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Principal Investigator

Heidi Hamm

Professor, Pharmacology Aileen M. Lange and Annie Mary Lyle Chair, Cardiovascular Research Professor, Ophthalmology and Visual Sciences Professor, Orthopedic Surgery and Rehabilitation

Heidi E. Hamm, Ph.D. is the Aileen M. Lange and Annie Mary Lyle Chair in Cardiovascular Research, and Professor of Pharmacology, Ophthalmology and Visual Sciences, and Orthopedics at Vanderbilt University.  This is one of the top Pharmacology departments in the country, judged by reputation, citation analysis, and NIH funding.  She oversaw an increase of the size of the Department, as well as a quintupling of its NIH funding, in her 14 years as Chair.  The Department’s strengths lie in GPCR signal transduction and neuroscience, and she has expanded it in the areas of drug discovery and structural biology of membrane proteins.  Her research focuses on the structure and function of GTP binding proteins and the molecular mechanisms of signal transduction.  G protein-mediated signaling cascades are key regulators of many physiological processes, including processes of development, differentiation, and regulation of cell division. In the brain, many key neurotransmitters and neuromodulators mediate a myriad of functions by activation of such G protein cascades. Her laboratory has been involved in studying G protein coupled signal transduction for many years.  Current areas of interest include Protease Activated Receptor signaling in the cardiovascular system and regulation of vesicular exocytosis mediated by Gi/o-coupled presynaptic receptors by Gbg subunit binding to SNAREs.


Dr. Hamm obtained her Ph.D. in 1980 from the Department of Zoology at the University of Texas-Austin and did postdoctoral training in the University of Wisconsin-Madison from 1980-1983. Her initial research centered around circadian clocks and melatonin synthesis in the avian retina; her postdoctoral work investigated the role of the G protein transducin in visual transduction using blocking monoclonal antibodies. She held faculty appointments at the University of Illinois at Chicago School of Medicine and Northwestern University before moving to Vanderbilt in 2000.

Postdoc Fellow, University of Wisconsin – Madison
Ph.D., University of Texas, Austin
B.A., Atlantic Union College

Current Members

Jackson B Cassada

Research Assistant, Pharmacology,


2016 East Tennessee State University, B.S. (Microbiology)

2020 Tennessee State University, M.S. (Biochemistry)

Anna Eitel

PhD Candidate, Biochemistry,


Moutoussamy, E.E., Waheed, Q., Binford, G.J., Khan, H.M., Moran, S.M., Eitel, A.R., Cordes, M.H.J., and Reuter, N. (2021) Specificity of Loxosceles clade phospholipase D enzymes for choline-containing lipids: role of a conserved aromatic cage. bioRxiv. DOI:

Chawla, U., Perera, S.D.M.C., Fried, S.D.E., Eitel, A.R., Weerasinghe, N., Mertz, B., Pitman, M.C., Struts, A.V., Brown, M.F. (2020) Activation of the G-Protein–Coupled Receptor Rhodopsin by Water. Angew. Chem. 60: 2288-2295. DOI: 10.1002/ange.202003342

Evans, H.G., Guthrie, J.W., Jujjavarapu, M., Hendrickson, N., Eitel, A., Park, Y., Garvey, J., Newman, R., Esckilsen, D., and Heyl, D.L. (2017) D-Amino Acid Analogues of the Antimicrobial Peptide CDT Exhibit Anti- Cancer Properties in A549, a Human Lung Adenocarcinoma Cell Line. Protein Pept. Lett. 24: 590-598. DOI: 10.2174/0.929866524666170621093647.



Kevin Erreger

Sr Research Specialist, Pharmacology

2004 Emory University Ph.D. (Neuroscience)
1998 State University of New York at Buffalo B.S. (Biophysics)

Research Interests:
My background is in biophysics and physiology and my current research interests focus on translational research and drug development. I coordinate multiple collaborative projects focused on Protease Activated Receptor 4 (PAR4). We are developing novel PAR4 antagonists for clinical use and also as tools for mouse models of disease. We view PAR4 as a relevant target to investigate in disease processes with inflammatory pathology. Currently, we are investigating the role of PAR4 in Azlheimer’s, kidney disease, and COVID-19.

