Sakari Joenvaara

Mr. Sakari Joenvaara


Research Focus & Metrics

Academic Career Length

16Years (2011-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 January 2011 in Clinical and Translational Allergy
Verified
Journal Article
Open access
PDF file
PMPirkko Mattila
Pirkko Mattila
SJSakari Joenvaara
Sakari Joenvaara
JRJutta Renkonen
Jutta Renkonen
STSanna Toppila-Salmi
Sanna Toppila-Salmi
RRRisto Renkonen
Risto Renkonen
The objective of this review is to focus on putative modified epithelial functions related to allergy. The dysregulation of the epithelial barrier might result in the allergen uptake, which could be the primary defect in the pathogenesis of allergic reaction. We review the literature of the role of respiratory epithelium as an active barrier, how allergens are transported through it and how it senses the hostile environmental allergens and other dangerous stimuli.

1 November 2018 in Oral Oncology
Verified
Journal Article
Closed access
ADAmy Dickinson
Amy Dickinson
MSMayank Saraswat
Mayank Saraswat
AMAntti Mäkitie
Antti Mäkitie
RSRobert Silén
Robert Silén
JHJaana Hagström
Jaana Hagström
SSSuvi Silén
Suvi Silén

1 January 2013 in Proteome Science
Verified
Journal Article
Open access
PDF file
VPVille I Parviainen
Ville I Parviainen
SJSakari Joenvaara
Sakari Joenvaara
NTNiina Tohmola
Niina Tohmola
RRRisto Renkonen
Risto Renkonen
Cell surface glycoprotein sialylation is one of the most ubiquitous glycan modifications found on higher eukaryotes. The surface sialylation pattern of cells is influenced by the cellular environment but also by the Golgi sialyltransferase activity and flux of metabolites through sialic acid producing pathways. Altered cell surface sialic acid patterns have been observed in several cancers and other pathological conditions. In this experiment we examined the cellular proteomic changes that occur in human embryonic kidney cells after 24 hours of sialic acid overproduction using N-Acetylmannosamine. We utilized high resolution mass spectrometry and label free protein quantification to characterize the relative changes in protein abundance as well as multiple reaction monitoring to quantify the cellular sialic acid levels.

23 July 2020 in Foods
Verified
Journal Article
Open access
PDF file
GAGeorg Arju
Georg Arju
ATAnastassia Taivosalo
Anastassia Taivosalo
DPDmitri Pismennõi
Dmitri Pismennõi
TLTaivo Lints
Taivo Lints
RVRaivo Vilu
Raivo Vilu
SJSakari Joenvaara
Sakari Joenvaara
Until now, cheese peptidomics approaches have been criticised for their lower throughput. Namely, analytical gradients that are most commonly used for mass spectrometric detection are usually over 60 or even 120 min. We developed a cheese peptide mapping method using nano ultra-high-performance chromatography data-independent acquisition high-resolution mass spectrometry (nanoUHPLC-DIA-HRMS) with a chromatographic gradient of 40 min. The 40 min gradient did not show any sign of compromise in milk protein coverage compared to 60 and 120 min methods, providing the next step towards achieving higher-throughput analysis. Top 150 most abundant peptides passing selection criteria across all samples were cross-referenced with work from other publications and a good correlation between the results was found. To achieve even faster sample turnaround enhanced DIA methods should be considered for future peptidomics applications.