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Recent and Selected
The
Role of Protein Dynamics in Thymidylate Synthase Catalysis: Variants
of Conserved 2'-Deoxyuridine 5'-Monophosphate (dUMP)-Binding
Tyr-261. Zachary Newby, Tom T. Lee, Richard J. Morse,
Yaoquan Liu, Lu Liu, Prasanna Venkatraman, Substrate Recognition by RNA 5-Methyluridine Methyltransferases
and Pseudouridine Synthases: A Structural Perspective. Sun
Hur, Robert M. Stroud, and Janet Finer-Moore. (2006) The
Journal of Biological Chemistry Vol. 281, No. 51, pp. 38969–38973. The
Structure of a Ketoreductase Determines the Organization of the
b-Carbon Processing Enzymes of Modular Polyketide Synthases.
Adrian T. Keatinge-Clay, and Robert M. Stroud. (2006) Structure 14,
737–748. Gas Channels for Ammonia. Khademi, S., and Stroud,R.M. (2006), Invited Chapter in Royal Society of Chemistry: Structural Biology of Membrane Proteins, ed., Reinhard Grisshammer and Susan K. Buchanan. Chapter 12, 212-234. The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonia gas conduction. Khademi, S., and Stroud, R.M. (2006) Physiology (Bethesda)21: 419-429. Aquaporins: Integral Membrane Channel Proteins. Stroud, R.M., Harries, W.E.C., Lee, J, Khademi, S., and Savage, D (2006), Invited Chapter in Royal Society of Chemistry: Structural Biology of Membrane Proteins, ed., Reinhard Grisshammer and Susan K. Buchanan. Chapter 11, 195-211. On the Mechanism of Sensing Unfolded Protein in the Endoplasmic Reticulum.Credle, J.J., Finer-Moore, J.S., Papa, F.R., Stroud, R.M. and Walter, P. (2005) Proc Nat Acad Sci 102, 18773-18784 Structural Basis for Conductance by the Archaeal Aquaporin AqpM at 1.68Å. Lee, J.K., Stroud, R.M. (2005) Proc. Nat Acad Sci U S A 102, 18932-7. A unique
RNA fold in the rumA-RNA-cofactor ternary complex contributes to substrate
selectivity and enzymatic function. Lee, T., Agarwalla,
S., Stroud, R.M. (2005) Cell 120, 599-611. Targeting proteins to membranes: structure of the signal
recognition particle. Egea, P.F., Stroud, R.M., Walter, P. (2005)
Current Opinion in Structural Biology 15:213-220. De novo design of an IL-4 antagonist and its structure
at 1.9Å. LaPorte,
S.L., Forsyth, C.M., Cunningham, B.C., Miercke, L.J., Akhaven, D.,
Stroud, R.M. (2004) PNAS vol 102 no.6 1889-1894. Mechanism of association and reciprocal activation
of two GTPases. Shan, S. O., Stroud, R. M., Walter, P. (2004) PLoS
Biol 2, e320 Structure of Human Pro-Chymase: A Model for
the Activating Transition of Granule Associated Proteases. Reiling,
K.K Krucinski, J. Miercke,L.J.W. Raymond, W.W., Caughey, G.H. Stroud,
R.M. (2003) Biochemistry 42, 2616-2624. PDB accession No. 1NN6 Conformational Dynamics Along
an Enzymatic Reaction Pathway: Thymidylate Synthase, ‘the Movie.’ Robert
M. Stroud, Janet S. Finer-Moore (2003) Biochemistry 42, 239-247.
(web released Dec 17th 2002 Bi 020598i) Anisotropic Dynamics of the JE-2147-HIV Protease
complex: Drug Resistance and Thermodynamic Binding Mode Examined
in a 1.09Å Structure. Reiling, K., Endres, N., Dauber, D., Craik,
C., Stroud, R. (2002) Biochemistry 41 No 14 4582 –4594. Crystal structure of the macrocycle-forming
thioesterase domain of the erythromycin polyketide synthases: Versatility
from a unique
substrate channel. Tsai, S.-C., Miercke, L.J.W., Krucinski, J.,
Gokhale, R., Chen, Julian C.-H., Foster, P.G., Cane, D.E., Khosla,
C., and Stroud,
R.M. (2001). PNAS 98 26 14808-14813. Crystal Structure of the HIV-1 Integrase Catalytic
Core and C-Terminal Domains Presents a Model for Viral DNA Binding. Chen, J. C.-H., Krucinski, J., Miercke, L.J.W., Finer-Moore, J.S.,
Tang, A.H.,
Leavitt, A.D., and Stroud, R.M. (2000) Proc. of Natl. Acad. Sci. 97, 15 8233-8238. Functional consequences of the Kaposi's Sarcoma-associated
herpesviral protease structure: Regulation of activity and
dimerization by
conserved structural elements. Reiling, K.K., Pray, T.R.,
Craik, C.S., and Stroud, R.M. (2000) Biochemistry 39, 42 12796-803. Functional changes in the structure of the SRP GTPase
on binding GDP and Mg2+ GDP. |
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