M. Yoder

发表

Unusual structural features in the parallel β-helix in pectate lyases

M. Yoder, S. Lietzke, F. Jurnak, 1993 .

Structure of pectate lyase A: comparison to other isoforms.

M. Yoder, L. Thomas, C. N. Doan, 2002, Acta crystallographica. Section D, Biological crystallography.

Purification, crystallization and X-ray analysis of crystals of pectate lyase A from Erwinia chrysanthemi

J. C. Myers, M. Yoder, C. N. Doan, 2000 .

Purification, crystallization and x-ray analysis of crystals of pectate lyase A from Exwinia chrysanthemi.

J. C. Myers, M. Yoder, C. N. Doan, 2000, Acta crystallographica. Section D, Biological crystallography.

Structure-based multiple alignment of extracellular pectate lyase sequences.

M. Yoder, S. Lietzke, F. Jurnak, 1995, Molecular plant-microbe interactions : MPMI.

Structure of PITPbeta in complex with phosphatidylcholine: comparison of structure and lipid transfer to other PITP isoforms.

M. Yoder, G. M. Helmkamp, J. Tremblay, 2005, Biochemistry.

An alpha to beta conformational switch in EF-Tu.

M. Yoder, F. Jurnak, R. Hilgenfeld, 1996, Structure.

WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).

M. Yoder, F. Jurnak, R. Hilgenfeld, 1999 .

The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution

M. Yoder, S. Lietzke, F. Jurnak, 1996, Plant physiology.

Crystallization, X-ray diffraction analysis and preliminary structure determination of the polygalacturonase PehA from Agrobacterium vitis.

M. Yoder, P. B. Vordtriede, 2008, Acta crystallographica. Section F, Structural biology and crystallization communications.

X-ray analysis of crystals of rat phosphatidylinositol-transfer protein with bound phosphatidylcholine.

M. Yoder, G. M. Helmkamp, J. Tremblay, 1999, Acta crystallographica. Section D, Biological crystallography.

New domain motif: the structure of pectate lyase C, a secreted plant virulence factor.

M. Yoder, F. Jurnak, N. Keen, 1993, Science.

Preliminary crystallographic analysis of the plant pathogenic factor, pectate lyase C from Erwinia chrysanthemi.

M. Yoder, F. Jurnak, D. A. DeChaine, 1990, The Journal of biological chemistry.

Differences in Crystal and Solution Structures of the Cytolethal Distending Toxin B Subunit

M. Yoder, J. Laity, L. Dreyfus, 2006, Journal of Biological Chemistry.

Structure of a Multifunctional Protein

M. Yoder, G. M. Helmkamp, J. Tremblay, 2001, The Journal of Biological Chemistry.

The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism)

M. Yoder, F. Jurnak, 1995, Plant physiology.

Functional Implications of Structure-Based Sequence Alignment of Proteins in the Extracellular Pectate Lyase Superfamily

B Henrissat, M. Yoder, S. Lietzke, 1995, Plant physiology.

Determinants of Specificity in the Interaction of Plants with Bacterial Pathogens

M. Yoder, F. Jurnak, C. Boyd, 1993 .

Parallel β-domains: a new fold in protein structures

J. Jenkins, M. Yoder, F. Jurnak, 1994 .

The parallel β helix and other coiled folds

M. Yoder, F. Jurnak, M D Yoder, 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

An α to β conformational switch in EF-Tu

Rolf Hilgenfeld, M. Yoder, F. Jurnak, 1996 .

Affinity purification of aminoacyl-tRNA.

M. Yoder, F. Jurnak, A. Louie, 1984, Analytical biochemistry.

The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi

M. Yoder, S. Lietzke, F. Jurnak, 1994, Plant physiology.

Progress on the Three-Dimensional Structural Determination of Trypsin-Modified EF-TU-GDP

M. Yoder, F. Jurnak, S. Heffron, 1989 .

An Essential Role of Glu-243 and His-239 in the Phosphotransfer Reaction Catalyzed by Pyruvate Dehydrogenase Kinase*

K. M. Popov, M. Yoder, A. Tuganova, 2001, The Journal of Biological Chemistry.

Program Evaluation: Food Stamps and Commodity Distribution in Rural Areas of Central Pennsylvania.

M. Yoder, M. Patrick, 1971 .

Background: The bacterial elongation factor EF-Tu recognizes and transports aminoacyl-tRNAs to mRNA-programmed ribosomes. EF-Tu shares many structural and functional properties with other GTPases whose conformations are regulated by guanine nucleotides.

M. Yoder, F. Jurnak, R. Hilgenfeld, 1996 .

Unusual structural features in the parallel beta-helix in pectate lyases.

M. Yoder, S. Lietzke, F. Jurnak, 1993, Structure.

Crystallization of Escherichia coli CdtB, the biologically active subunit of cytolethal distending toxin.

M. Yoder, L. Dreyfus, Jill S. Hontz, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.

An improved bulk purification method for Escherichia coli elongation factor, Ts.

M. Yoder, F. Jurnak, J. Lennane, 1984, Analytical Biochemistry.

Bulk preparation and crystallization of the Escherichia coli elongation factor Tu-Ts complex.

M. Yoder, F. Jurnak, C. Torres, 1985, Analytical biochemistry.