Stanford scientist discovers and tracks his diabetes onset
Friday, 16 March 2012
Contact: Krista Conger
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For more on stem cells and cloning, go to CellNEWS at
http://cellnews-blog.blogspot.com/
Stanford scientist discovers and tracks his diabetes onset
Friday, 16 March 2012
Posted by ZenMaster at Friday, March 16, 2012
Labels: California, diabetes, DNA, genetic screening, genome, human, protein, proteome, research, RNA, sequence, US, virus 0 comments
Scientists Learn How Stem Cell Implants Help Heal Traumatic Brain Injury
Friday, 13 January 2012
For years, researchers seeking new therapies for traumatic brain injury have been tantalized by the results of animal experiments with stem cells. In numerous studies, stem cell implantation has substantially improved brain function in experimental animals with brain trauma. But just how these improvements occur has remained a mystery.
Posted by ZenMaster at Friday, January 13, 2012
Labels: actin, brain, GDNF, proteome, stem cells 0 comments
Proteomics: Critical Similarity
Between Embryonic and iPS Cells
Posted by ZenMaster at Monday, September 12, 2011
Labels: embryonic, human, iPS, proteome, research, stem cells, US 0 comments
EMBL and CRG scientists reveal what a self-sufficient cell cannot do without Saturday, 28 November 2009 What are the bare essentials of life, the indispensable ingredients required to produce a cell that can survive on its own? Can we describe the molecular anatomy of a cell, and understand how an entire organism functions as a system? These are just some of the questions that scientists in a partnership between the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, and the Centre de Regulacio Genòmica (CRG) in Barcelona, Spain, set out to address. In three papers published back-to-back today in Science, they provide the first comprehensive picture of a minimal cell, based on an extensive quantitative study of the biology of the bacterium that causes atypical pneumonia, Mycoplasma pneumoniae. The study uncovers fascinating novelties relevant to bacterial biology and shows that even the simplest of cells is more complex than expected. Mycoplasma pneumoniae is a small, single-cell bacterium that causes atypical pneumonia in humans. It is also one of the smallest prokaryotes – organisms whose cells have no nucleus – that do not depend on a host's cellular machinery to reproduce. This is why the six research groups, which set out to characterize a minimal cell in a project headed by scientists Peer Bork, Anne-Claude Gavin and Luis Serrano, chose M. pneumoniae as a model: it is complex enough to survive on its own, but small and, theoretically, simple enough to represent a minimal cell – and to enable a global analysis. A network of research groups at EMBL's Structural and Computational Biology Unit and CRG's EMBL-CRG Systems Biology Partnership Unit approached the bacterium at three different levels. One team of scientists described M. pneumoniae's transcriptome, identifying all the RNA molecules, or transcripts, produced from its DNA, under various environmental conditions. Another defined all the metabolic reactions that occurred in it, collectively known as its metabolome, under the same conditions. A third team identified every multi-protein complex the bacterium produced, thus characterising its proteome organisation. "At all three levels, we found M. pneumoniae was more complex than we expected", says Luis Serrano, co-initiator of the project at EMBL and now head of the Systems Biology Department at CRG. When studying both its proteome and its metabolome, the scientists found many molecules were multifunctional, with metabolic enzymes catalyzing multiple reactions, and other proteins each taking part in more than one protein complex. They also found that M. pneumoniae couples biological processes in space and time, with the pieces of cellular machinery involved in two consecutive steps in a biological process often being assembled together.
