Daniela Stock | |
---|---|
Occupation | Scientist |
Academic background | |
Alma mater | Free University of Berlin, Max Planck Institute of Biochemistry |
Academic work | |
Institutions | University of New South Wales |
Main interests | Structural biology |
Daniela Stock FAA is an Australian scientist at the Victor Chang Cardiac Research Institute with a conjoint position at the University of New South Wales in Sydney,Australia. She is a structural biologist whose research has provided insight into the molecular picture of rotary ATPases. [2]
Stock was a graduate student and postdoctoral scientist at the Max Planck Institute of Biochemistry in Munich,Germany. [3]
Stock started the Structural and Computational Biology Division at the Victor Chang Cardiac Research Institute.[ citation needed ] She was elected as a Fellow of the Australian Academy of Science in 2016. [4] [5]
Stock has led ground breaking work describing molecular rotary motors which are used in the conversion of biological energy,known as rotary ATPases. [6] The Australian Academy of Science states that Stock has "redefined bioenergetics of the 1990s by solving the x-ray structure" of yeast mitochondrial ATPase. [7] Stock has worked on the structure and function of ATP synthases,as the Principal Investigator on multiple NHMRC grants . [8] She was a proponent of the development plan for use of Crystallographers using the Australian Synchrotron,to create a high-speed Macromolecular Crystallography Environment. [9]
Stock was interviewed in 2106 Challenging Ideas series from IBMCINEB,where researchers from Seminars invited speakers discuss thought provoking ideas. She commented that grant funders have short spans,and "translational research in three years is too short,meaning long term research is more valuable",as well as "good discoveries come from basic research". [1] Stock has also contributed to the International Union of Crystallography. [10]
Her selection to the Australian Academy in 2016 described her as providing 'pioneering work'. [11] The UNSW Campus Morning Mail "leadership line-up" described her as 'one of 21 Fab Fellows'. [5]
Additional publications may be found on Research Gate. [16]
Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis,a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases.
ATPases (EC 3.6.1.3,Adenosine 5'-TriPhosphatase,adenylpyrophosphatase,ATP monophosphatase,triphosphatase,SV40 T-antigen,ATP hydrolase,complex V (mitochondrial electron transport),(Ca2+ + Mg2+)-ATPase,HCO3−-ATPase,adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy,which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is:
Robert Huber is a German biochemist and Nobel laureate. known for his work crystallizing an intramembrane protein important in photosynthesis and subsequently applying X-ray crystallography to elucidate the protein's structure.
Sir John Ernest Walker is a British chemist who won the Nobel Prize in Chemistry in 1997. As of 2015 Walker is Emeritus Director and Professor at the MRC Mitochondrial Biology Unit in Cambridge,and a Fellow of Sidney Sussex College,Cambridge.
Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however,is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.
26S protease regulatory subunit 6A,also known as 26S proteasome AAA-ATPase subunit Rpt5,is an enzyme that in humans is encoded by the PSMC3 gene. This protein is one of the 19 essential subunits of a complete assembled 19S proteasome complex Six 26S proteasome AAA-ATPase subunits together with four non-ATPase subunits form the base sub complex of 19S regulatory particle for proteasome complex.
Proteasome subunit alpha type-4 also known as macropain subunit C9,proteasome component C9,and 20S proteasome subunit alpha-3 is a protein that in humans is encoded by the PSMA4 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex.
Proteasome subunit beta type-1 also known as 20S proteasome subunit beta-6 is a protein that in humans is encoded by the PSMB1 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex. In particular,proteasome subunit beta type-1,along with other beta subunits,assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. The eukaryotic proteasome recognized degradable proteins,including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome,the immunoproteasome,is the processing of class I MHC peptides.
Proteasome subunit beta type-3,also known as 20S proteasome subunit beta-3,is a protein that in humans is encoded by the PSMB3 gene. This protein is one of the 17 essential subunits that contribute to the complete assembly of the 20S proteasome complex. In particular,proteasome subunit beta type-2,along with other beta subunits,assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. The eukaryotic proteasome recognizes degradable proteins,including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes.
ATPase,subunit C of Fo/Vo complex is the main transmembrane subunit of V-type,A-type and F-type ATP synthases. Subunit C was found in the Fo or Vo complex of F- and V-ATPases,respectively. The subunits form an oligomeric c ring that make up the Fo/Vo/Ao rotor,where the actual number of subunits vary greatly among specific enzymes.
Proteasome subunit beta type-5 as known as 20S proteasome subunit beta-5 is a protein that in humans is encoded by the PSMB5 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex. In particular,proteasome subunit beta type-5,along with other beta subunits,assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. This protein contains "chymotrypsin-like" activity and is capable of cleaving after large hydrophobic residues of peptide. The eukaryotic proteasome recognized degradable proteins,including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome,the immunoproteasome,is the processing of class I MHC peptides.
26S protease regulatory subunit 4,also known as 26S proteasome AAA-ATPase subunit Rpt2,is an enzyme that in humans is encoded by the PSMC1 gene. This protein is one of the 19 essential subunits of a complete assembled 19S proteasome complex. Six 26S proteasome AAA-ATPase subunits together with four non-ATPase subunits form the base sub complex of 19S regulatory particle for proteasome complex.
26S protease regulatory subunit 6B,also known as 26S proteasome AAA-ATPase subunit Rpt3,is an enzyme that in humans is encoded by the PSMC4 gene. This protein is one of the 19 essential subunits of a complete assembled 19S proteasome complex Six 26S proteasome AAA-ATPase subunits together with four non-ATPase subunits form the base sub complex of 19S regulatory particle for proteasome complex.
Proteasome subunit alpha type-5 also known as 20S proteasome subunit alpha-5 is a protein that in humans is encoded by the PSMA5 gene. This protein is one of the 17 essential subunits that contributes to the complete assembly of 20S proteasome complex.
26S protease regulatory subunit S10B,also known as 26S proteasome AAA-ATPase subunit Rpt4,is an enzyme that in humans is encoded by the PSMC6 gene. This protein is one of the 19 essential subunits of a complete assembled 19S proteasome complex Six 26S proteasome AAA-ATPase subunits together with four non-ATPase subunits form the base sub complex of 19S regulatory particle for proteasome complex.
Proteasomal ubiquitin receptor ADRM1 is a protein that in humans is encoded by the ADRM1 gene. Recent evidences on proteasome complex structure confirmed that the protein encoded by gene ADRM1,also known in yeast as 26S Proteasome regulatory subunit Rpn13,is a subunit of 19S proteasome complex.
In the field of enzymology,a proton ATPase is an enzyme that catalyzes the following chemical reaction:
Proteasome endopeptidase complex is an enzyme. This enzyme catalyses the following chemical reaction
Jan Löwe is a German molecular and structural biologist and the Director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge,UK. He became Director of the MRC-LMB in April 2018,succeeding Sir Hugh Pelham. Löwe is known for his contributions to the current understanding of bacterial cytoskeletons.
{{cite web}}
: CS1 maint: numeric names: authors list (link)