Kokalj-Jenko, Saša, biokemija, 1976-
Saša Kokalj-Jenko
VIAF ID: 114154440116535340599 ( Personal )
Permalink: http://viaf.org/viaf/114154440116535340599
Preferred Forms
4xx's: Alternate Name Forms (4)
Works
Title | Sources |
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Amyloids and protein misfolding : proline gates to amyloid structures | |
Biology for health and disease : workshop on integrating proteomics, interactomics and structural biology via systems biology approaches : Brussels, 16-17 march 2010 | |
Cathepsin S bound to the surface retains its full activity | |
A central role for protein aggregation in neurodegenerative disease : mechanistic and structural studies of human stefins | |
Crystal structure of stefin A in complex with cathepsin H reveals the mechanism of cysteine exopeptidase - inhibitor interaction | |
Different propensity to form amyloid-fibrils by two homologous proteins - human stefins A and B | |
Essential role of Pro 74 in stefin B fibril formation; cyclophilin A delays the fibril growth | |
Extracellular action of cathepsins in the thyroid gland | |
Fibrillation of stefin B : stepwise progress towards the assembly into amyloid fibrils | |
Folding and amyloid-fibril formation for a series of human stefins' chimeras: any correlation? | |
Force spectroscopy measurements of MoSIx nanowires with functionalized molecules | |
How do stefins form amyloid fibrils? : from a structural point of view | |
Immobilization of proteins onto MoSxly nanowires | |
Individual recombinant thyroglobulin type-1 domains are substrates for lysosomal cysteine proteinases | |
Ključna vloga prolina 74 pri rasti fibril stefina B; ciklofilin A podaljša lag fazo rasti fibril | |
Mechanism of amyloid fibril formation by human stefin-B as monitored using flow cytometry | |
Mechanismo de formación de fibrilos amiloides de la estefina B humana : [presented at] 7° Congreso Argentino de Neuropsiquiatría, 3° Congreso Latinoamericano de Neuropsiquiatría, VIII Jornadas de la Enfermedad de Alzheimer | |
Model for stefin B amyloid-fibrillation from the kinetics & size the toxic oligomers | |
Modulation of contact order effects in the two-state folding of stefins A and B | |
Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions | |
Mo[sub]6S[sub](9-x)I[sub]x nanowire recognitive molecular-scale connectivity | |
Proline isomerization in stefin B : a crucial step towards amyloid fibril formation | |
Roles of papain-like cathepins in immune system response : excluding interactions as the other face of selectivity | |
Self-assembly of gold particles to MoS[sub]xI[sub]y nanowires ends | |
Single molecule force spectroscopy of cathepsin L - stefin A interaction | |
Stefin B fibrillation: how many intermediates are there between its native structure and the mature fibrillar form? | |
Stefin B - modelni protein za študij napačnega zvijanja proteinov in njihove agregacije | |
Structure of cystatin B tetrameter : prolines as switches in amyloid fibril formation | |
Strukturne študije kompleksov katepsinov s proteinskimi inhibitorji | |
Strukturne študije oligomerov in amiloidnih fibril stefinov A in B : doktorska disertacija | |
Toxic oligomers of amyloidogenic proteins and aggregation in U2OS cell line : a case study of human stefin B (cystatin B) | |
Toxicity, size and morphology of prefibrillar oligomers : applied from the outside or expressed inside cells | |
Uporaba sinhrotronske svetlobe pri študiju strukture proteinov = Synchrotron radiation in macromolecular crystallography |