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Nersissian, A M; Mehrabian, Z B; Nalbandyan, R M; Hart, P J; Fraczkiewicz, G; Czernuszewicz, R S; Bender, C J; Peisach, J; Herrmann, R G; Valentine, J S.

Protein Sci ; 5(11): 2184-92, 1996 Nov.

Artículo en Inglés | MEDLINE | ID: mdl-8931137

13.

Cell death mechanisms in ALS.

Bredesen, D E; Wiedau-Pazos, M; Goto, J J; Rabizadeh, S; Roe, J A; Gralla, E B; Ellerby, L M; Valentine, J S.

Neurology ; 47(4 Suppl 2): S36-8; discussion S38-9, 1996 Oct.

Artículo en Inglés | MEDLINE | ID: mdl-8858049

14.

Through the glass lightly.

Valentine, J S.

Science ; 267(5204): 1614, 1995 Mar 17.

Artículo en Inglés | MEDLINE | ID: mdl-17808150

15.

Through the glass lightly.

Valentine, J S.

Science ; 267(5204): 1617, 1995 Mar 17.

Artículo en Inglés | MEDLINE | ID: mdl-17808173

16.

Letter to the editor.

Valentine, J S.

Science ; 256(5064): 1615, 1992 Jun 19.

Artículo en Inglés | MEDLINE | ID: mdl-17841076

17.

Delivering copper inside yeast and human cells.

Valentine, J S; Gralla, E B.

Science ; 278(5339): 817-8, 1997 Oct 31.

Artículo en Inglés | MEDLINE | ID: mdl-9381192

18.

A pH-dependent superoxide dismutase activity for zinc-free bovine erythrocuprein. Reexamination of the role of zinc in the holoprotein.

Pantoliano, M W; Valentine, J S; Burger, A R; Lippard, S J.

J Inorg Biochem ; 17(4): 325-41, 1982 Dec.

Artículo en Inglés | MEDLINE | ID: mdl-7161601

19.

Methods for the study of superoxide chemistry in nonaqueous solutions.

Valentine, J S; Miksztal, A R; Sawyer, D T.

Methods Enzymol ; 105: 71-81, 1984.

Artículo en Inglés | MEDLINE | ID: mdl-6328207

20.

Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis.

Lyons, T J; Gralla, E B; Valentine, J S.

Met Ions Biol Syst ; 36: 125-77, 1999.

Artículo en Inglés | MEDLINE | ID: mdl-10093924

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Human Bcl-2 reverses survival defects in yeast lacking superoxide dismutase and delays death of wild-type yeast.

Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method.

Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species.

Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis.

Engineering metal-binding sites in proteins.

The dark side of dioxygen biochemistry.

Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins.

Molecular confinement influences protein structure and enhances thermal protein stability.

A missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 A resolution.

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: plant-specific mononuclear blue copper proteins.

Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis.

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form.

Cell death mechanisms in ALS.

Through the glass lightly.

Through the glass lightly.

Letter to the editor.

Delivering copper inside yeast and human cells.

A pH-dependent superoxide dismutase activity for zinc-free bovine erythrocuprein. Reexamination of the role of zinc in the holoprotein.

Methods for the study of superoxide chemistry in nonaqueous solutions.

Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis.