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Macromolecular derivatives of NAD + in heart nuclei: Poly adenosine diphosphoribose and adenosine diphosphoribose proteins
Macromolecular derivatives of NAD + in heart nuclei: Poly adenosine diphosphoribose and adenosine diphosphoribose proteins
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Macromolecular derivatives of NAD + in heart nuclei: Poly adenosine diphosphoribose and adenosine diphosphoribose proteins

Ferro, Ari M. ; Kun, Ernest

Biochemical and biophysical research communications, 1976-07, Vol.71 (1), p.150-154 [Periódico revisado por pares]

United States: Elsevier Inc

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2
Inhibition of RNA synthesis in salivary glands of [formula omitted] by 5′-methylthioadenosine
Inhibition of RNA synthesis in salivary glands of [formula omitted] by 5′-methylthioadenosine
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Inhibition of RNA synthesis in salivary glands of [formula omitted] by 5′-methylthioadenosine

Law, Ronald E. ; Sinibaldi, Ralph M. ; Cummings, Michael R. ; Ferro, Adolph J.

Biochemical and biophysical research communications, 1976-12, Vol.73 (3), p.600-606 [Periódico revisado por pares]

Elsevier Inc

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3
Inhbition of RNA synthesis in salivary glands of Drosophila melanogaster by 5'-methylthioadenosine
Inhbition of RNA synthesis in salivary glands of Drosophila melanogaster by 5'-methylthioadenosine
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Inhbition of RNA synthesis in salivary glands of Drosophila melanogaster by 5'-methylthioadenosine

Law, R E ; Sinibaldi, R M ; Cummings, M R ; Ferro, A J

Biochemical and biophysical research communications, 1976-12, Vol.73 (3), p.600-606 [Periódico revisado por pares]

United States

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4
Inactivation of S-Adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine
Inactivation of S-Adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine
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Inactivation of S-Adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine

Ferro, Adolph J. ; Vandenbark, Arthur A. ; MacDonald, Margaret R.

Biochemical and biophysical research communications, 1981-05, Vol.100 (2), p.523-531 [Periódico revisado por pares]

United States: Elsevier Inc

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5
5-Methylthioribose kinase activity in plants
5-Methylthioribose kinase activity in plants
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5-Methylthioribose kinase activity in plants

Kushad, M.M ; Richardson, D.G ; Ferro, A.J

Biochemical and biophysical research communications, 1982-01, Vol.108 (1), p.167-173 [Periódico revisado por pares]

United States: Elsevier Inc

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6
Calcium/calmodulin regulation of ATPase activity and endogenous phosphorylation of mammalian brain actomyosin
Calcium/calmodulin regulation of ATPase activity and endogenous phosphorylation of mammalian brain actomyosin
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Calcium/calmodulin regulation of ATPase activity and endogenous phosphorylation of mammalian brain actomyosin

Ferro, Jesus Aparecido ; Larson, Roy Edward

Biochemical and biophysical research communications, 1987-06, Vol.145 (3), p.1217-1224 [Periódico revisado por pares]

San Diego, CA: Elsevier Inc

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7
Secretion of a neuropeptide metabolizing enzime msimilar to endopeptidase 22.19 by glioma c 6 cells
Secretion of a neuropeptide metabolizing enzime msimilar to endopeptidase 22.19 by glioma c 6 cells
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Secretion of a neuropeptide metabolizing enzime msimilar to endopeptidase 22.19 by glioma c 6 cells

Emer Suavinho Ferro D V Tambourgi; F Gobersztein; M D Gomes; M Sucupira; M C S Armelin; Thereza Liberman Kipnis; Antonio Carlos Martins de Camargo

New York v.191, n.1 , p.275-81, 1993 Biochemical and Biophysical Research Communications

New York 1993

Localização: ICB - Inst. Ciências Biomédicas    (PC-ICB BMF SEP 1993 )(Acessar)

8
Secretion of a Neuropeptide-Metabolizing Enzyme Similar to Endopeptidase 22.19 by Glioma C6-Cells
Secretion of a Neuropeptide-Metabolizing Enzyme Similar to Endopeptidase 22.19 by Glioma C6-Cells
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Secretion of a Neuropeptide-Metabolizing Enzyme Similar to Endopeptidase 22.19 by Glioma C6-Cells

Ferro, E.S. ; Tambourgi, D.V. ; Gobersztejn, F. ; Gomes, M.D. ; Sucupira, M. ; Armelin, M.C.S. ; Kipnis, T.L. ; Camargo, A.C.M.

Biochemical and biophysical research communications, 1993-02, Vol.191 (1), p.275-281 [Periódico revisado por pares]

San Diego, CA: Elsevier Inc

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9
Dynorphin-Derived Peptides Reveal the Presence of a Critical Cysteine for the Activity of Brain Endo-oligopeptidase A
Dynorphin-Derived Peptides Reveal the Presence of a Critical Cysteine for the Activity of Brain Endo-oligopeptidase A
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Dynorphin-Derived Peptides Reveal the Presence of a Critical Cysteine for the Activity of Brain Endo-oligopeptidase A

Gomes, M.D. ; Juliano, L. ; Ferro, E.S. ; Matsueda, R. ; Camargo, A.C.M.

Biochemical and biophysical research communications, 1993-12, Vol.197 (2), p.501-507 [Periódico revisado por pares]

San Diego, CA: Elsevier Inc

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10
Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family comparison with the related recombinant endopeptidase 3.4.24.15
Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family comparison with the related recombinant endopeptidase 3.4.24.15
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Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family comparison with the related recombinant endopeptidase 3.4.24.15

V Rioli A Kato; F C Portaro; G K Cury; K Kaat; B Vincent; F Checler; A C Camargo; M J Glucksman; J L Roberts; S Hirose; Emer Suavinho Ferro

Biochemical and Biophysical Research Communications v. 250, n. 1, p. 5-11, 1998

1998

Item não circula. Consulte sua biblioteca.(Acessar)

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Deste Autor:

  1. Ferro, E
  2. Rioli, V
  3. Camargo, A
  4. Oliveira, V
  5. Machado, M

Neste Assunto:

  1. Biophysics
  2. Biochemistry & Molecular Biology
  3. Life Sciences & Biomedicine
  4. Science & Technology
  5. Animals

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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