Early hydrogen-bonding events in the folding reaction of ubiquitin.

по Briggs, M S, Roder, H
Опубликовано 1992

Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.

по Gochin, M., Roder, H.
Опубликовано 1995

Localized solution structure refinement of an F45W variant of ubiquitin using stochastic boundary molecular dynamics and NMR distance restraints.

по Laub, P. B., Khorasanizadeh, S., Roder, H.
Опубликовано 1995

Relation Between Wire Resistance and Fluid Pressure in the Transient Hot-Wire Method

по Roder, H. M., Perkins, R. A.
Опубликовано в: J Res Natl Inst Stand Technol (1989)

Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c.

по Feng, Y Q, Roder, H, Englander, S W
Опубликовано 1990

A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale.

по Shastry, M C, Luck, S D, Roder, H
Опубликовано 1998

Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.

по Zhang, Y. Z., Paterson, Y., Roder, H.
Опубликовано 1995

Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state.

по Rankin, S. E., Watts, A., Roder, H., Pinheiro, T. J.
Опубликовано 1999

Absolute Determination of the Thermal Conductivity of Argon at Room Temperature and Pressures Up to 68 MPa

по deCastro, C.A.N., Roder, H.M.
Опубликовано в: J Res Natl Bur Stand (1977) (1981)

Chemical exchange in two dimensions in the 1H NMR assignment of cytochrome c.

по Feng, Y Q, Wand, A J, Roder, H, Englander, S W
Опубликовано 1991

Determinants of protein hydrogen exchange studied in equine cytochrome c.

по Milne, J. S., Mayne, L., Roder, H., Wand, A. J., Englander, S. W.
Опубликовано 1998

A High-Temperature Transient Hot-Wire Thermal Conductivity Apparatus for Fluids

по Perkins, R. A., Roder, H. M., Nieto de Castro, C. A.
Опубликовано в: J Res Natl Inst Stand Technol (1991)

Second and Third Virial Coefficients for Hydrogen

по Goodwin, R. D., Diller, D. E., Roder, H. M., Weber, L. A.
Опубликовано в: J Res Natl Bur Stand A Phys Chem (1964)

Nanosecond flash photolysis study of carbon monoxide binding to the beta chain of hemoglobin Zürich [beta 63(E7)His leads to Arg].

по Dlott, D D, Frauenfelder, H, Langer, P, Roder, H, DiIorio, E E
Опубликовано 1983

Squalamine: an aminosterol antibiotic from the shark.

по Moore, K S, Wehrli, S, Roder, H, Rogers, M, Forrest, J N, McCrimmon, D, Zasloff, M
Опубликовано 1993

Comparison of the magnetic properties of deoxy- and photodissociated myoglobin.

по Roder, H, Berendzen, J, Bowne, S F, Frauenfelder, H, Sauke, T B, Shyamsunder, E, Weissman, M B
Опубликовано 1984

SQUID measurement of metalloprotein magnetization. New methods applied to the nitrogenase proteins.

по Day, E P, Kent, T A, Lindahl, P A, Münck, E, Orme-Johnson, W H, Roder, H, Roy, A
Опубликовано 1987

Fast events in protein folding initiated by nanosecond laser photolysis.

по Jones, C M, Henry, E R, Hu, Y, Chan, C K, Luck, S D, Bhuyan, A, Roder, H, Hofrichter, J, Eaton, W A
Опубликовано 1993

Trans/13-cis isomerization is essential for both the photocycle and proton pumping of bacteriorhodopsin.

по Chang, C H, Govindjee, R, Ebrey, T, Bagley, K A, Dollinger, G, Eisenstein, L, Marque, J, Roder, H, Vittitow, J, Fang, J M
Опубликовано 1985

VeriStrat(®) has prognostic value in advanced stage NSCLC patients treated with erlotinib and sorafenib

по Kuiper, J L, Lind, J S W, Groen, H J M, Roder, J, Grigorieva, J, Roder, H, Dingemans, A M C, Smit, E F
Опубликовано 2012