Research Resources

Office of the Vice President for Research & Economic Development (OVPRED)

Leadership for all administrative research units serving the research enterprise at UAB. OVPRED oversees Core Facilities, Institutional Animal Care and Use Committee, and Institutional Review Board.

Integrated Research Administration Portal (IRAP)

Electronic submission of funding applications and compliance forms for future research initiatives.

UAB Institute for Innovation and Entrepreneurship

The nexus for UAB innovation, entrepreneurial educational models, applied research, and management of intellectual property.

Funding Sources and Grant Opportunities

Presentations and general information related to effective grant writing.

Office of Postdoctoral Education

UAB is committed to the development and success of outstanding postdoctoral scientists.

Conflict of Interest Review Board (CIRB)

Charged with the ongoing development of policies and procedures related to conflicts of interest in sponsored research, review of disclosures of financial interests submitted by investigators, and the development of conflict of interest management plans.

Research News

Community Engagement Institute links community leaders and academic researchers
Community Engagement Institute links community leaders and academic researchers
UAB’s Community Engagement Institute brings academic researchers and community leaders together to brainstorm ways to improve Birmingham, the region and the world.
Written by Christina Crowe

ccts engagementKeynote speaker Sampson Davis, M.D., tours the poster session.The second annual Community Engagement Institute enjoyed an overflow crowd for the daylong education and training event designed to benefit both community and academic partners.

The event, held Oct. 2 at the Birmingham-Jefferson Convention Complex, was organized by the University of Alabama at Birmingham Center for Clinical and Translational Science’s One Great Community Council and the UAB Center for the Study of Community Health’s Jefferson County Community Participation Board.

Author and physician Sampson Davis, M.D., addressed the more than 250 individuals in attendance about the importance of family and community support in cultivating personal success. Davis returned to his hometown of Newark, New Jersey, after graduating from medical school where he and two of his high school friends — who also became doctors — started an organization called The Three Doctors. Their goal is to spread the word of health, education and youth mentoring, and become “the Michael Jordan of education,” so that learning becomes a glamorized trend throughout all communities.

In the afternoon, Al Richmond, MSW, executive director, Community-Campus Partnerships for Health, shared some of what he has learned in his more than 25 years in a career that uniquely blends social work and public health to address racial and ethnic health disparities.

“This event is setting the stage for enhanced community engagement, for learning about what people can do in their own communities, as well as displaying the diversity of resources available at UAB,” Richmond said.

This year’s CEI event was free to the public, and attendance more than doubled from last year. Attendees represented members of more than 100 Greater Birmingham faith-based organizations, universities, government and nonprofit agencies, local and state health department representatives, community organizers, city and county officials, and representatives from the National Institutes of Health and the Environmental Protection Agency.

The CEI’s breakout sessions touched on three topics: activism, advocacy and community organizing; structural racism and community health; and ways to fully involve communities in collaborative research.

The CEI’s breakout sessions touched on three topics: activism, advocacy and community organizing; structural racism and community health; and ways to fully involve communities in collaborative research.

New this year, the CEI poster session featured more than 30 posters on a diverse array of public health topics, including domestic violence and HIV awareness and prevention programs, and other projects dedicated to tackling tough local public health issues. Event attendees were encouraged to network and receive a directory of all attendees’ names to facilitate future collaborations.

Max Michael, M.D., dean of the UAB School of Public Health, emphasized the importance of working to foster collaborations between higher education institutions and their larger communities.

“The momentum for this event continues to grow,” Michael said, “and reflects the desire by our Greater Birmingham community members from a broad range of organizations to have a platform to engage in meaningful conversations about how we can improve our communities’ public health.”

“We continue to be encouraged by the response to this important event, which highlights the deep knowledge, experience and talent in our communities,” said Shauntice Allen, Ph.D., director of One Great Community. “We plan to harness the momentum the CEI generates to work toward achieving, and maintaining, improved health outcomes for our community as a whole.”

