@book{MTMT:36154374,
	title = {Érettségi felkészítő - Kémia - Emelt szint},
	url = {https://m2.mtmt.hu/api/publication/36154374},
	isbn = {9789633124109},
	author = {Kiss, Edina and Láng, Emma and Molnár, István and Vasanits, Anikó},
	publisher = {ELTE Eötvös Kiadó},
	unique-id = {36154374},
	year = {2025},
	orcid-numbers = {Kiss, Edina/0000-0001-5054-4530; Láng, Emma/0000-0002-7638-8983; Molnár, István/0000-0002-4965-3980; Vasanits, Anikó/0000-0001-6469-5436}
}

@article{MTMT:2014123,
	title = {Conformational analysis of amyloid precursor protein fragment containing amino acids 667-676, and the effect of D-Asp and iso-Asp substitution at Asp(672) residue},
	url = {https://m2.mtmt.hu/api/publication/2014123},
	author = {Shanmugam, G and Polavarapu, PL and Láng, Emma and Majer, Zsuzsanna (Deckerné)},
	doi = {10.1016/j.jsb.2012.01.012},
	journal-iso = {J STRUCT BIOL},
	journal = {JOURNAL OF STRUCTURAL BIOLOGY},
	volume = {177},
	unique-id = {2014123},
	issn = {1047-8477},
	abstract = {Amyloid precursor protein (APP) fragment containing amino acids 667-676, (APP(667-676)), is a substrate for beta-secretase which is responsible for generating amyloid beta peptides. Conformational analysis of APP(667-676) peptide [Ac-Ser-Glu-Val-Lys-Met-Asp-Ala-Glu-Phe-Arg-NH2] and the effect of substitution of Asp(672) with D-Asp and iso-L-Asp, studied for the first time, demonstrate that the peptide backbone of APP(667-676) is flexible and adopts different conformations in different solvent environments (water, trifluoroethanol and dimethylsulfoxide). A major conformational difference was observed in trifluoroethanol solvent when Asp(672) is substituted with D-Asp and iso-Asp. These conformational changes involved in APP(667-676) may assist in understanding the interactions between beta-secretase and APP(667-676), with relevance to Alzheimer's disease. (C) 2012 Elsevier Inc. All rights reserved.},
	year = {2012},
	eissn = {1095-8657},
	pages = {621-629},
	orcid-numbers = {Láng, Emma/0000-0002-7638-8983}
}

@article{MTMT:114332,
	title = {Vibrational spectroscopic detection of H-bonded b- and g-turns in cyclic peptides and glycopeptides},
	url = {https://m2.mtmt.hu/api/publication/114332},
	author = {Vass, Elemér and Láng, Emma and Samu, J and Majer, Zsuzsanna (Deckerné) and Kajtár-Peredy, Mária and Mák, Marianna and Radics, Lajos and Hollósi, Miklós},
	doi = {10.1016/S0022-2860(97)00216-0},
	journal-iso = {J MOL STRUCT},
	journal = {JOURNAL OF MOLECULAR STRUCTURE},
	volume = {440},
	unique-id = {114332},
	issn = {0022-2860},
	year = {1998},
	eissn = {1872-8014},
	pages = {59-71},
	orcid-numbers = {Vass, Elemér/0000-0001-8898-3846; Láng, Emma/0000-0002-7638-8983}
}

@article{MTMT:1230617,
	title = {Racemization-induced defolding and aggregation of fragments of beta-amyloid protein: an early step in the formation of amyloid plaques},
	url = {https://m2.mtmt.hu/api/publication/1230617},
	author = {Láng, Emma and Majer, Zsuzsanna (Deckerné) and Vass, Elemér and Szabó, Sándor and Hallgas, B and Hollósi, Miklós},
	journal-iso = {IDEGGYOGY SZEMLE},
	journal = {IDEGGYOGYASZATI SZEMLE / CLINICAL NEUROSCIENCE},
	volume = {51},
	unique-id = {1230617},
	issn = {0019-1442},
	year = {1998},
	eissn = {2498-6208},
	pages = {11-12},
	orcid-numbers = {Láng, Emma/0000-0002-7638-8983; Vass, Elemér/0000-0001-8898-3846; Szabó, Sándor/0009-0006-5697-966X}
}

@article{MTMT:2715,
	title = {Synthesis and conformational analysis of the N-glycosylated cyclic:cyclo[Gly-Pro-Asn(GlcNAc)-Gly-NH-(CH2)(4)-CO]},
	url = {https://m2.mtmt.hu/api/publication/2715},
	author = {Láng, Emma and Hargittai, B and Majer, Zsuzsanna (Deckerné) and Perczel, András and Mák, Marianna and Kajtár-Peredy, Mária and Radics, Lajos and Fasman, GD and Hollósi, Miklós},
	journal-iso = {PROTEIN PEPTIDE LETT},
	journal = {PROTEIN AND PEPTIDE LETTERS},
	volume = {3},
	unique-id = {2715},
	issn = {0929-8665},
	abstract = {This paper reports the synthesis and conformational characterization of
		the cyclic peptides cyclo[Gly-Pro-Asp(ocHex)-Gly-NH-(CH2)(4)-Co] ((1)
		under bar), cyclo[Gly-Pro-Asp-Gly-NH-(CH2)(4)-CO] ((2) under bar),
		cyclo[Gly-Pro-Asn-Gly-NH-(CH2)(4)-CO] ((3) under bar) and the
		Asn-glycosylated cyclic title compound
		cyclo[Gly-Pro-Asn(GlcNAc)-Gly-NH-(CH2)(4)-CO] ((4) under bar) (Scheme
		1).},
	year = {1996},
	eissn = {1875-5305},
	pages = {9-16},
	orcid-numbers = {Láng, Emma/0000-0002-7638-8983; Perczel, András/0000-0003-1252-6416}
}

@inproceedings{MTMT:120015,
	title = {Synthesis of phosphotyrosine-containing peptides: comparison of different methods and their use to investigate cell signalling via the T-cell receptor},
	url = {https://m2.mtmt.hu/api/publication/120015},
	author = {Tóth, Gábor and Váradi, Györgyi and Janáky, Tamás and Penke, Botond and Mák, Marianna and Láng, Emma and Ötvös, László and Hegedűs, Zoltán and Monostori, Éva},
	booktitle = {Peptides 1994},
	unique-id = {120015},
	year = {1995},
	pages = {743-744},
	orcid-numbers = {Tóth, Gábor/0000-0002-3604-4385; Váradi, Györgyi/0000-0001-7907-8908; Janáky, Tamás/0000-0002-6466-8283; Penke, Botond/0000-0003-0938-0567; Láng, Emma/0000-0002-7638-8983; Monostori, Éva/0000-0002-7442-3562}
}

@article{MTMT:1087403,
	title = {Chromatographic Studies ON The Racemization of Thiopeptides},
	url = {https://m2.mtmt.hu/api/publication/1087403},
	author = {Szókán, Gyula and Majer, Zsuzsanna (Deckerné) and Láng, Emma and Kajtar, M and Hollósi, Miklós and Peredykajtar, M},
	doi = {10.1080/10826079508010404},
	journal-iso = {J LIQ CHROMATOGR},
	journal = {JOURNAL OF LIQUID CHROMATOGRAPHY},
	volume = {18},
	unique-id = {1087403},
	issn = {0148-3919},
	abstract = {It was found by chromatographic, CD and NMR methods, that the thionation of piperazine-2,5-diones [cyclo(Aaa(1)-Aaa(2)) --> cyclo (Aaat(1)-Aaat(2) (Aaa = -NH-CHR-CO-; Aaat = -NH-CHR-CS-)] or piperazine-2,5-onthiones [cyclo(Aaat(1)-Aaa(2)) --> cyclo (Aaat(1)-Aaat(2))] and, occasionally, even the spontaneous cyclization of endothiodipeptide esters [H-Aaat(1)-Aaa(2) OR] result in enantiomeric (Aaa(1) or Aaa(2) = Gly) or diastereomeric mixtures of piperazine monothiones or dithiones. The diastereoisomers were separated by semipreparative HPLC and their quantitative product distribution was determined by an optimized HPLC method on Hypersil-silica column with CH2Cl2-EtOAc eluent mixtures. Isocratic RP-HPLC on ODS-Hypersil column and pre-column derivatization with 1-fluoro-2,4-dinitrophenyl-5-L-alanine amide (Marfey's reagent) were used to monitor the racemization of Ala and Pro residues and to determine the ratio of enantiomers. Thionation of urethane protected dipeptide esters or dethionation of the corresponding endothiodipeptide derivatives were not found to result in significant racemization. However, during the thionation of cyclic dipeptides or thiopeptides or isolation of piperazine-2,5- mono- or dithiones a partial or complete racemization could always be detected. Moreover, the acidic hydrolysis of thiopeptides was also accompanied by racemization and resulted in partially racemized amino (oxo)acids.},
	year = {1995},
	eissn = {2331-0413},
	pages = {941-964},
	orcid-numbers = {Láng, Emma/0000-0002-7638-8983}
}

@article{MTMT:1087405,
	title = {Hydrogen-bonding And Isomerization IN Thioamide Peptide Derivatives},
	url = {https://m2.mtmt.hu/api/publication/1087405},
	author = {Shaw, RA and Láng, Emma and Hollósi, Miklós and Mantsch, HH},
	doi = {10.1016/0584-8539(95)01448-9},
	journal-iso = {SPECTROCHIM ACTA A},
	journal = {SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY},
	volume = {51},
	unique-id = {1087405},
	issn = {1386-1425},
	abstract = {The conformations of fourteen thiopeptides in three solvents (acetonitrile, methylene chloride, DMSO) are discussed as inferred by interpretation of the amide infrared absorptions. The spectra indicate that the enhanced acidity of the thioamide N-H proton (and hence the stronger hydrogen-bonding donor potential) promotes the formation of C-5 ring structures that are not often found in unsubstituted peptides, and strong C(S)-N-H --> O=C hydrogen bonds render both C-7 (gamma-turn) and C-10 (beta-turn) structures more stable than their oxoamide counterparts. The ability of infrared spectra to discriminate among C-5, C-7, and C-10 structures is evaluated and discussed.},
	keywords = {PEPTIDE; ANALOGS; Isomerism; hydrogen bond; intramolecular H-bonds; SECONDARY THIOAMIDES; LEUCINE-ENKEPHALIN; THIOPEPTIDE},
	year = {1995},
	eissn = {1873-3557},
	pages = {1399-1412},
	orcid-numbers = {Láng, Emma/0000-0002-7638-8983}
}

@article{MTMT:2014168,
	title = {TYROSINE-PHOSPHORYLATION VERSUS SERINE-PHOSPHORYLATION LEADS TO CONFORMATIONAL-CHANGES IN A SYNTHETIC TAU-PEPTIDE},
	url = {https://m2.mtmt.hu/api/publication/2014168},
	author = {FABIAN, H and Ötvös, László and SZENDREI, GI and Láng, Emma and MANTSCH, HH},
	doi = {10.1080/07391102.1994.10508760},
	journal-iso = {J BIOMOL STRUCT DYN},
	journal = {JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS},
	volume = {12},
	unique-id = {2014168},
	issn = {0739-1102},
	abstract = {One of the major immunodominant epitopes of the paired helical filaments (PHF) of Alzheimer's disease is the peptide sequence GAEIVYKSPVVSGD (T3), comprising amino acids 389-402 of the microtubule associated protein, tau when it is phosphorylated at the first serine residue. While the corresponding anti-PHF monoclonal antibody recognizes the peptide phosphorylated at either serine, it does not recognize the tyrosine-phosphorylated peptide. Here we describe the effect of serine- versus tyrosine-phosphorylation on the conformation of a synthetic tau peptide. While adding a phosphate to the serine residue has practically no impact on the structure of the non-phosphorylated peptide, phosphorylation of the tyrosine results in considerable conformational changes.},
	year = {1994},
	eissn = {1538-0254},
	pages = {573-579},
	orcid-numbers = {Láng, Emma/0000-0002-7638-8983}
}

@article{MTMT:2743,
	title = {SYNTHESIS AND CONFORMATIONAL-ANALYSIS OF N-GLYCOPEPTIDES. 2. CD, MOLECULAR-DYNAMICS, AND NMR SPECTROSCOPIC STUDIES ON LINEAR N-GLYCOPEPTIDES},
	url = {https://m2.mtmt.hu/api/publication/2743},
	author = {Perczel, András and Láng, Emma and Hollósi, Miklós and Fasman, GD},
	doi = {10.1002/bip.360330416},
	journal-iso = {BIOPOLYMERS},
	journal = {BIOPOLYMERS},
	volume = {33},
	unique-id = {2743},
	issn = {0006-3525},
	abstract = {The comprehensive structural analysis reported herein of eight
		N-glycopeptides, in three different solvents, is based on quantitative
		CD experiments, homonuclear nuclear Overhauser effect measurements, and
		molecular dynamics (MD) calculations. Although several orientations of
		the two amide planes attached to the carbohydrate pyranose ring are
		possible, according to NOE, CD data, and MD simulations, of all of the
		glycopeptide models, regardless of the type of the carrier peptide,
		only one dominant conformer population was found. This conformer is
		characterized by a nearly trans orientation of the CH and NH hydrogens
		of both acetamido groups. This finding is in perfect agreement with
		x-ray crystallographic data on the solid state conformation of the
		1-N-acetyl- and 1-N- (beta-aspartoyl)
		-2-acetamido-2-deoxy-beta-D-glucopyranosylamine. The precise
		identification of this dominant conformer of N-glycopeptides in
		solution was the major question addressed herein by the structural
		analyses. A ''CD additivity'' experiment was carried out using an
		equimolar solution of Boc-Pro-Asp-NHCH3 and
		1-N-acetyl-3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-beta-D-glucopyranosyla
		mine at ambient temperature in acetonitrile. The CD spectrum obtained
		from the equimolar solution of the above two molecules (the
		''spectroscopic sum'') was identical with the CD curve obtained from
		the algebraic summation of the individually recorded CD spectra of the
		peptide and the carbohydrate moiety (''mathematical sum'').
		The global picture of the CD spectral analyses of the eight parent
		peptides with the eight N-glycopeptides revealed that in
		trifluoroethanol and acetonitrile, the side-chain modification of the
		Asn models (natural N-glycopeptide analogues) by N-glycosylation has a
		significant effect on the conformation of the carrier peptide,
		resulting in a decrease in the original type I beta-turn content.
		Simultaneously, the type II beta-turn conformational percentage
		increased to almost-equal-to 20%. Such a conformational ratio change
		seems to be larger than the expected errors arising from the CD
		analyses, and agrees with the results of MD calculations.
		N-glycosylation of Asn residues causes perturbations, not only through
		the covalent bond, but also through specific hydrogen bonds between the
		backbone and side chain atoms. CD spectroscopy, augmented by efficient
		CD curve deconvolution techniques, has proved to be a useful tool for
		studying multicomponent conformer mixtures of small linear peptides in
		solution and changes of conformational equilibria caused by
		N-glycosylation.},
	year = {1993},
	eissn = {1097-0282},
	pages = {665-685},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416; Láng, Emma/0000-0002-7638-8983}
}