Laboratory for protein dynamics

The research activities of the laboratory are based on research and understanding of protein dynamics as the key determinant for the formation and development of tumors, metastasis, determining the therapeutic target and the basis for their response to therapy.

Neda Slade

Head

Ph.D. Neda Slade

+385 1 456 0926
Fax: +385 1 456 1010
left right

The main LPD research directions are:

  1. Identifying the tumor suppressor protein p53 interaction partners in melanoma, with an emphasis on the p53/p73 isoforms as well as NME / nm23 / NDPK and Gli protein family; and detecting the roles of identified proteins in context of p53 activity in melanoma.
  2. Studying p53 mutations in the context of endemic nephropathy, an environmental disease, which cause is related to the occurrence of the upper urinary tract carcinoma.
  3. Studying the influence of nucleoside diphosphate kinase subunits, Nme1 and Nme2, in cellular migration, and their potential synergistic role in this process in vitro. The members of the group II Nme proteins, in particular, Nme 6, including its localization and biological role in the cell will be investigated.
  4. Studying the effect of potentially neuroprotective compounds on the phosphorylation of tau protein in the culture of P19 neurons.

Anđela Horvat
PhD

Postdoctoral fellow
+385 1 456 0997
1752 1754

Bastien Lucien Jean Proust

+385 1 456 0996
1754 1512

Maja Herak Bosnar
PhD

senior research associate
+385 1 456 0996
1752

Maja Jazvinšćak Jembrek
PhD

Research Associate
+385 1 456 0997
1753

Neda Slade
Ph.D.

senior scientist
+385 1 456 0926
1511

Nikolina Hanžić
M.Sc.

PhD student (assistant)
1754

Nikolina Škrobot Vidaček
Ph.D.

senior assistant
1754
Nemo6 - Structure, Function and Evolution of Nme6/Nm23-H6 Protein

Nemo6 - Structure, Function and Evolution of Nme6/Nm23-H6 Protein

Glavni istraživač / voditelj: Maja Herak Bosnar

Nucleoside-diphosphate kinases (Nme/Nm23/NDPK) constitute a family of evolutionary conserved enzymes involved in many crucial biological processes. The family consists of ten members divided in two groups. Group I, which encompasses Nme1-Nme4, has been extensively studied, especially Nme1 in the context of metastasis formation. The Group II members are evolutionary older, especially the Nme5, Nme6 and Nme7 and little is known about their structure and function. Numerous proteins from evolutionary distinct organisms exhibit extraordinary similarity in primary structure with their orthologues in mammals including humans, as do their predicted secondary and tertiary structures. Therefore, it is presumed that they have similar or identical biochemical and biological functions. Building upon our previous work on the human and sponge Nme family proteins, the proposed project will focus on resolving the structure, as well as biochemical and biological functions of the human Nme6 and its changes during evolution. We will employ a range of biochemical methods and combine them with modern molecular biology methods supported by advanced confocal microscopy techniques.

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ProNetMel - New Protein Networks for Novel Therapeutic Avenues in Human Melanoma

ProNetMel - New Protein Networks for Novel Therapeutic Avenues in Human Melanoma

Glavni istraživač / voditelj: Neda Slade

The main focus of this project is to reveal interactions of p53 with protein partners in melanoma that are capable of modifying its function. We are particularly interested in possible interactions of p53 with family members, namely p53 and p73 isoforms, with nm23, especially nm23-H1 and nm23-H2, and Gli family of proteins.

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