Videos of Davis’ and Richmond’s talks, as well as photos of the event, are available on the CEI website,

Loder-Jackson named associate editor of urban education research journal
Loder-Jackson named associate editor of urban education research journal
School of Education professor to serve as one of two associate editors for Journal of Urban Learning, Teaching, and Research.

tondra loder jackson2Tondra Loder-Jackson, Ph.D., associate professor in the UAB School of Education’s Department of Human Studies, has been named associate editor for the 2016 issue of the Journal of Urban Learning, Teaching, and Research.

The journal is a publication of the American Educational Research Association’s Urban Learning, Teaching, and Research Special Interest Group. The AERA is a national research society that works to advance knowledge about education, encourage scholarly inquiry related to education, and promote the use of research to improve education and serve the public good. Special-interest groups like Urban Learning, Teaching, and Research provide a forum within the AERA for the involvement of individuals drawn together by a common interest in a field of study, teaching or research.

Loder-Jackson will serve as one of two associate editors for the journal. Her program of research is focused on topics related to urban education, Birmingham’s civil rights and education history, activism of educators from a historical perspective, life course perspectives on African-American education, and home, school and community relations.

Tugs and pulls: How a molecular motor untangles protein
Tugs and pulls: How a molecular motor untangles protein
E. coli ClpB is a bacterial enzyme that untangles proteins. Such tangles are hallmarks of neurodegenerative diseases like Parkinson’s and Alzheimer’s. A study led by UAB's Aaron Lucius, Ph.D., offers new insight on this amazing molecular machine, and could eventually point toward new treatment approaches.

A marvelous molecular motor that untangles protein in bacteria may sound interesting, yet perhaps not so important. Until you consider the hallmarks of several neurodegenerative diseases — Huntington’s disease has tangled huntingtin protein, Parkinson’s disease has tangled α-synuclein, and Alzheimer’s disease has tangles of tau and β-amyloid. In fact, a similar untangling motor from yeast has already shown effectiveness in mouse and nematode models of Huntington’s disease.

Aaron LuciusAaron LuciusSo Aaron Lucius, Ph.D., professor in the University of Alabama at Birmingham Department of Chemistry, is studying the bacterial protein ClpB of E. coli, as a steppingstone to expanded research on medically significant models in coming years. The question is how does ClpB actually do its job to untangle proteins?

“We don’t know how proteins get tangled, but if we can study how proteins get disaggregated, it may have clinical relevance,” Lucius said.

ClpB is one of a vast assortment of similar molecular machines found in all living cells, known as hexameric AAA + enzymes. They have six subunits that form a hexagon with a hole in the middle, and they burn ATP for energy. While the machines are all similar, the kinds of work they do vary widely — examples include unwinding DNA, helping digest proteins, untangling proteins, cutting microtubules, helping shape plant cells and driving membrane fusion.

ClpB is closely related to the ClpA enzyme of E. coli. Unlike ClpB — which has the job of untangling a protein that has lost its proper shape — ClpA helps to digest unnecessary proteins into small peptide fragments. Proteins are chains of amino acids, linked together like beads on string, and then folded into a precise shape. ClpA is able to grab one end of a protein that has been marked for recycling, and pull it through the central hole of ClpA, like an anchor chain winched in through the hawse hole of a ship. ATP hydrolysis powers that processive pulling, and the unraveled protein chain is pushed into an attached ClpP enzyme, which cuts up the chain “like a molecular paper shredder,” Lucius said.

A previous lab group had garnered evidence that ClpB is also a processive translocase, meaning that it pulls the protein chain all the way through that central hole in a long series of stepwise tugs, but they were forced to introduce an artefact into the ClpB enzyme to do their experiments. Lucius and his fellow UAB researchers are now challenging that model. After finding a way to test ClpB without introducing the artefact, their experimental results show that the ClpB enzyme makes only one or two tugs on the tangled protein, and then lets go.

“Our results support a molecular mechanism where ClpB catalyzes protein disaggregation by tugging and releasing exposed tails or loops,” they wrote in a paper recently published in the Biochemical Journal, similar to how someone would tug at the loose strands of a tangled ball of yarn.

This proposed new paradigm of how ClpB functions may apply to other untangling enzymes. “It will take time to see if it is accepted,” Lucius said.

news clpB2Molecular structure of the N-terminal domain of ClpB, a heat-shock protein. Credit: Jawahar Swaminathan and the European Bioinformatics Institute. The study of hexameric AAA+ enzyme function requires sophisticated experimental approaches. “We can’t see the proteins; we have to come up with clever ways to infer what they are doing,” Lucius said.

His lab discovered such a clever technique in 2010 while working with ClpA. But when graduate student Tao Li tried to apply it to ClpB studies, and expected to find similar results of processive translocation that the earlier group had reported, “she did three years of every possible experiment to see if it translocates and found no evidence in support of translocation,” Lucius said. So the UAB lab began to consider alternatives, which led to the finding that the ClpB enzyme made only one or two tugs before releasing the substrate protein. They also tested ClpB that had the artefact inserted and found evidence that what had appeared to be translocation to the previous researchers was only nonspecific protein degradation without translocation through the central hole of ClpB.

The experimental approach

ClpB binds to the substrate protein in the presence of an ATP analog that promotes binding but cannot function to power the enzyme. The bound substrate has a fluorescent label attached to its far end, but that fluorescence is dampened by the binding to ClpB. The mixture is put into one syringe, and high concentration of ATP and unlabeled substrate is put into another syringe. With the press of a trigger, a piston powered by 120-pounds-per-square-inch nitrogen gas mixes the contents of the two syringes together within two-thousandths of a second, and now, in the presence of ATP, the ClpB machine can go to work. This technique is known as fluorescence stopped-flow. 

The UAB researchers look for the increased fluorescence when ClpB releases the labeled substrate. If the enzyme is pulling the labeled substrate protein through the central hole of the hexamer, there will be a time lag before the fluorescence increases. That lag will increase as longer substrate proteins are tested. But if the ClpB only tugs once or twice, and then releases the substrate, there will be no lag. Conditions are set so that, after each single ClpB hexamer releases its fluorescently labeled substrate, the enzyme will not bind another because there is an excess of unlabeled substrate. Thus, this fluorescence stopped-flow method shows only a single turnover for each enzyme complex.

When this system was used with ClpA, there was a lag before fluorescence increase, and that lag increased with increased length of the substrate protein. Both those results are consistent with the ClpA enzyme, powered by ATP, pulling the substrate protein through its central hole. With a 127-amino-acid substrate, that lag lasted 10 seconds. When this system was used with ClpB, there was no lag, and the length of the substrate made no difference in how quickly the fluorescent signal increased. Thus, ClpB was releasing the substrate quickly.

The paper, “Escherichia coli ClpB is a non-processive polypeptide translocase,” was recently published online in advance of print in Biochemical Journal. Lucius is corresponding author. Co-authors, all from the UAB Department of Chemistry, are Tao Li, Ph.D. (now at Washington University School of Medicine), Clarissa Weaver, Jiabei Lin, Elizabeth Duran and Justin Miller, Ph.D. (now at St. Jude Children’s Research Hospital).

This work was supported by NSF grant MCB-1412624.

King crabs threaten Antarctic ecosystem due to warming ocean
King crabs threaten Antarctic ecosystem due to warming ocean
Predators’ arrival could radically alter marine life

king crabThe king crab Paralomis birsteini, photographed on the continental slope off Marguerite Bay, Antarctica, at a depth of 1100 m.King crabs may soon become high-level predators in Antarctic marine ecosystems where they have not played a role in tens of millions of years, according to a new study on which University of Alabama at Birmingham researchers worked in conjunction with the Florida Institute of Technology and other institutions.

