BIOCH.eu

ABOUT US

RESEARCH INTERESTS

• Structure-function studies of intramembrane electron transport proteins: plasma membrane NADPH-oxidases Nox and Rboh, plant cytochrome b6f complex.
  
  
• Function of plant beta-lactamase homologs.
  
  
• Plant oxidative stress and environmental adaptation: host-patogen interaction in apple scab disease.

 LABORATORY TECHNIQUE EXPERIENCE

• Protein chemistry techniques: chromatography applications in protein purification and analysis (liquid and affinity chromatography methods, HPLC); electrophoretic protein separation (SDS-PAGE, 2-DE), immunoblotting and ELISA; absorbtion sprectroscopy methods, including kinetic protein activity analysis; protein proteolytic digestion analysis; MALDI and basic ESI mass-spectrometry and data analysis; polyclonal antibody production; antibody epitope mapping using phage display library.
  
  
• Molecular biology techniques: PCR, RT-PCR, sequencing, gene cloning and protein expression in procaryotic and eucaryotic (mammalian, insect) systems.
  
  
• Microscopy techniques: fluorescent microscopy, flow-cytometry, Fluorescence recovery after photo-bleaching (FRAP), basic scanning electron microscopy skills.
  
  
• Cell culture techniques: bacterial, mammalian, insect cell cultures; mammalian cell bioreactor culture.

COLLABORATION

• Dr Julius Liobikas, Institute for Biomedical Research of Medical Academy, Lithuanian University of Health Sciences, Kaunas, Lithuania.
  
  
• Subhash Mohan Agarwal, Institute of Cytology and Preventive Oncology, Indian Council of Medical Research, Noida, India.
  
  
• Dr Odeta Buzaite and Dr Sarunas Asmontas, Department of Biology, Vytautas Magnus University, Kaunas, Lithuania.

SELECTED PUBLICATIONS

• Cramer WA, Zakharov SD, Saif Hasan S, Zhang H, Baniulis D, Zhalnina MV, Soriano GM, Sharma O, Rochet JC, Ryan C, Whitelegge J, Kurisu G, Yamashita E.
  Membrane proteins in four acts: Function precedes structure determination. Methods, 2011, 55(4): 415-420.
   
• Baniulis D, Zhang H, Zakharova T, Hasan SS, Cramer WA.
  Purification and crystallization of the cyanobacterial cytochrome b6f complex. Methods Mol. Biol., 2011, 684: 65-77.
   
• Ryan CM, Souda P, Bassilian S, Ujwal R, Zhang J, Abramson J, Ping P, Durazo A, Bowie JU, Hasan SS, Baniulis D, Cramer WA, Faull KF, Whitelegge JP.
  Post-translational modifications of integral membrane proteins resolved by top-down Fourier-transform mass spectrometry with collisionally activated dissociation. Mol. Cell. Proteomics, 2010, 9(5): 791-803.
   
• Twigg AI, Baniulis D, Cramer WA, Hendrich MP.
  EPR detection of an O(2) surrogate bound to heme c(n) of the cytochrome b(6)f complex. J. Am. Chem. Soc., 2009, 131(35): 12536-12537
   
• Baniulis D, Yamashita E, Whitelegge JP, Zatsman AI, Hendrich MP, Hasan SS, Ryan CM, Cramer WA.
  Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120.
  J. Biol. Chem., 2009, 284(15): 9861-9869.
   
• Baniulis D, Yamashita E, Zhang H, Hasan SS, Cramer WA
  Structure-Function of the Cytochrome bf Complex. Photochem Photobiol., 2008, 84 (6):1349-1358.
   
• Baniulis D, Liobikas J, Gelvonauskiene D, Sasnauskas A, Vaitiekaitis G, Stanys V.
  Computational analysis of thaumatin-II allergenicity and prediction of antigenic elements of thaumatin-like family proteins. Biologija (Vilnius), 2008, 54 (3): 202-207.
  