Yim YY, McDonald WH, Betke KM, Kaya A, Hyde K, Erreger K, Gilsbach R, Hein L, Hamm HE.
Specificities of Gβγ subunits for the SNARE complex before and after stimulation of α2a-adrenergic receptors. Sci Signal. 2021 Dec 21;14(714):eabc4970.

Herborg F, Jensen KL, Tolstoy S, Arends NV, Posselt LP, Shekar A, Aguilar JI, Lund VK, Erreger K, Rickhag M, Lycas MD, et al., Identifying dominant-negative actions of a dopamine transporter variant in patients with parkinsonism and neuropsychiatric disease. JCI Insight, 2021. 6(18).

Pulley JM, Rhoads JP, Jerome RN, Challa AP, Erreger K, Joly MM, Lavieri RR, Perry KE, Zaleski NM, Shirey-Rice JK, and Aronoff DM, Using What We Already Have: Uncovering New Drug Repurposing Strategies in Existing Omics Data. Annu Rev Pharmacol Toxicol, 2020. 60: p. 333-352.

Campbell NG, Shekar A, Aguilar JI, Peng D, Navratna V, Yang D, Morley AN, Duran AM, Galli G, O’Grady B, Ramachandran R, Erreger K, et al., Galli A, Structural, functional, and behavioral insights of dopamine dysfunction revealed by a deletion in SLC6A3. Proc Natl Acad Sci U S A, 2019. 116(9): p. 3853-3862.
Reddy IA, Smith NK, Erreger K, Ghose D, Saunders C, Foster DJ, Turner B, Poe A, Albaugh VL, McGuinness O, Hackett TA, et al., Bile diversion, a bariatric surgery, and bile acid signaling reduce central cocaine reward. PLoS Biol, 2018. 16(7): p. e2006682.

Reddy IA, Pino JA, Weikop P, Osses N, Sorensen G, Bering T, Valle C, Bluett RJ, Erreger K, Wortwein G, Reyes JG, et al., Glucagon-like peptide 1 receptor activation regulates cocaine actions and dopamine homeostasis in the lateral septum by decreasing arachidonic acid levels. Transl Psychiatry, 2016. 6: p. e809.
Hamilton PJ, Shekar A, Belovich AN, Christianson NB, Campbell NG, Sutcliffe JS, Galli A, Matthies HJ, and Erreger K, Zn(2+) reverses functional deficits in a de novo dopamine transporter variant associated with autism spectrum disorder. Mol Autism, 2015. 6: p. 8.

Dadalko OI, Siuta M, Poe A, Erreger K, Matthies HJ, Niswender K, and Galli A, mTORC2/rictor signaling disrupts dopamine-dependent behaviors via defects in striatal dopamine neurotransmission. J Neurosci, 2015. 35(23): p. 8843-54.
Cartier E, Hamilton PJ, Belovich AN, Shekar A, Campbell NG, Saunders C, Andreassen TF, Gether U, Veenstra-Vanderweele J, Sutcliffe JS, Ulery-Reynolds PG, et al., Erreger K, Galli A, Rare autism-associated variants implicate syntaxin 1 (STX1 R26Q) phosphorylation and the dopamine transporter (hDAT R51W) in dopamine neurotransmission and behaviors. EBioMedicine, 2015. 2(2): p. 135-146.

Ng J, Zhen J, Meyer E, Erreger K, Li Y, Kakar N, Ahmad J, Thiele H, Kubisch C, Rider NL, Morton DH, et al., Dopamine transporter deficiency syndrome: phenotypic spectrum from infancy to adulthood. Brain, 2014. 137(Pt 4): p. 1107-19.
Hansen FH, Skjorringe T, Yasmeen S, Arends NV, Sahai MA, Erreger K, Andreassen TF, Holy M, Hamilton PJ, Neergheen V, Karlsborg M, et al., Missense dopamine transporter mutations associate with adult parkinsonism and ADHD. J Clin Invest, 2014. 124(7): p. 3107-20.

Hamilton PJ, Belovich AN, Khelashvili G, Saunders C, Erreger K, Javitch JA, Sitte HH, Weinstein H, Matthies HJG, and Galli A, PIP2 regulates psychostimulant behaviors through its interaction with a membrane protein. Nat Chem Biol, 2014. 10(7): p. 582-589.

Bowton E, Saunders C, Reddy IA, Campbell NG, Hamilton PJ, Henry LK, Coon H, Sakrikar D, Veenstra-VanderWeele JM, Blakely RD, Sutcliffe J, et al., Erreger K, Galli A, SLC6A3 coding variant Ala559Val found in two autism probands alters dopamine transporter function and trafficking. Transl Psychiatry, 2014. 4: p. e464.

Hamilton PJ, Campbell NG, Sharma S, Erreger K, Herborg Hansen F, Saunders C, Belovich AN, Consortium NAAS, Sahai MA, Cook EH, Gether U, et al., De novo mutation in the dopamine transporter gene associates dopamine dysfunction with autism spectrum disorder. Mol Psychiatry, 2013. 18(12): p. 1315-23.

Hamilton PJ, Campbell NG, Sharma S, Erreger K, Hansen FH, Saunders C, Belovich AN, Sahai MA, Cook EH, Gether U, McHaourab HS, et al., Drosophila melanogaster: a novel animal model for the behavioral characterization of autism-associated mutations in the dopamine transporter gene. Mol Psychiatry, 2013. 18(12): p. 1235.

Graham DL, Erreger K, Galli A, and Stanwood GD, GLP-1 analog attenuates cocaine reward. Mol Psychiatry, 2013. 18(9): p. 961-2.

Dixit M, Kim S, Matthews GF, Erreger K, Galli A, Cobb CE, Hustedt EJ, and Beth AH, Structural arrangement of the intracellular Ca2+ binding domains of the cardiac Na+/Ca2+ exchanger (NCX1.1): effects of Ca2+ binding. J Biol Chem, 2013. 288(6): p. 4194-207.

Erreger K, Davis AR, Poe AM, Greig NH, Stanwood GD, and Galli A, Exendin-4 decreases amphetamine-induced locomotor activity. Physiol Behav, 2012. 106(4): p. 574-8.

Bowton E, Saunders C, Erreger K, Sakrikar D, Matthies HJ, Sen N, Jessen T, Colbran RJ, Caron MG, Javitch JA, Blakely RD, et al., Dysregulation of dopamine transporters via dopamine D2 autoreceptors triggers anomalous dopamine efflux associated with attention-deficit hyperactivity disorder. J Neurosci, 2010. 30(17): p. 6048-57.

Erreger K and Traynelis SF, Zinc inhibition of rat NR1/NR2A N-methyl-D-aspartate receptors. J Physiol, 2008. 586(3): p. 763-78.

Erreger K, Grewer C, Javitch JA, and Galli A, Currents in response to rapid concentration jumps of amphetamine uncover novel aspects of human dopamine transporter function. J Neurosci, 2008. 28(4): p. 976-89.

Chen PE, Geballe MT, Katz E, Erreger K, Livesey MR, O’Toole KK, Le P, Lee CJ, Snyder JP, Traynelis SF, and Wyllie DJ, Modulation of glycine potency in rat recombinant NMDA receptors containing chimeric NR2A/2D subunits expressed in Xenopus laevis oocytes. J Physiol, 2008. 586(1): p. 227-45.

Binda F, Dipace C, Bowton E, Robertson SD, Lute BJ, Fog JU, Zhang M, Sen N, Colbran RJ, Gnegy ME, Gether U, et al., Erreger K, Galli A, Syntaxin 1A interaction with the dopamine transporter promotes amphetamine-induced dopamine efflux. Mol Pharmacol, 2008. 74(4): p. 1101-8.

Erreger K, Geballe MT, Kristensen A, Chen PE, Hansen KB, Lee CJ, Yuan H, Le P, Lyuboslavsky PN, Micale N, Jorgensen L, et al., Subunit-specific agonist activity at NR2A-, NR2B-, NR2C-, and NR2D-containing N-methyl-D-aspartate glutamate receptors. Mol Pharmacol, 2007. 72(4): p. 907-20.

