aaron collier
Scientist, Downstream Process Development at Passage Bio
scientist , downstream process development passage bio
self-directed scientist 10 year experience expressing recombinant protein using mammalian , bacterial , insect cell line developing , optimizing , executing protocol purification using akta instrument . highly accomplished bioanylitcal characterization protein structure function using technique enzymatic activity assay , x-ray crystallography , ultracentrifugation , mass spectrometry , electron microscopy , circular dichroism . leverage knowledge skill provide valuable expertise company pharmaceutical / biotechnology industry .
Passage Bio
https://www.linkedin.com/company/passage-bio
Princeton, New Jersey, United States
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Scientist, Downstream Process Development
Evotec
https://www.linkedin.com/company/evotec
Provide pharmaceutical and biotech clients with the purified proteins needed for their downstream research programs. Specializing in oncology targets.

• Execute protein purification and characterization experiments on a wide range of target proteins including antibodies, protein complexes, enzymes, and structural proteins.
• Troubleshoot experimental issues as they arise to ensure that project goals are achieved within the defined timelines and budgetary constraints.
• Analyze, write, and present experimental data and technical reports on project results as well as consult with clients regarding future project designs.
• Organize the maintenance and upkeep of 17 chromatography instruments for laboratory use.
Princeton, New Jersey, United States
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Senior Scientist - Protein Purification
Rutgers University
https://www.linkedin.com/company/rutgersu
Managed a diverse team of researchers to engineer a second generation therapy for the treatment of a rare, neurological, lysosomal storage disease LINCL in order to improve the cellular stability and brain biodistribution of the native protein. 

•	Developed, optimized, and executed protocols for large scale expression in mammalian cell lines, purification using AKTA instruments, and the downstream characterization of protein species for use in enzyme replacement therapy.
•	 Screened variants and chemical modifications to the protein of interest and characterized the resulting effects on biodistribution, enzyme kinetics, half-life, clearance, and toxicity in cell lines and experimental animals. 
•	Oversaw day-to-day lab operations to ensure experimental and documentation protocols are follow by lab personnel.
•	Repaired and maintained lab equipment including the AKTA chromatography instruments.
Piscataway Township, New Jersey
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Research Associate
GE Healthcare
https://www.linkedin.com/company/gehealthcare
Oversaw a $4M territory with a portfolio comprised of the AKTA chromatography, Whatman filtration, Illustra nucleic acid isolation / amplification, and Amersham product lines. 

•	Acknowledged by leaders for successfully managing a diverse portfolio of GE consumables and instruments for academic, biotech, and industrial accounts. Charged with identifying customer product needs while securing / distributing promotional materials.
•	Surpassed sales goals in 2015 / 2016 while utilizing client relationship strategies developed from scientific expertise to build key connections. 
•	Organized and directed vendor shows, equipment trainings, and demos to educate prospective customers; acted as Subject Matter Expert on chromatography for the Texas sales team.
Houston, Texas
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Independent Contractor Representative
GE Healthcare
https://www.linkedin.com/company/gehealthcare
•	Visited labs at Rice University and the MD Anderson Cancer Center to determine specific product needs and to distribute GE promotional material
•	Transmitted information on products and technologies used at the visited accounts to GE Healthcare sales representatives via biweekly reports
•	Collaborated with GE sales representatives to market GE products and services
Houston, Texas
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University Contractor Representative
Rice University
https://www.linkedin.com/company/riceuniversity
Pioneered the characterization of a human infecting strain of Picobirnavirus, a previously unstudied virus

•	Utilized bacterial and insect cell cultures to express viral macromolecules of interest that were then purified using an AKTA FPLC chromatography system to be used in biophysical and biochemical experiments
•	Built high resolution, 3-dimensional models representing multiple conformational states of the Picobirnavirus RNA polymerase based upon high resolution X-ray diffraction data
•	Determined the kinetics of the RNA polymerase’s interaction with a variety of synthetic RNA oligonucleotides using a combination of fluorescence anisotropy and gel shift assays
•	Characterized the assembly of the wild-type Picobirnavirus capsid protein and a host of capsid protein mutants to determine the intermediate assembly states using transmission electron microscopy
•	Maintained the AKTA FPLC chromatography systems within the lab including replacing multiple internal components
•	Mentored an undergraduate student in the development of a novel, viral based method for controlling the expression of low abundance proteins in E. coli
Houston, Texas
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Graduate Student
Doctor of Philosophy (Ph.D.)
Thesis Title: Initiation of RNA polymerization and polymerase encapsidation by a strain of Picobirnavirus
Biochemistry and Cell Biology
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Rice University
https://www.linkedin.com/school/riceuniversity/
Bachelor’s Degree
Physics
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Texas A&M University
https://www.linkedin.com/school/texas-a&m-university/
Late-infantile neuronal ceroid lipofuscinosis (LINCL) is a neurodegenerative lysosomal storage disorder caused by mutations in the gene encoding the protease tripeptidyl-peptidase 1 (TPP1).  Progression of LINCL can be slowed or halted by enzyme replacement therapy, where recombinant human TPP1 is administered to patients.  In this study, we utilized protein engineering techniques to increase the stability of recombinant TPP1 with the rationale that this may lengthen its lysosomal half-life, potentially increasing the potency of the therapeutic protein.  Utilizing multiple structure-based methods that have been shown to increase the stability of other proteins, we have generated and evaluated over 70 TPP1 variants.  The most effective mutation, R465G, increased the melting temperature of TPP1 from 55.6{degree sign}C to 64.4{degree sign}C and increased its enzymatic half-life at 60{degree sign}C from 5.4 min to 21.9 min.  However, the intracellular half-life of R465G and all other variants tested in cultured LINCL-patient derived lymphoblasts was similar to that of WT TPP1.  These results provide structure/function insights into TPP1 and indicate that improving in vitro thermal stability alone is insufficient to generate TPP1 variants with improved physiological stability.  This conclusion is supported by a proteome-wide analysis that indicates that lysosomal proteins have higher melting temperatures but also higher turnover rates than proteins of other organelles.  These results have implications for similar efforts where protein engineering approaches, which are frequently evaluated in vitro, may be considered for improving the physiological properties of proteins, particularly those that function in the lysosomal environment.
Lysosomal protein thermal stability does not correlate with cellular half-life: Global observations and a case study of tripeptidyl-peptidase 1.
The Biochemical Journal
https://www.ncbi.nlm.nih.gov/pubmed/31957806
During the replication cycle of double-stranded (ds) RNA viruses, the viral RNA-dependent RNA polymerase (RdRP) replicates and transcribes the viral genome from within the viral capsid. How the RdRP molecules are packaged within the virion and how they function within the confines of an intact capsid are intriguing questions with answers that most likely vary across the different dsRNA virus families. In this study, we have determined a 2.4 Å resolution structure of an RdRP from the human picobirnavirus (hPBV). In addition to the conserved polymerase fold, the hPBV RdRP possesses a highly flexible 24 amino acid loop structure located near the C-terminus of the protein that is inserted into its active site. In vitro RNA polymerization assays and site-directed mutagenesis showed that: (1) the hPBV RdRP is fully active using both ssRNA and dsRNA templates; (2) the insertion loop likely functions as an assembly platform for the priming nucleotide to allow de novo initiation; (3) RNA transcription by the hPBV RdRP proceeds in a semi-conservative manner; and (4) the preference of virus-specific RNA during transcription is dictated by the lower melting temperature associated with the terminal sequences. Co-expression of the hPBV RdRP and the capsid protein (CP) indicated that, under the conditions used, the RdRP could not be incorporated into the recombinant capsids in the absence of the viral genome. Additionally, the hPBV RdRP exhibited higher affinity towards the conserved 5’-terminal sequence of the viral RNA, suggesting that the RdRP molecules may be encapsidated through their specific binding to the viral RNAs during assembly.
Initiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virus
PLoS Pathogens
http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1005523
Partitiviruses constitute one of the nine currently recognized families of viruses with encapsidated, double-stranded (ds)RNA genomes. The partitivirus genome is bisegmented, and each genome segment is packaged inside a separate viral capsid. Different partitiviruses infect plants, fungi, or protozoa. Recent studies have shed light on the three-dimensional structures of the virions of three representative fungal partitiviruses. These structures include a number of distinctive features, allowing informative comparisons with the structures of dsRNA viruses from other families. The results and comparisons suggest several new conclusions about the functions, assembly, and evolution of these viruses.
Advances in Virus Research volume 86: 3-D Structures in Fungal Partitiviruses
Academic Press, Waltham, MA
Center for Advanced Biotechnology & Medicine - Rutgers University
Director's Award for Best Poster by a Postdoctoral Fellow
Department of Biochemistry and Cell Biology at Rice University
Outstanding Student Seminar Award
National Institute of Health
NIH Fellowship from the Houston Area Molecular Biophysics Program
Houston Livestock Show & Rodeo
Fellowship from the Houston Livestock Show & Rodeo
Abla Tannous
      
          



            
              
        
              
  

    
        I worked with Aaron for over two years during my postdoctoral work at Rutgers University. From the first day Aaron joined our lab, I was rapidly impressed with his wide scientific knowledge, his meticulous experimental design and execution, and his work ethics.  Aaron is a highly skilled scientist with an all-encompassing knowledge of protein biochemistry ranging from protein expression, purification and characterization. His multidisciplinary expertise extends to countless aspects of cell, molecular biology, biochemistry and biophysics. He’s the best co-worker anyone can wish for with a wonderful team spirit, always giving a helpful hand and can be counted on when needed. In addition, Aaron is an excellent communicator and mentor. This was very evident when I co-taught with him a summer undergraduate research program at Rutgers, as well as from his successful mentorship of undergraduate students in the lab.  I was lucky to have the privilege to work with Aaron and I think his hard-working attitude, his dedication and his admirable interpersonal skills would make any group lucky to have him work with them. 
https://nz.linkedin.com/in/aaron-collier-357ab386
New Zealand
Aaron Collier
Planning & RMA Specialist
https://www.linkedin.com/in/kacollier
Austin, TX
Aaron Collier
Solution Engineer, Enterprise at VMware
https://www.linkedin.com/in/aaron-collier-8769782
Beaumont-Port Arthur Area
Aaron Collier
https://www.linkedin.com/in/aaron-collier-b196545
Stephenville, TX
Aaron Collier
Vice President at Collier Consulting, Inc.
https://www.linkedin.com/in/aaron-collier-818a13a
Rohnert Park, CA
Aaron Collier
Senior Vice President of Information Technology at Redwood Credit Union
Texas A&M University Alumni
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Rutgers iJOBS
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NJ Bio Pharma Networking Group (NJBPNG)
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MolecularLab (Community of Molecular Biology & Biotech companies, students, researchers)
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