  
• Yan J, Dashdorj N, Baniulis D, Yamashita E, Savikhin S, Cramer WA
  On the structural role of the aromatic residue environment of the chlorophyll a in the cytochrome b6f complex. Biochemistry, 2008, 47 (12): 3654-3661.
  
  
• Taylor RM, Baniulis D, Burritt JB, Gripentrog JM, Lord CI, Riesselman MH, Maaty W, Bothner BP, Angel TE, Dratz EA, Linton GF, Malech HL, Jesaitis AJ
  Analysis of human phagocyte flavocytochrome b(558) by mass spectrometry. J. Biol. Chem., 2006, 281 (48): 37045-37056.
  
  
• Liobikas J, Baniulis D, Stanys V, Toleikis A, Eriksson O
  Identification and analysis of a novel serine ß-lactamase-like plant protein by a bioinformatic approach. Biologija (Vilnius), 2006, 3: 126-129.
  
  
• Baniulis D, Nakano Y, Nauseef WM, Banfi B, Cheng G, Lambeth DJ, Burritt JB, Taylor RM, Jesaitis AJ
  Evaluation of two anti-gp91(phox) antibodies as immunoprobes for Nox family proteins: mAb 54.1 recognizes recombinant full-length Nox2, Nox3 and the C-terminal domains of Nox1-4 and cross-reacts with GRP 58. Biochim. Biophys. Acta, 2005, 1752 (2): 186-196.
  
  
• Baniulis D, Burritt JB, Taylor RM, Dinauer MC, Heyworth PG, Parkos CA, Magnusson KE, Jesaitis AJ
  Monoclonal antibody CL5 recognizes the amino terminal domain of human phagocyte flavocytochrome b558 large subunit, gp91phox. Eur. J. Haematol., 2005, 74 (4): 337-347.
  
  
• Baniulis D, Nauseef WM, Burritt JB, Taylor RM, Heyworth PG, Dinauer MC, Bumelis VA, Magnusson KE, Jesaitis AJ
  Unusual polyclonal anti-gp91 peptide antibody interactions with X-linked chronic granulomatous disease-derived human neutrophils are not from compensatory expression of Nox proteins 1, 3, or 4. Eur. J. Haematol., 2005, 74 (3): 241-249.
  
  
• Taylor RM, Burritt JB, Baniulis D, Foubert TR, Lord CI, Dinauer MC, Parkos CA, Jesaitis AJ
  Site-specific inhibitors of NADPH oxidase activity and structural probes of flavocytochrome b: characterization of six monoclonal antibodies to the p22phox subunit. J. Immunol., 2004, 173 (12): 7349-7357.
  
  
• Taylor RM, Foubert TR, Burritt JB, Baniulis D, McPhail LC, Jesaitis AJ
  Anionic amphiphile and phospholipid-induced conformational changes in human neutrophil flavocytochrome b observed by fluorescence resonance energy transfer. Biochim. Biophys. Acta, 2004, 1663 (1-2): 201-213.
   
• Burritt JB, Foubert TR, Baniulis D, Lord CI, Taylor RM, Mills JS, Baughan TD, Roos D, Parkos CA, Jesaitis AJ
  Functional epotipe on human neutrophil flavocytochrome b558. J. Immunol., 2003, 170 (12): 6082-6089.
   
• Taylor RM, Burritt JB, Foubert TR, Snodgrass MA, Stone KC, Baniulis D, Gripentrog JM, Lord C, Jesaitis AJ
  Single-step immunoaffinity purification and characterization of dodecylmaltoside-solubilized human neutrophil flavocytochrome b. Biochim. Biophys. Acta, 2003, 1612 (1): 65-75.
   
• Foubert TR, Bleazard JB, Burritt JB, Gripentrog JM, Baniulis D, Taylor RM, Jesaitis AJ
  Identification of a spectrally stable proteolytic fragment of human neutrophil flavocytochrome b composed of the NH2-terminal regions of gp91(phox) and p22(phox). J. Biol. Chem., 2001, 276 (42): 38852-38861.

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The page updated on 02 02 2012.