Dravid SM, Erreger K, Yuan H, Nicholson K, Le P, Lyuboslavsky P, Almonte A, Murray E, Mosely C, Barber J, French A, et al., Subunit-specific mechanisms and proton sensitivity of NMDA receptor channel block. J Physiol, 2007. 581(Pt 1): p. 107-28.
Yuan H, Erreger K, Dravid SM, and Traynelis SF, Conserved structural and functional control of N-methyl-D-aspartate receptor gating by transmembrane domain M3. J Biol Chem, 2005. 280(33): p. 29708-16.

Erreger K and Traynelis SF, Allosteric interaction between zinc and glutamate binding domains on NR2A causes desensitization of NMDA receptors. J Physiol, 2005. 569(Pt 2): p. 381-93.

Erreger K, Geballe MT, Dravid SM, Snyder JP, Wyllie DJ, and Traynelis SF, Mechanism of partial agonism at NMDA receptors for a conformationally restricted glutamate analog. J Neurosci, 2005. 25(34): p. 7858-66.

Erreger K, Dravid SM, Banke TG, Wyllie DJ, and Traynelis SF, Subunit-specific gating controls rat NR1/NR2A and NR1/NR2B NMDA channel kinetics and synaptic signalling profiles. J Physiol, 2005. 563(Pt 2): p. 345-58.

Erreger K, Chen PE, Wyllie DJ, and Traynelis SF, Glutamate receptor gating. Crit Rev Neurobiol, 2004. 16(3): p. 187-224.
Zheng F, Erreger K, Low CM, Banke T, Lee CJ, Conn PJ, and Traynelis SF, Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A. Nat Neurosci, 2001. 4(9): p. 894-901.

Mott DD, Erreger K, Banke TG, and Traynelis SF, Open probability of homomeric murine 5-HT3A serotonin receptors depends on subunit occupancy. J Physiol, 2001. 535(Pt 2): p. 427-43.


Joseph Parello

Visiting Scholar, Pharmacology

MS, Physics/Mathematics (1959)
MS, Chemistry (1960)

Research Interests: 
Based on a multidisciplinary approach (synthetic methods in organic chemistry; biophysical and computational methods in structural biology: NMR, crystallization, optical spectrocopies; neutron scattering; homology modeling) our research is focused on two major pharmacological challenges: (i) regulation of chromatin acetylation through a synthetic strategy with novel inhibitors that synergize with major antitumoral drugs in cancer biology and therapy; (ii) search for antidepressant drugs of natural origin (terpenes) selectively acting on the kappa-opioid receptor.


Gupta A, Gomes I, Bobeck EN, Fakira AK, Massaro NP, Sharma I, Cavé A, Hamm HE, Parello J, Devi LA. Collybolide is a novel biased agonist of κ-opioid receptors with potent antipruritic activity. Proc Natl Acad Sci U S A. 2016 May 24;113(21):6041-6. PubMed Central PMCID: PMC4889365.

Phyllochrysine et sécurine, alcaloïdes du Phyllantus discoides Muell. Arg. (Euphorbiacées), J. Parello , A. Melera et R. Goutarel. Bull. Soc. Chim., 1963 , 898 -910.

Couplage entre spins nucléaires en résonance magnétique nucléaire (RMN) et méthode de double résonance . J. Parello . Bull. Soc. Chim., 1964, 2033 -2062.

The structure of Sugar Osazones . L. Mester , E .Moczar and J . Parello . J. Amer. Chem. Soc., 1965 , 87, 596-599.

Etude des spectres de masse de la sécurinine et dérivés d’hydrogénation. H.E.Audier et J.Parello. Bull. Soc. Chim., 1968,1552-1559.

Alcaloïdes stéroïdiques -LXXV. Etude dichroïque du chromophore nitrone . J.Parello et X.Lusinchi. Tetrahedron. 1968, 24, 6747-6754.

Alcaloïdes steroïdiques LXXVIII . Etude dichroïque du chromophore amine tertiaire aliphatique . J. Parello et F. Picot . Tetrahedron Letters, 1968, 9, 5083-5086.