“No Barrier to Emergence of Bathyal King Crabs on the Antarctic Shelf,” published this week in the Proceedings of the National Academy of Sciences, ties the reappearance of these crabs to global warming.

This study is a continuation of previous work in the field of Antarctic marine ecology done by James McClintock, Ph.D., paper co-author and professor in UAB’s College of Arts and Sciences’ Department of Biology, along with his colleagues.

“The rising temperature of the ocean west of the Antarctic Peninsula — one of the most rapidly warming places on the planet — should make it possible for king crab populations to move to the shallow continental shelf from their current deep-sea habitat within the next several decades,” said lead author Richard Aronson, Ph.D., professor and head of Florida Tech’s Department of Biological Sciences.

Researchers found no barriers, such as salinity levels, types of sediments on the seafloor or food resources, to prevent the predatory crustaceans from arriving if the water became warm enough. That arrival would have a huge impact.

“Because other creatures on the continental shelf have evolved without shell-crushing predators, if the crabs moved in they could radically restructure the ecosystem,” Aronson said.

nathaniel palmerNathaniel B. Palmer in the ice off Marguerite Bay.The study provides initial data and does not by itself prove that crab populations will expand into shallower waters.

“The only way to test the hypothesis that the crabs are expanding their depth-range is to track their movements through long-term monitoring,” McClintock said.

In the 2010 to 2011 Antarctic summer, in research funded by the National Science Foundation, the team used an underwater camera sled to document a reproductive population of the crabs for the first time on the continental slope off Marguerite Bay on the western Antarctic Peninsula. That area is only a few hundred meters deeper than the continental shelf where the delicate ecosystem flourishes.

“The mounting anticipation as the researchers watched the transmissions from the seafloor culminated in a mixture of both satisfaction and unease upon the seeing the first image of a king crab on the Antarctic slope,” said Margaret Amsler, a research assistant and co-author from UAB.

“The overall effect of the migration of king crabs to shallower waters,” said postdoctoral scientist and study co-author Kathryn Smith of Florida Institute of Technology, “would be to make the unique Antarctic ecosystem much more like ecosystems in other areas of the globe, a process ecologists call biotic homogenization.”

sea sledSeaSled towed vehicle being deployed from the Palmer off Marguerite Bay.Such changes, the researchers concluded, would fundamentally alter the Antarctic seafloor ecosystem and diminish the diversity of marine ecosystems globally.

The data used in the paper were collected during an expedition to Antarctica run jointly by NSF, the Swedish Polar Research Secretariat and the Swedish Research Council. The expedition included scientists from Florida Tech, UAB, the Woods Hole Oceanographic Institution, the University of Gothenburg in Sweden and the University of Southampton in the United Kingdom.

Journalists may access the embargoed paper through EurekAlert. They should register with and request access to PNAS materials. Already registered journalists may request access to PNAS at

A video version of this news story available by contacting Dena Headlee at or (703) 292-7739.

October is Breast Cancer Awareness Month
October is Breast Cancer Awareness Month
Summary: Several activities are planned in and around UAB for Breast Cancer Awareness Month.

pink ribbonBreast cancer is the most common cancer among women in the United States, other than skin cancer. It is the second leading cause of cancer death in women, after lung cancer. Thanks to early detection and improvements in treatment, millions of women are surviving the disease.

The Breast Cancer Research Foundation of Alabama has raised more than $5 million to support cancer research at the University of Alabama at Birmingham Comprehensive Cancer Center. The BCRFA helps to ensure that physicians and scientists can seize every opportunity for groundbreaking discovery.

In honor of Breast Cancer Awareness Month, the BCRFA and other organizations are hosting local events:

Sept. 25–Oct. 25: Calera Goes Pink!

