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Hodsdon Laboratory -- Publications | ![]() |
1. Mao Y, Balkin DM, Zoncu R, Erdmann KS,
Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL
bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.
EMBO J. 2009;28(13):1831-42. PMCID: PMC2711190. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19536138
2. Keeler
C, Tettamanzi MC, Meshack S, Hodsdon ME. Contribution of individual histidines
to the global stability of human prolactin. Protein Sci. 2009;18(5):909-20.
PMCID: PMC2771294. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19384991
3. Tettamanzi
MC, Keeler C, Meshack S, Hodsdon ME. Analysis of site-specific histidine
protonation in human prolactin. Biochemistry. 2008;47(33):8638-47. PMCID:
PMC2766358. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18652486
4. Jensen
MR, Kristensen SM, Keeler C, Christensen HE, Hodsdon ME, Led JJ. Weak
self-association of human growth hormone investigated by nitrogen-15 NMR
relaxation. Proteins. 2008;73(1):161-72. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18409193
5. Keeler
C, Jablonski EM, Albert YB, Taylor BD, Myszka DG, Clevenger CV, Hodsdon ME. The
kinetics of binding human prolactin, but not growth hormone, to the prolactin
receptor vary over a physiologic pH range. Biochemistry. 2007;46(9):2398-410. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17279774
6. Murphy
JW, Cho Y, Sachpatzidis A, Fan C, Hodsdon ME, Lolis E. Structural and
functional basis of CXCL12 (stromal cell-derived factor-1 alpha) binding to
heparin. J Biol Chem. 2007;282(13):10018-27. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17264079
7. Devine
L, Thakral D, Nag S, Dobbins J, Hodsdon ME, Kavathas PB. Mapping the binding
site on CD8 beta for MHC class I reveals mutants with enhanced binding. J
Immunol. 2006;177(6):3930-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16951356
8. Tettamanzi
MC, Yu C, Bogan JS, Hodsdon ME. Solution structure and backbone dynamics of an
N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUG. Protein
Sci. 2006;15(3):498-508. PMCID: PMC2249771. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16501224
9. Guarracino
DA, Chiang HR, Banks TN, Lear JD, Hodsdon ME, Schepartz A. Relationship between
salt-bridge identity and 14-helix stability of beta3-peptides in aqueous
buffer. Org Lett. 2006;8(5):807-10. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16494446
10. Stephens
OM, Kim S, Welch BD, Hodsdon ME, Kay MS, Schepartz A. Inhibiting HIV fusion
with a beta-peptide foldamer. J Am Chem Soc. 2005;127(38):13126-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16173723
11. Mao
Y, Senic-Matuglia F, Di Fiore PP, Polo S, Hodsdon ME, De Camilli P.
Deubiquitinating function of ataxin-3: insights from the solution structure of
the Josephin domain. Proc Natl Acad Sci U S A. 2005;102(36):12700-5. PMCID:
PMC1188261. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16118278
12. Hsiao
AL, Santucci KA, Seo-Mayer P, Mariappan MR, Hodsdon ME, Banasiak KJ, Baum CR.
Pediatric fatality following ingestion of dinitrophenol: postmortem
identification of a "dietary supplement". Clin Toxicol (Phila).
2005;43(4):281-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16035205
13. Kritzer
JA, Hodsdon ME, Schepartz A. Solution structure of a beta-peptide ligand for
hDM2. J Am Chem Soc. 2005;127(12):4118-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15783163
14. Scheuermann
TH, Keeler C, Hodsdon ME. Consequences of binding an S-adenosylmethionine
analogue on the structure and dynamics of the thiopurine methyltransferase
protein backbone. Biochemistry. 2004;43(38):12198-209. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15379558
15. Kritzer
JA, Lear JD, Hodsdon ME, Schepartz A. Helical beta-peptide inhibitors of the
p53-hDM2 interaction. J Am Chem Soc. 2004;126(31):9468-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15291512
16. Devine
L, Hodsdon ME, Daniels MA, Jameson SC, Kavathas PB. Location of the epitope for
an anti-CD8alpha antibody 53.6.7 which enhances CD8alpha-MHC class I
interaction indicates antibody stabilization of a higher affinity CD8
conformation. Immunol Lett. 2004;93(2-3):123-30. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15158607
17. Keeler
C, Hodsdon ME, Dannies PS. Is there structural specificity in the reversible
protein aggregates that are stored in secretory granules? J Mol Neurosci.
2004;22(1-2):43-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14742909
18. Scheuermann
TH, Lolis E, Hodsdon ME. Tertiary structure of thiopurine methyltransferase
from Pseudomonas syringae, a bacterial orthologue of a polymorphic,
drug-metabolizing enzyme. J Mol Biol. 2003;333(3):573-85. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14556746
19. Keeler
C, Dannies PS, Hodsdon ME. The tertiary structure and backbone dynamics of
human prolactin. J Mol Biol. 2003;328(5):1105-21. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12729745
20. Sankoorikal
BJ, Zhu YL, Hodsdon ME, Lolis E, Dannies PS. Aggregation of human wild-type and
H27A-prolactin in cells and in solution: roles of Zn(2+), Cu(2+), and pH.
Endocrinology. 2002;143(4):1302-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11897686
21. Hodsdon
ME, Frieden C. Intestinal fatty acid binding protein: the folding mechanism as
determined by NMR studies. Biochemistry. 2001;40(3):732-42. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11170390
22. Steele
RA, Emmert DA, Kao J, Hodsdon ME, Frieden C, Cistola DP. The three-dimensional
structure of a helix-less variant of intestinal fatty acid-binding protein.
Protein Sci. 1998;7(6):1332-9. PMCID: PMC2144039. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9655337
23. Hodsdon
ME, Cistola DP. Ligand binding alters the backbone mobility of intestinal fatty
acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997;36(8):2278-90. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9047330
24. Hodsdon
ME, Cistola DP. Discrete backbone disorder in the nuclear magnetic resonance
structure of apo intestinal fatty acid-binding protein: implications for the
mechanism of ligand entry. Biochemistry. 1997;36(6):1450-60. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9063893
25. Hodsdon
ME, Ponder JW, Cistola DP. The NMR solution structure of intestinal fatty
acid-binding protein complexed with palmitate: application of a novel distance
geometry algorithm. J Mol Biol. 1996;264(3):585-602. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8969307
26. Hodsdon
ME, Toner JJ, Cistola DP. 1H, 13C and 15N assignments and chemical
shift-derived secondary structure of intestinal fatty acid-binding protein. J
Biomol NMR. 1995;6(2):198-210. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8589608
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