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personal data approved: 2016. IV. 13.
Personal data
name Botond Penke
year of birth 1942
name of institution
doctoral school
SzTE Doctoral School of Pharmaceutical Sciences (Academic staff member)
SzTE Theoretical Medicine Doctoral School (Academic staff member)
SzTE Graduate School of Chemistry (Core member emeritus)
Council of the Doctoral School
the share of work in the different doctoral schools. SzTE Doctoral School of Pharmaceutical Sciences 16%
SzTE Theoretical Medicine Doctoral School 32%
SzTE Graduate School of Chemistry 51%
SzTE KDI1-SzTE Council of the Doctoral School 1%
accreditation statement submitted to: University of Szeged
Contact details
E-mail address penkeovrisc.mdche.u-szeged.hu
phone number +36 62 545-135
own web page
Academic title
scientific degree, title DSc
year degree was obtained 1989
discipline to which degree belongs chemistry
institution granting the degree HAS
scientific degree, title Corresponding member of Hung. Acad. of Sci.
year degree was obtained 2001
discipline to which degree belongs
institution granting the degree HAS
scientific degree, title Member of Hung. Acad. of Sci.
year degree was obtained 2007
discipline to which degree belongs chemistry
institution granting the degree HAS
Employment
2013 - University of Szeged
professor emeritus
Thesis topic supervisor
number of doctoral students supervised until now 15
number of students who fulfilled course requirements 14
students who obtained their degrees:
Julianna Jójárt PhD 2012  TMDS
(50%) István Földi PhD 2011  TMDS
Éva Klement PhD 2010  TMDS
Eszter Sipos PhD 2009  TMDS
Gábor Juhász PhD 2009  TMDS
Viktor Szegedi PhD 2007  TMDS
András Palotás PhD 2006  TMDS
(50%) Tamás Letoha PhD 2005  TMDS
Zsolt László Datki PhD 2005  TMDS
Zsolt Molnár PhD 2005  TMDS
László Hackler PhD 2004  DSPS-SzTE
Csaba Hetényi PhD 2002  DSPS-SzTE
Lajos Kovács PhD 1999  
G. László Puskás PhD 1997  
József László Varga PhD 1997  
Zoltán Székely PhD 1997  

  Thesis topic proposals
Research
research area Chemistry and biochemistry of amino acids, peptides and proteins.
research field in which current research is conducted chemistry
biology
Publications
2015

Volgyi K, Juhasz G, Kovacs Z, Penke B: Dysfunction of Endoplasmic Reticulum (ER) and Mitochondria (MT) in Alzheimer's Disease: The Role of the ER-MT Cross-Talk., CURRENT ALZHEIMER RESEARCH &: (&) p. &.
type of document: Journal paper/Article
number of independent citations: 2
language: English
2013

Veszelka S, Tóth AE, Walter FR, Datki Z, Mózes E, Fülöp L, Bozsó Z, Hellinger É, Vastag M, Orsolits B, Környei Z, Penke B, Deli MA: Docosahexaenoic acid reduces amyloid β-induced toxicity in cells of the neurovascular unit, JOURNAL OF ALZHEIMERS DISEASE 36: (3) pp. 487-501.
type of document: Journal paper/Article
impact factor: 4.174*
number of independent citations: 2
language: English
Full text 
2012

Liu SR, Liu Y, Hao WL, Wolf L, Kiliaan AJ, Penke B, Rube CE, Walter J, Heneka MT, Hartmann T, Menger MD, Fassbender K: TLR2 Is a Primary Receptor for Alzheimer's Amyloid beta Peptide To Trigger Neuroinflammatory Activation, JOURNAL OF IMMUNOLOGY 188: (3) pp. 1098-1107.
type of document: Journal paper/Article
impact factor: 5.520
number of independent citations: 25
language: English
DOI 
2012

Penke B, Toth AM, Foldi I, Szucs M, Janaky T: Intraneuronal β-amyloid and its interactions with proteins and subcellular organelles, ELECTROPHORESIS 33: (24) pp. 3608-3616.
type of document: Journal paper/Review paper
impact factor: 3.261
number of independent citations: 1
language: English
URL 
2011

Földi I, Datki ZL, Szabó Z, Bozsó Z, Penke B, Janáky T: Proteomic study of the toxic effect of oligomeric Aβ1-42 in situ prepared from 'iso-Aβ1-42', JOURNAL OF NEUROCHEMISTRY 117: (4) pp. 691-702. Paper 21388376.
type of document: Journal paper/Article
impact factor: 4.061
number of independent citations: 6
language: English
DOI 
2005

Liu Y, Walter S, Stagi M, Cherny D, Letiembre M, Schulz Schaeffer W, Heine H, Penke B, Neumann H, Fassbender K: LPS receptor (CD14): a receptor for phagocytosis of Alzheimer's amyloid peptide, BRAIN 128: (8)
type of document: Journal paper/Article
number of independent citations: 138
language: English
DOI 
2002

Hetenyi C, Szabo Z, Klement T, Datki Z, Kortvelyesi T, Zarandi M, Penke B: Pentapeptide amides interfere with the aggregation of beta-amyloid peptide of Alzheimer's disease, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 292:
type of document: Journal paper/Article
number of independent citations: 49
language: English
Full text 
2000

Harkany T, Ábrahám I, Kónya C, Nyakas C, Zarándi M, Penke B, Luiten PGM: Mechanisms of beta-amyloid neurotoxicity: Perspectives of pharmacotherapy, REVIEWS IN THE NEUROSCIENCES 11: (4)
type of document: Journal paper/Review paper
number of independent citations: 92
language: English
2000

Ishii K, Muelhauser F, Liebl U, Picard M, Kuhl S, Penke B, Bayer T, Wiessler M, Hennerici M, Beyreuther K, Hartmann T, Fassbender K: Subacute NO generation induced by Alzheimer's beta-amyloid in the living brain: reversal by inhibition of the inducible NO synthase, FASEB JOURNAL 14:
type of document: Journal paper/Article
number of independent citations: 46
language: English
DOI 
1998

Jancso G, Domoki F, Santha P, Varga J, Fischer J, Orosz K, Penke B, Becskei A, Dux M, Toth L: Beta-amyloid (1-42) peptide impairs blood-brain barrier function after intracarotid infusion in rats, NEUROSCIENCE LETTERS 253:
type of document: Journal paper/Article
number of independent citations: 49
language: English
DOI 
Number of independent citations to these publications:410 
Scientometric data
list of publications and citations
number of scientific publications that meet accreditation criteria:
435
number of scientific publications:
621
monographs and professional books:
1
monographs/books in which chapters/sections were contributed:
7 
number of independent citations to scientific publications and creative works:
6887

 
All rights reserved © 2007, Hungarian Doctoral Council. Doctoral Council registration number at commissioner for data protection: 02003/0001. Program version: 1.2318 ( 2016. XI. 26. )