Domain Architecture of the Heme-Independent Yeast Cystathionine β-Synthase Provides Insights into Mechanisms of Catalysis and Regulation von Jhee, Kwang-Hwan, McPhie, Peter, Miles, Edith Wilson

Volltext

Constraints on the behavior of a descending ice probe due to force balance von Cassler, Bailey, Smith, Miles W.E., Durka, Michael J., Furst, Benjamin I., Hockman, Benjamin J., Ullman, Michael J.

Volltext

Experimental Validation of Cryobot Thermal Models for the Exploration of Ocean Worlds von do Vale Pereira, Paula, Durka, Michael J., Hogan, Bartholomew P., Richmond, Kristof, Smith, Miles W. E., Winebrenner, Dale P., Elam, W. Timothy, Hockman, Benjamin J., Lopez, Alberto, Tanner, Neal, Moor, Joshua, Ralston, James, Alexander, Miriam, Zimmerman, Wayne, Flannery, Nolan, Kuhl, William, Wielgosz, Sarah, Cahoy, Kerri L., Cwik, Thomas A., Stone, William C.

Volltext

Modeling a class of thermal ice probes for accessing the solar system’s ocean worlds von Durka, Michael J., Smith, Miles W.E., Ullman, Michael J., Cassler, Bailey, Otis, Richard, Cwik, Thomas A., Hockman, Benjamin J., Barry, Matthew M.

Volltext

Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium von Hyde, C C, Ahmed, S A, Padlan, E A, Miles, E W, Davies, D R

Volltext

Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism von ANDERSON, K. S, MILES, E. W, JOHNSON, K. A

Volltext

Investigation of Allosteric Linkages in the Regulation of Tryptophan Synthase:  The Roles of Salt Bridges and Monovalent Cations Probed by Site-Directed Mutation, Optical Spectrosc... von Weber-Ban, Eilika, Hur, Oscar, Bagwell, Candy, Banik, Utpal, Yang, Li-Hong, Miles, Edith W, Dunn, Michael F

Volltext

βD305A Mutant of Tryptophan Synthase Shows Strongly Perturbed Allosteric Regulation and Substrate Specificity von Ferrari, Davide, Yang, Li-Hong, Miles, Edith W, Dunn, Michael F

Volltext

The molecular basis of substrate channeling von Miles, E W, Rhee, S, Davies, D R

Volltext

A Quasi-Experimental Assessment of the Effect of Computerizing Noncognitive Paper-and-Pencil Measurements: A Test of Measurement Equivalence von King, Wesley C, Miles, Edward W

Volltext

The Reaction of Yeast Cystathionine β-Synthase Is Rate-Limited by the Conversion of Aminoacrylate to Cystathionine von Jhee, Kwang-Hwan, Niks, Dimitri, McPhie, Peter, Dunn, Michael F, Miles, Edith Wilson

Volltext

The measurement of equity sensitivity von King Jr, Wesley C., Miles, Edward W.

Volltext

The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230 von MILES, E. W, KAWASAKI, H, SYED ASHRAFUDDIN AHMED, MORITA, H, NAGATA, S

Volltext

Tryptophan synthase: A multienzyme complex with an intramolecular tunnel von Miles, Edith Wilson

Volltext

Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex von BRZOVIC, PS, SAWA, Y, HYDE, CC, MILES, EW, DUNN, MF

Volltext

Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product releas... von ZICHUN LU, NAGATA, S, MCPHIE, P, MILES, E. W

Volltext

The Importance of Employee Demographic Profiles for Understanding Experiences of Work-Family Interrole Conflicts von Eagle, Bruce W., Icenogle, Marjorie L., Maes, Jeanne D., Miles, Edward W.

Volltext

Characterization of the functional role of a flexible loop in the .alpha.-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy an... von Brzovic, Peter S., Hyde, C. Craig, Miles, Edith W., Dunn, Michael F.

Volltext

The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant re... von NAGATA, S, HYDE, C. C, MILES, E. W

Volltext

Yeast Cystathionine β-Synthase Is a Pyridoxal Phosphate Enzyme but, Unlike the Human Enzyme, Is Not a Heme Protein von Jhee, Kwang-Hwan, McPhie, Peter, Miles, Edith Wilson

Volltext