@article{MTMT:1337556,
	title = {Calcium-dependent inhibition of in vitro thin-filament motility by native titin},
	url = {https://m2.mtmt.hu/api/publication/1337556},
	author = {Kellermayer, Miklós and Granzier, HL},
	doi = {10.1016/0014-5793(96)00055-5},
	journal-iso = {FEBS LETT},
	journal = {FEBS LETTERS},
	volume = {380},
	unique-id = {1337556},
	issn = {0014-5793},
	abstract = {Titin (also known as connectin) is a giant filamentous protein 
		that spans the distance between the Z- and NI-lines of the 
		vertebrate muscle sarcomere and plays a fundamental role in the 
		generation of passive tension. Titin has been shown to bind 
		strongly to myosin, making it tightly associated to the thick 
		filament in the sarcomere. Recent observations have suggested 
		the possibility that titin also interacts with actin, implying 
		further functions of titin in muscle contraction, We show - 
		using in vitro motility and binding assays - that native titin 
		interacts with both filamentous actin and reconstituted thin 
		filaments. The interaction results in the inhibition of the 
		filaments' in vitro motility. Furthermore, the thin-thin 
		filament interaction occurs in a calcium-dependent manner: 
		increased calcium results in enhanced binding of thin filaments 
		to titin and greater suppression of in vitro motility.},
	year = {1996},
	eissn = {1873-3468},
	pages = {281-286},
	orcid-numbers = {Kellermayer, Miklós/0000-0002-5553-6553}
}

@article{MTMT:1005483,
	title = {MECHANICAL-PROPERTIES OF SKINNED RABBIT PSOAS AND SOLEUS MUSCLE-FIBERS DURING LENGTHENING - EFFECTS OF PHOSPHATE AND CA2+},
	url = {https://m2.mtmt.hu/api/publication/1005483},
	author = {Stienen, G J M and Versteeg, P G A and Papp, Zoltán and Elzinga, G},
	journal-iso = {J PHYSIOL-LONDON},
	journal = {JOURNAL OF PHYSIOLOGY-LONDON},
	volume = {451},
	unique-id = {1005483},
	issn = {0022-3751},
	year = {1992},
	eissn = {1469-7793},
	pages = {503-523}
}