Join the City of Calera as they Go Pink to support breast cancer research in Alabama. This citywide event kicks off with the Calera High School football game on Friday, Sept. 25, and culminates with a golf tournament at Timberline on Oct. 25. For details, call BCRFA at 205-996-5463.

October: Pink Ribbon Project

Dozens of fire stations across the state will Go Pink! throughout the month of October and will be selling specially designed Pink Ribbon Project T-shirts for $15 and $20. Proceeds from shirt sales will help the BCRFA provide seed dollars required to secure sustaining, national grants for breast cancer research at the UAB Comprehensive Cancer Center.

October: Tameron BC Awareness Campaign

Tameron Automotive Group will donate $100 in support of breast cancer research for every car sold during October at Tameron Honda (1675 Montgomery Highway, Birmingham) and Tameron Hyundai (1595 Montgomery Highway, Birmingham).

Oct. 9 and Oct. 20: BCRFA’s Go Pink! T-shirt Sale

From 7:30 a.m.-1:30 p.m. on Oct. 9 and 11 a.m.-3 p.m. on Oct. 20, short-sleeved and long-sleeved T-shirts will be on sale by the elevators in the North Pavilion Building at UAB Hospital. Short-sleeved shirts are $15, and long-sleeved shirts are $20.

Oct. 10: Ross Bridge Uncorked! On the Green

The community is invited to come out to this free annual event at Ross Bridge (2101 Grand Avenue, Hoover) to sample beer and wine, and make a donation to support BCRFA. Wine tasting is from noon-2 p.m., and beer sampling is from 2:30-5 p.m. A valid ID is required prior to sampling. For more information, visit

Oct. 16: Pink Luncheon “Crazy for a Cure”

Make a minimum donation of $15 to BCRFA and enjoy a Mexican buffet, fun and prizes at the MSE Building Co. at 5500 Derby Drive, Birmingham. RSVP at 205-833-9010.

Oct. 17: Susan G. Komen Race for the Cure

The Susan G. Komen Race for the Cure is the largest series of 5K run/fitness walks in the world. The local race will begin at Linn Park in downtown Birmingham. The survivor parade will be at 8:30 a.m., the 5K starts at 9 a.m., and the 1-mile fun run/walk is at 10 a.m., with awards ceremony at 11 a.m. Detailed information is online at

Oct. 17: New Light Support Group

In lieu of the New Light Support Group meeting, members of the support group will participate in the Susan G. Komen Race for the Cure on Oct. 17, which will be held in Linn Park in downtown Birmingham. To join a team and help celebrate the life, bravery and the memory of survivors, contact Kimberly Robinson at 205-975-7912 or

Oct. 18: Fashion and Friends Charity Expo

This charity business expo will be held in the Main Hall at the Bessemer Civic Center from 4-8 p.m. There will be vendors, speakers and food, with ticket proceeds going to support BCRFA. Tickets are $10 in advance. For more information, visit

Oct. 25: Pink Private Shopping Night, Belk at the Summit

From 6:30-9 p.m. BCRFA and Belk are once again partnering to host this exclusive private shopping night. A $25 ticket includes complimentary food and beverages, live entertainment, fabulous door prizes, and the opportunity to shop exclusive shopping discounts at Belk. Tickets are available for purchase online at or by calling BCRFA at 205-996-5463.

Phi Kappa Phi Love of Learning Awards

Love of Learning Awards will help fund post-baccalaureate studies and/or career development for active Phi Kappa Phi members to include (but not be limited to): Graduate or professional studies, doctoral dissertations, continuing education, career development, travel related to teaching/studies, etc. Recipients of the Fellowship award are not eligible to apply. Eighty awards, at $500 each, will be awarded.

The competition is open to all active (dues current) Phi Kappa Phi members who:

  • Have completed their baccalaureate studies by application submission deadline.
  • Did not receive a Fellowship or Award of Excellence grant.
Fore more information please go to: