Találati lista | Tudóstér

001-es BibID:	BIBFORM031294
Első szerző:	Brubel Réka
Cím:	Investigation of pituitary adenylate cyclase activating polypeptide in human gynecological and other biological fluids by using MALDI TOF mass spectrometry. / Brubel R., Reglodi D., Jambor E., Koppan M., Varnagy A., Biro Z., Kiss P., Gaal V., Bodis J., Bay Cs., Veszpremi B., Tamas A., Nemeth J., Mark L.
Dátum:	2011
Megjegyzések:	Pituitary adenylate cyclase activating polypeptide (PACAP) is a multifunctional and pleiotropic neuropeptide. PACAP hasdiverse effects in the endocrine system, among others, it plays important roles in oogenesis, implantation and development ofthe nervous system.However, it is not knownwhether PACAP is present in the fluids of the human reproductive organs. The aimof the present study was to determine, by means of mass spectrometry and radioimmunoassay, whether PACAP is present inhuman amniotic fluid, ovarian follicular fluid and cervico-vaginal fluid. Samples were obtained from healthy adult volunteers.Our MALDI TOF and MALDI TOF/TOF spectrometry results show that PACAP38 is present in all of the follicular fluid samples,and PACAP-like immonoreactivity was also measured by radioimmunoassay. However, we did not find the characteristic peakrepresenting the unmodified 38 amino acid form of the peptide in normal cervico-vaginal smear and amniotic fluid samples.Furthermore, we analyzed other body fluids for comparison, such as human nasal fluid, saliva and aqueous humor. PACAPwas not found in these latter samples. In summary, the present study provides evidence for the presence of PACAP in humanfollicular fluid, suggesting a role in oocyte function, but determination of the exact physiological significance awaits furtherinvestigation.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban cervico-vaginal fluid amniotic fluid follicular fluid nasal fluid saliva aqueous humor mass spectrometry radioimmunoassay
Megjelenés:	Journal of Mass Spectrometry. - 46 : 2 (2011), p. 189-194. -
További szerzők:	Reglődi Dóra (Idegtudományok) Jámbor E. Koppán Miklós Várnagy A. Biró Zsolt (szemész) Kiss P. Gaál V. Bodis József (Pécs) Bay Csaba Veszprémi B. Tamás A. (Pécs) Németh József (1954-) (vegyész, analitikus) Mark L.
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM055469
Első szerző:	Somogyi Árpád (kémikus)
Cím:	Chemical ionization in the atmosphere? A model study on negatively charged "exotic" ions generated from Titan's tholins by ultrahigh resolution MS and MS/MS / Árpád Somogyi, Mark A. Smith, Véronique Vuitton, Roland Thissen, István Komáromi
Dátum:	2012
ISSN:	1387-3806
Megjegyzések:	Titan tholins generated by complex processes (including ion-molecule reactions) in a laboratory plasma were investigated by ultrahigh resolution MS and tandem MS/MS measurements. Titan has a special interest in astrobiology because "in situ" measurements by the Cassini-Huygens spacecraft indicate the presence of complex organic molecules of prebiotic interest. The present work focuses on negatively charged ions that have not been systematically studied by ultrahigh resolution MS and MS/MS. The negatively charged ions were generated from a tholin sample by both laser desorption ionization (LDI) and electrospray ionization (ESI). The chemical compositions determined for the negatively charged ions clearly indicate the presence of highly unsaturated (H/C < 1) species with high nitrogen content (presumably related to multiple cyano functionalities). This is characteristically different from the previously analyzed positively charged ions that are more saturated and contain amino and imino functionalities. Based on tandem MS/MS experiments and quantum chemical calculations we propose characteristic structural features for selected ions. They include open chain (C6N3-) and aromatic ring structures (C10N5-). The basic non-aromatic structural unit C2N3- seems to play an important role and several structural "families" can be derived as HCN. HCCH and H-2 "adducts" of this ion.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	International Journal of Mass Spectrometry. - 316-318 (2012), p. 157-163. -
További szerzők:	Smith, Mark A. Vuitton, Véronique Thissen, Roland Komáromi István (1957-) (vegyész, molekuláris biológus, biokémikus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM083418
035-os BibID:	(PMID)31967473
Első szerző:	Steckel Arnold
Cím:	Investigation of Neutral Losses and the Citrulline Effect for Modified H4 N-Terminal Pentapeptides / Arnold Steckel, Katalin Uray, Gergo Kalló, Éva Csosz, Gitta Schlosser
Dátum:	2020
ISSN:	1044-0305
Megjegyzések:	Tandem mass spectrometry is an indispensable tool in proteomics used for protein sequencing and quantitation. On the basis of the sequential fragments usually generated from peptide ions via collision-induced dissociation, electron-transfer dissociation, or a combination of the two, probabilistic database search engines could be used for the identification of the peptides. The correct localization of posttranslational modifications (PTMs) poses a more challenging problem than the general identification of proteins. Histones are involved in the regulation of DNA transcription via the wealth of PTMs on their N-terminal tail. In this study, we analyzed the histone H4 peptide SGRGK incorporating four different posttranslational modifications: citrullination, acetylation, phosphorylation, and arginine methylation at various positions. The pentapeptides model the enzymatic cleavage of the N-terminal tail of human histone H4 protein by LysC protease. Fragmentation of the peptides was investigated using higher-energy collisional dissociation (HCD), electron-transfer dissociation (ETD), and electron-transfer higher-energy collisional dissociation (EThcD) on an ultrahigh resolution and mass accuracy instrument. We found that while all three techniques have their unique characteristics, advantages, and pitfalls, EThcD generated the most fragment ion-rich spectra. Despite potential ambiguities regarding exact fragment identities, full sequence coverage and PTM mapping may also be achievable. We also found novel neutral losses from the charge-reduced precursors characteristic to citrullination in ETD and EThcD which may be used in proteomic applications. N-Terminal acetylation and arginine methylation could also be confirmed by their characteristic neutral losses from the charge-reduced precursors.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk citrullináció acetiláció arginin metiláció poszttranszlációs módosítás hiszton kód ütközés indukálta disszociáció elektron transzfer disszociáció tandem tömegspektrometria
Megjelenés:	Journal of The American Society For Mass Spectrometry. - 31 : 3 (2020), p. 565-573. -
További szerzők:	Uray Katalin Kalló Gergő (1989-) (molekuláris biológus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Schlosser Gitta
Pályázati támogatás:	GINOP-2.3.3-15-2016-00020 GINOP VEKOP-2.3.3-15-2017-00020 GINOP 2018-1.2.1-NKP-2018-00005 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	bibEBI00010183
Első szerző:	Szabó Pál T.
Cím:	Identification of factor C protein from Streptomyces griseus by microelectrospray mass spectrometry / P. T. Szabó, Z. Kele, Zs. Birkó, F. Szeszák, S. Biró, T. Janáky
Dátum:	1999
Megjegyzések:	Factor C, an extracellular signal protein of cellular differentiation, was studied and significant homology was found to several zinc finger-type regulatory proteins. The complete amino acid sequence, deduced from the gene, that encodes the protein, did not support the hypothesis that this protein might be a zinc finger-type regulatory protein. However, a theoretical single nucleotide insertion in the gene can result in another similarly sized protein containing about 20 His residues, which would be responsible for the high zinc affinity of factor C. The protein sample was reduced, alkylated and then in-gel digested with trypsin. The peptide fragments were then separated by capillary chromatography and identified by microelectrospray mass spectrometry. Peaks of higher intensity were sequenced by tandem mass spectrometry. The identified peptide fragments and the measured molecular mass of factor C protein also confirmed the original sequence of protein, as there was no shift in the open reading frame.
Tárgyszavak:	idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Mass Spectrometry. - 34 : 12 (1999), p. 1312-1316. -
További szerzők:	Kele Zoltán Hádáné Birkó Zsuzsanna (1971-) (molekuláris genetikus) Szeszák Ferenc Biró Sándor (1949-) (molekuláris genetikus) Janáky Tamás
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: