Lanyi JK. Bacteriorhodopsin as a model for proton pumps. „Nature”. 6531 (375), s. 461–3, czerwiec 1995. DOI: 10.1038/375461a0. PMID: 7777054.
Varga K., Aslimovska L., Parrot I., Dauvergne MT., Haertlein M., Forsyth VT., Watts A. NMR crystallography: the effect of deuteration on high resolution 13C solid state NMR spectra of a 7-TM protein. „Biochimica et biophysica acta”. 12 (1768), s. 3029–35, grudzień 2007. DOI: 10.1016/j.bbamem.2007.09.023. PMID: 18001693.
Tittor J., Schweiger U., Oesterhelt D., Bamberg E. Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N. „Biophysical journal”. 4 (67), s. 1682–90, październik 1994. DOI: 10.1016/S0006-3495(94)80642-3. PMID: 7819500.
Brown LS., Dioumaev AK., Needleman R., Lanyi JK. Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model. „Biophysical journal”. 3 (75), s. 1455–65, wrzesień 1998. DOI: 10.1016/S0006-3495(98)74064-0. PMID: 9726947.
Oesterhelt D., Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. „Nature: New biology”. 39 (233), s. 149–52, wrzesień 1971. PMID: 4940442.
Lanyi JK. Bacteriorhodopsin as a model for proton pumps. „Nature”. 6531 (375), s. 461–3, czerwiec 1995. DOI: 10.1038/375461a0. PMID: 7777054.
Lake JA., Clark MW., Henderson E., Fay SP., Oakes M., Scheinman A., Thornber JP., Mah RA. Eubacteria, halobacteria, and the origin of photosynthesis: the photocytes. „Proceedings of the National Academy of Sciences of the United States of America”. 11 (82), s. 3716–20, czerwiec 1985. PMID: 3858845.
Racker E., Stoeckenius W. Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation. „The Journal of biological chemistry”. 2 (249), s. 662–3, styczeń 1974. PMID: 4272126.
Lanyi JK. Bacteriorhodopsin. „International review of cytology”, s. 161–202, 1999. PMID: 10212980.
Varga K., Aslimovska L., Parrot I., Dauvergne MT., Haertlein M., Forsyth VT., Watts A. NMR crystallography: the effect of deuteration on high resolution 13C solid state NMR spectra of a 7-TM protein. „Biochimica et biophysica acta”. 12 (1768), s. 3029–35, grudzień 2007. DOI: 10.1016/j.bbamem.2007.09.023. PMID: 18001693.
Henderson R., Baldwin JM., Ceska TA., Zemlin F., Beckmann E., Downing KH. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. „Journal of molecular biology”. 4 (213), s. 899–929, czerwiec 1990. PMID: 2359127.
Tittor J., Schweiger U., Oesterhelt D., Bamberg E. Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N. „Biophysical journal”. 4 (67), s. 1682–90, październik 1994. DOI: 10.1016/S0006-3495(94)80642-3. PMID: 7819500.
Luecke H. Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump. „Biochimica et biophysica acta”. 1 (1460), s. 133–56, sierpień 2000. PMID: 10984596.
Lanyi JK., Lanyi JK. Pathways of proton transfer in the light-driven pump bacteriorhodopsin. „Experientia”. 6-7 (49), s. 514–7, lipiec 1993. PMID: 11536537.
Brown LS., Dioumaev AK., Needleman R., Lanyi JK. Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model. „Biophysical journal”. 3 (75), s. 1455–65, wrzesień 1998. DOI: 10.1016/S0006-3495(98)74064-0. PMID: 9726947.