Alcaloides steroïdiques LXXIX – Photochimie de nitrones et d’oxazirannes steroïdiques . J. Parello , R . Beugelmans, P. Milliet et X. Lusinchi . Tetrahedron Letters, 1968, 9, 5081-5092.

N.M.R. studies on nitrogen-containing sugar derivatives substituted by15N. Part I. The nature of the chelate ring in sugar osazones . L.Mester, G.Vass, A.Stephen and J.Parello. Tetrahedron Letters,1968, 4053-4056.

Conformational studies on muscular parvalbumins. I. Optical rotatory dispersion and circular dichroism analysis. Parello J; Pechere J F Biochimie 1971, 53, 1079-83.

Oxazirannes. Obtention de lactames N-substitués par photolyse d’oxazirannes. E. Desherces, M. Rivière, J. Parello et A. Lattes, C.R.Acad. Sci. Paris, 1972, 275(C), 581-584.

Model studies in relation to the molecular structure of chromatin. Gourévitch M, Puigdomènech P, Cavé A; Etienne G; Méry J, Parello J Biochimie 1974, 56, 967-85.

Isolation and structural analysis of collybolide, a novel sesquiterpene extracted from Collybia maculata. Carbon-13 NMR of lactones. Bui, A. M.; Cave, A.; Janot, M. M.; Parello, J.; Potier, P.; Scheidegger, U. Tetrahedron 1974, 30, 1327-36.

Photolysis of oxaziridines. IV. Regioselectivity and solvent effects in the opening of oxaziridines at the spiranic junction. Oliveros-Desherces, E.; Riviere, M.; Parello, J.; Lattes, A. Tetrahedron Lett. 1975, 851-854.

Conformation mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residues. Cavé A; Dobson CM; Parello J; Williams R J FEBS Lett. 1976, 65,190-194.

Superstructure of linear duplex DNA. Vollenweider, H. J.; Koller, T.; Parello, J.; Sogo, J. M. Proc. Nat. Acad. Sci. USA 1976, 73, 4125-4129.

A calcium-43 NMR study of the binding of calcium to parvalbumins. Parello, J.; Lilja, H.; Cave, A.; Lindman, B. FEBS Lett. 1978, 87, 191-195.

Chemical studies on histone acetylation using a synthetic peptide fragment of histone H4. Kervabon A; Parello J; Méry J FEBS Lett. 1979, 98, 152-156.

Na+ binding to parvalbumins studied by 23Na NMR. Parello J; Reimarsson P; Thulin E; Lindman B FEBS Lett. 1979, 100, 153-156.

Magnesium ion binding to parvalbumins studied by magnesium-25 and cadmium-113 NMR spectroscopy. Cave, A.; Parello, J.; Drakenberg, T.; Thulin, E.; Lindman, B. FEBS Lett. 1979, 100, 148-52.

Enzymatic deacetylation of a synthetic peptide fragment of histone H4. Kervabon A; Mery J; Parello J FEBS Lett. 1979, 106, 93-6.

Dynamic aspects of the structure of globular proteins by high resolution NMR spectroscopy. The fluid-like structure of the internal hydrophobic core of muscular parvalbumins. A. Cavé and J. Parello, in Les Houches, Session XXXIII, 1979. Membranes and Intercellular Communication, North-Holland Publishing Company, 1981, 197-227.

Effect of cations on the acetylation of chromatin in vitro. Dod B; Kervabon A; Parello J Eur. J. Biochem. 1982, 121, 401-405.

NMR studies of muscle proteins. Ribeiro A; Parello J; Jardetzky O. Prog. Biophys. Molec. Biol. 1984, 43, 95-160.

Metal-ion binding to parvalbumin. A 113Cd-n.m.r. study of the binding of different lanthanide ions. Drakenberg T; Sward M; Cave A; Parello J Biochem. J. 1985, 227, 711- 7.

A chromatin core particle obtained by selective cleavage of histones by clostripain. Dumuis-Kervabon A; Encontre I; Etienne G; Jauregui-Adell J; Mery J; Mesnier O; Parello J. EMBO J. 1986, 5, 1735-42.

Chromatin core particle obtained by selective cleavage of histones H3 and H4 by clostripain. Encontre I; Parello J. J. Mol. Biol. 1988, 202, 673-6.

Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius). Declercq J P; Tinant B; Parello J; Etienne G; Huber R., J. Mol. Biol., 1988, 202, 349-53.

Two-dimensional 1 H nuclear magnetic resonance study of pike pl 5.0 parvalbumin (Esox lucius). Sequential resonance assignments and folding of the polypeptide chain. Erratum in: J Mol Biol 1989 Aug 20;208(4):723-4 Padilla A; Cave A; Parello J., J. Mol. Biol., 1988, 204, 995-1017.

Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments. Declercq JP, Tinant B, Parello J, Rambaud J. J Mol Biol. 1991, 220,1017-1039.

Crystallization of catalytic subunit of adenosine cyclic monophosphate-dependent protein kinase. Zheng JH, Knighton DR, Parello J, Taylor SS, Sowadski JM. Methods Enzymol. 1991, 200, 508-521.

Mass spectrometry of proteins: studies of parvalbumins by plasma desorption, laser desorption and electrospray mass spectrometry. Roepstorff, P.; Klarskov, K.; Andersen, J.; Mann, M.; Vorm, O.; Etienne, G.; Parello, J. International Journal of Mass Spectrometry and Ion Processes 1991, 111, 151-172.

Homonuclear Three-Dimensional 1H NMR Spectroscopy of Pike Parvalbumin. Comparison of Short- and Medium-Range NOEs from 2D and 3D NMR. A. Padilla, G.W. Vuister, R. Boelens, G.J. Kleywegt, A. Cavé, J. Parello and R. Kaptein. J. Am. Chem. Soc. 1990, 112, 5024-5030.

Reisman, J., Jariel-Encontre, I., Hsu, V.L., Parello, J., Geiduschek, E.P., Kearns, D.R. (1991). Improving Two-dimensional 1H NMR NOESY Spectra of a Large Protein by Selective Deuteriation. J. Amer. Chem. Soc. 113, 2787-2789.

Crystallization studies of the catalytic subunit of cAMP-dependent protein kinase: crystals of murine recombinant catalytic subunit and a mutant, Cys 343—-Ser 1 diffract to 2.7 A resolution. Zheng J H; Knighton DR; Xuong N H; Parello J; Taylor S S; Sowadski J M., Acta Cryst. B, 1992, 48 ( Pt 2) 241-4.

Crystal structure of the unique parvalbumin component from muscle of the leopard shark (Triakis semifasciata). The first X-ray study of an alpha-parvalbumin. Roquet F; Declercq J P; Tinant B; Rambaud J; Parello J J Mol Biol 1992, 223, 705-20.

A 1 H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-Iabeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer. Reisman J M; Hsu V L; Jariel-Encontre I; Lecou C; Sayre M H; Kearns DR; Parello J., Eur. J. Biochem. 1993, 213, 865- 73.

Regioselective synthesis of inhibitors of histone acetyltransferase covalently linking spermidine to the S-terminus of coenzyme A. G. Roblot, R. Wylde, A. Martin and J. Parello,Tetrahedron 1993, 49, 6381-6398.

Proton and nitrogen NMR sequence-specific assignments and secondary structure determination of the Bacillus subtilis SPO1-encoded transcription factor 1. Jia X; Reisman J M; Hsu V L; Geiduschek E P; Parello J; Kearns D.R. Biochemistry 1994, 33, 8842-52.

Crystals of the cell-binding module of fibronectin obtained from a series of recombinant fragments differing in length. Dickinson CD; Gay DA; Parello J; Ruoslahti E; Ely K.R., J. Mol Biol 1994, 238, 123-7.

Evidence indicating proximity in the nucleosome between the histone H4 N termini and the globular domain of histone H1. Baneres J L; Essalouh L; Jariel-Encontre I; Mesnier O; Garrod S; Parello J., J. Mol. Biol. 1994, 243, 48-59.

Dynamics of a globular protein as studied by neutron scattering and solid-state NMR. Zanotti, J.-M.; Bellissent-Funel, M.-C.; Parello, J., Physica B: Condensed Matter 1997, 234-236,  228-230.

The N tails of histones H3 and H4 adopt a highly structured conformation in the nucleosome. Baneres J L; Martin A; Parello J. J. Mol. Biol., 1997, 273, 503-8.

The cation-binding domain from the alpha subunit of integrin alphaS beta1 is a minimal domain for fibronectin recognition. Baneres J L; Roquet F; Green M; LeCalvez H; Parello J., J. Biol. Chem. 1998, 273, 24744-53.

Ca2+/Mg2+ ex change in parvalbumin and other EF-hand proteins. A theoretical study. Allouche D; Parello J; Sanejouand Y H., J. Mol. Biol. 1999, 285, 857-73.

Two well-defined motifs in the cAMP-dependent protein kinase inhibitor (PKlalpha) correlate with inhibitory and nuclear export function. Hauer J A; Sarthe P; Taylor S S; Parello J; Padilla A. Prot. Science, 1999, 8, 545-53.

\Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin. Zanotti J M; Bellissent-Funel MC; Parello J., Biophys. J. 1999, 76, 2390-411.

Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core. Declercq J P; Evrard C; Lamzin V; Parello J Prot. Science 1999, 8, 2194-204.

NMR and Hydration of Biomacromolecules in Aqueous Solutions. J. Parello, in Hydration Processes in Biology (M.-C. Bellissent-Funel, ed.), IOS Press, 1999, 379-385.

A minimized human integrin alpha(5)beta(1) that retains ligand recognition. Baneres J L; Roquet F; Martin A; Parello J., J. Biol. Chem. 2000, 275, 5888-903.

Durand D; Hullot P; Vidal J P; Girard J P; Baneres J L; Parello J; Muller A; Bonne C; Rossi J C., Leukotriene B4 photoaffinity probes: design, synthesis and evaluation of new arylazide-1,3-disubstituted cyclohexanes. Bioorg. Med. Chem. Lett. 2000, 10, 811-4.

Photochemical rearrangement of oxaziridines and nitrones in the hexahydroindole series: a convenient synthetic route to 1-azabicyclo[5.2.0]nonan-2-ones as novel RGD mimetics. Bourguet E; Baneres J L; Girard J P; Parello J; Vidal J P; Lusinchi X; Declercq J P., Org. Lett. 2001, 3, 3067-70.

A neutron scattering study of the histone sub-assemblies within the nucleosome core particle. J.-L. Banères, J. Parello, G. Zaccaï and D. Svergun, The ILL millenium symposium & european user meeting, Proceedings, ILL Neutrons for Science, 2001, 55-57.

Bourguet E, Baneres JL, Parello J, Lusinchi X, Girard JP, Vidal JP. Nonpeptide RGD antagonists: A novel class of mimetics, the 5,8-disubstituted 1-azabicyclo[5.2.0]nonan-2-one lactam. Bioorg Med Chem Lett. 2003;13,1561-4.

Banères, J.-L., Martin, A., Hullot, P., Girard, J.-P., Rossi, J.-C., & Parello, J. (2003). Structure-based analysis of GPCR function. Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol., 329, 801-814.

Banères, J.-L., & Parello, J. (2003). Structure-based analysis of GPCR function. Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J. Mol. Biol., 329, 815-829.

Keya Bandyopadhyay, Casey Lee, Ali Haghighi, Jean-Louis Banères, Joseph Parello and Ruth A. Gjerset (2007). Serine Phosphorylation-Dependent Coregulation of Topoisomerase I by the p14ARF Tumor Suppressor. Biochemistry, 46 (49), 14325 -14334.

Preininger AM, Parello J, Meier SM, Liao G, Hamm HE (2008) Receptor-mediated changes at the myristoylated amino terminus of Galpha(i) proteins.Biochemistry 47,10281-93.

Martin, Damian, Laguerre, Parello, Pucci, Serre, Mary, Marie & Baneres (2009). Engineering a G protein-coupled receptor for structural studies: Stabilization of the BLT1 receptor ground state. Protein Science, 18, 727-734.