human stefin B: studying the native and prefibrillar states | Q46657445 | ||
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 chromatography | Q47366397 | ||
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry | Q47708702 | ||
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 aged | Q48380704 | ||
Cloning a synthetic gene for human stefin B and its expression in E. coli | Q22254878 | ||
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 interaction | Q24556546 | ||
Stepwise evolution of protein native structure with electrospray into the gas phase, 10(-12) to 10(2) s | Q24653770 | ||
Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily | Q27634658 | ||
Essential role of proline isomerization in stefin B tetramer formation | Q27643513 | ||
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 prognosis | Q28145435 | ||
Novel cystatin B mutation and diagnostic PCR assay in an Unverricht-Lundborg progressive myoclonus epilepsy patient | Q28252321 | ||
Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1) | Q28275721 | ||
The cystatins: Protein inhibitors of cysteine proteinases | Q28283958 | ||
Cystatin B deficiency sensitizes neurons to oxidative stress in progressive myoclonus epilepsy, EPM1 | Q28582306 | ||
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 landscape | Q33570944 | ||
Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells. | Q33661328 | ||
Unverricht-Lundborg disease with cystatin B gene abnormalities | Q34111631 | ||
Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry | Q34173720 | ||
Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: distinguishing two-state from multi-state transitions | Q34468020 | ||
Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators | Q34754105 | ||
Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration | Q35795163 | ||
Protein folding mechanisms studied by time-resolved electrospray mass spectrometry | Q36417077 | ||
Differences in aggregation properties of three site-specific mutants of recombinant human stefin B. | Q36526184 | ||
Cystatins: biochemical and structural properties, and medical relevance | Q37175525 | ||
Structure-neurotoxicity relationships of amyloid beta-protein oligomers | Q37329557 | ||
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 assembly | Q38051908 | ||
Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly | Q38272762 | ||
Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo. | Q40071241 | ||
Studying noncovalent protein complexes by electrospray ionization mass spectrometry | Q41671168 | ||
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 biotope | Q57088033 | ||
Quadrupole time-of-flight mass spectrometry of the native hemocyanin of the deep-sea crab Bythograea thermydron | Q57088062 | ||
Similar toxicity of the oligomeric molten globule state and the prefibrillar oligomers | Q57186606 | ||
Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions | Q57220352 | ||
The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument | Q57666433 | ||
Amyloid fibril formation by human stefin B: influence of pH and TFE on fibril growth and morphology | Q58179795 | ||
Differences in the effects of TFE on the folding pathways of human stefins A and B | Q60214193 | ||
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 phases | Q60214202 | ||
On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states | Q60214206 | ||
Intermediates in denaturation of a small globular protein, recombinant human stefin B | Q68111939 | ||
Protein inhibitors of cysteine proteinases. I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes | Q71248338 | ||
Amyloid fibril formation by human stefin B in vitro: immunogold labelling and comparison to stefin A | Q74438034 | ||
Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry | Q78786937 | ||
Ion mobility separation coupled with MS detects two structural states of Alzheimer's disease Aβ1-40 peptide oligomers | Q83211046 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 9 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 18362-18384 | |
P577 | publication date | 2013-09-05 | |
P1433 | published in | International Journal of Molecular Sciences | Q3153277 |
P1476 | title | The role of initial oligomers in amyloid fibril formation by human stefin B | |
P478 | volume | 14 |
Q55276020 | Inhibition of Protein Aggregation by Several Antioxidants. |
Q61813190 | Possible Mechanisms by which Stefin B could Regulate Proteostasis and Oxidative Stress |
Q42105214 | Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation |
Q92694063 | Prolines Affect the Nucleation Phase of Amyloid Fibrillation Reaction; Mutational Analysis of Human Stefin B |
Q39438003 | Putative alternative functions of human stefin B (cystatin B): binding to amyloid-beta, membranes, and copper |
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