This image represents the integration of genomic, metabolic, proteomic, structural and cellular information about Mycoplasma pneumoniae in this project: one layer of an Electron Tomography scan of a bottle-shaped M. pneumoniae cell (grey) is overlaid with a schematic representation of this bacterium's metabolism, comprising 189 enzymatic reactions, where blue indicates interactions between proteins encoded in genes from the same functional unit. Apart from these expected interactions, the scientists found that, surprisingly, many proteins are multifunctional. For instance, there were various unexpected physical interactions (yellow lines) between proteins and the subunits that form the ribosome, which is depicted as an Electron microscopy image (yellow). Credit: Takuji Yamada /EMBL. Posted by ZenMaster at Saturday, November 28, 2009
Labels: DNA, genome, Mycoplasma, proteome, research, RNA, sequence 0 comments
For scientists who track interactions between cell proteins, a time of reckoning has arrived Tuesday, 06 January 2009 During the past 20 years, researchers have identified thousands of cell protein interactions, with the ultimate goal of inventorying all that occur within cells of various organisms — a comprehensive catalogue known as the interactome. Such information will be critical to understanding the basic mechanics of cellular life, and how malfunctions in these processes contribute to cancer. Unfortunately, the data collected by different teams of researchers has been somewhat inconsistent. One group's "map" of protein interactions in yeast cells, for example, may only partially overlap the map produced by another group. Because science depends on investigators' ability to reproduce and build on one another's work, such variability presents a considerable obstacle. The value of interactome maps — and the potential of further research — will be at issue as long as the accuracy and thoroughness of the underlying data is uncertain. To recapture momentum, the field needs to be clear about the strengths and weaknesses of different methods of tracking protein interactions, researchers say, and reach a consensus on questions such as:
In a series of four papers published in the January issue of the journal Nature Methods, investigators in
Dana-Farber Cancer Institute's Center for Cancer Systems Biology (CCSB) start to answer those questions by examining the accuracy and thoroughness of current interactome maps and the techniques by which they are compiled. The studies — in a special issue of the journal on the interactome — provide a set of ground rules for future research and demonstrate the power of such research when backed by well-proven experimental techniques. The CCSB's director, Marc Vidal, PhD, is the senior author of the papers. Framework for study The first study, lead-authored by the CCSB's Kavitha Venkatesan, PhD, offers a framework for gauging the quality of current maps of the interactome in human cells. The maps draw on three sources of information about protein interactions: high throughput yeast two-hybrid (HT-Y2H) procedures, which use robotic equipment to screen thousands of proteins to see which bind to each other (the binding switches on a "reporter" gene that can be chemically detected); compilations of published studies on small numbers of protein interactions; and studies that predict interactions based on computational techniques. While each approach is useful, it isn't clear whether small-scale experiments provide better data than high volume screenings (as some studies have suggested), whether the interactions detected in experiments actually occur in living cells, and whether existing maps depict a small- or large-sized chunk of the entire interactome. All experimental techniques generate some false positives — in which interactions are "detected" that haven't really taken place — and false negatives — in which interactions that have occurred fail to be found. To weed them out, the new framework examines experimental methods from the standpoint of precision, sensitivity, and completeness. "The framework approach takes as standards interactions reported in multiple studies of high quality, and then verifies those standards against results obtained by other techniques," says Venkatesan. Using the framework, the Dana-Farber team found that each technique captures only 20-30 percent of all the interactions within cells. That led them to determine that the human interactome contains about 130,000 interactions, a small minority of which have been mapped so far. The second study offers researchers a tool kit for determining whether a newly discovered interaction is indeed real, and not a false positive reading from a particular type of experiment. The kit is a set of four, high-capacity protein interaction tests that have been weighted in relation to a common set of benchmark data. When scientists identify two proteins as likely interactors, the pair can be tested in the tool kit to obtain a "confidence score" about whether they do, in fact, interact. "This general approach will allow researchers to systematically and objectively assign confidence scores to all individual protein-protein interactions in cells," says lead author Pascal Braun, PhD.. "Such a universally interpretable quality standard is critical for constructing accurate interactome maps." The third study uses the quality control framework from the first study to compile a new, expanded map of the interactome of the worm Caenorhabditis elegans (C. elegans), a scientific favourite whose cells have roughly the same number of genes as human cells do. The previous version of the map was assembled from studies involving about 2,000 proteins. For the new map, lead author Nicolas Simonis, PhD, of the CCSB and his associates screened some 10,000 protein pairs, documenting 3,864 high quality interactions. The framework enabled the researchers to estimate that the worm's genome includes about 116,000 interactions, meaning that 96 percent of its interactome remains uncharted. Trust, but verify Interactome maps are constructed from a variety of sources — new experiments and data from earlier studies. As Michael Cusick, PhD, and co-authors show in the fourth Nature Methods paper, the information in some of those much-used databases is not as reliable as one would hope. The team focused on databases built from published studies that involve just a few protein interactions — an approach sometimes thought to be more accurate than mass-screening techniques. Researchers typically cull information from several such studies to draw conclusions about which proteins interact. In examining such studies closely, however, the researchers found that the results overlap rather infrequently. Of some 12,000 interactions that have been identified in yeast cells, 75 percent were reported in one study only. When Cusick and colleagues reviewed 100 of these shakily supported interactions, they could independently substantiate only 25 percent of them. The authors suggest that the lower-than-expected quality of this data has less to do with the skill of the scientists who handle the data than with the inherent difficulty of extracting information from long, text-heavy documents. "Often, these studies use different reporting guidelines, which makes it difficult to compile results in a uniform way," Cusick remarks. One solution is the molecular interaction experiment initiative, or MIMIx, which standardizes reporting of protein interactions in published manuscripts. "Interaction mapping is a complex field," Cusick states. "By teasing apart the process of interaction discovery and verification, we've identified where problems are coming from and offered solutions to minimize inconsistencies in the future. This will be critical as efforts continue to map the entire interactome of various species, including humans." ......... ZenMasterPanoramic View of Protein-RNA Interactions in Living Cells Sunday, 02 November 2008 DNA, it has turned out, is not all it was cracked up to be. In recent years we learned that the molecule of life, the discovery of the 20th century, did not – could not – by itself explain the huge differences in complexity between a human and a worm. Forced to look elsewhere, scientists turned to RNA, a direct yet more complex transcript of DNA. But methodological problems have historically plagued the study of RNA regulation in living cells, limiting not only the accuracy of results but also our understanding of RNA's role in human disease. But now, in research to appear in the November 2 advance online issue of Nature, Robert B. Darnell, head of the Laboratory of Molecular Neuro-oncology at Rockefeller University and a Howard Hughes Medical Institute investigator, and his team have changed all that. By adapting techniques mastered in the test tube and combining them with high throughput technology, the team has developed a genome-wide platform to study how specialized proteins regulate RNA in living, intact cells. The platform allows researchers to identify, in a single experiment, every sequence within every strand of RNA to which proteins bind. The result is an unbiased and unprecedented look at how differences in RNA can explain how a worm and a human can each have 25,000 genes yet be so different. "RNA offers a way to make the cell much more complex than what this limited set of genes can offer," says Darnell, who is Robert and Harriet Heilbrunn Professor at Rockefeller. "But how is RNA being regulated in different conditions and diseases, and in different cell types? With this platform, we now have a way to address all these questions." Traditional methods used molecules to extract protein-RNA complexes from living tissue. But often the molecule only extracted the RNA. Other times, the protein bound too weakly to survive the purification process, which involved stripping the complex of unwanted debris. To address the issue, Darnell and his team used a trick from test-tube biochemistry that molecularly cements these regulatory proteins to RNA at the moment they touch. The technique, when applied to high throughput sequencing, is called high throughput sequencing-cross linking immunoprecipitation, or HITS-CLIP for short. Since the RNA and RNA-binding protein are fused together, the researchers can really beat up the extract and rigorously purify the protein without fear of losing the RNA. At the end of the day, they are left with the RNA sequence to which the protein was bound. They can then take these sequences to Rockefeller's high throughput sequence facility, and with the help of Research Support Specialist Scott Dewell, overlay them onto the genome and see where they match. What they get is a map of every position on every transcribed RNA where the RNA binding protein is binding. When DNA is transcribed into RNA, the primary transcript is divided into many blocks called exons, which are separated by empty spaces. In order to convert the transcript into some sort of message, all the spaces need to be removed; but if an exon is dropped, a different version of that protein, which could carry a very different message, is created. "That's RNA splicing," says first author Donny Licatalosi, a postdoctoral associate in the lab. "It is what gives rise to this massive pool of diverse and complex tissues with a relatively small number of genes." In the past, the group used a sophisticated process of evidence and inference to make predictions of the points of regulation along the transcript. "Now, we have direct biochemical validation that these interactions occur in the brain to regulate splicing," says Licatalosi. "The observed map – and this was amazing – looked just like our predicted map," says Darnell. Darnell, Licatalosi and their colleagues Aldo Mele, a research assistant, John Fak, a research assistant, Sung-Wook Chi, a graduate fellow in computational biology and medicine, Xuning Wang, assistant director of biocomputing and Jennifer Darnell, a research associate professor, looked at an RNA-binding protein called Nova2 that is found exclusively in neurons. They found that depending on where Nova2 binds to RNA, they could predict and directly observe whether an exon would be included or excluded in the final transcript, and which protein version it created. "The cell seems to be going through great trouble to regulate these RNAs in different conditions and different cell types," says Darnell. "When RNA developed the ability to make a more stable copy of itself – DNA – it didn't write itself off as a relic for the textbooks. It stayed at the core of complex processes in the cell." Reference: HITS-CLIP yields genome-wide insights into brain alternative RNA processing Donny D. Licatalosi, Aldo Mele, John J. Fak, Jernej Ule, Melis Kayikci, Sung Wook Chi, Tyson A. Clark, Anthony C. Schweitzer, John E. Blume, Xuning Wang, Jennifer C. Darnell & Robert B. Darnell Nature advance online publication 2 November 2008, doi:10.1038/nature07488 ......... ZenMaster
Posted by ZenMaster at Sunday, November 02, 2008
Labels: brain, proteome, research, RNA, splicing, US 0 comments
A map of where proteins are located in tissues and cells could help scientists understand the molecular basis of diseases
Saturday, 18 October 2008
Researchers in Sweden are compiling a remarkable ‘atlas’, the Human Protein Atlas, that pinpoints the location of thousands of individual proteins in the body’s tissues and cells which will give scientists important insights into the function of different proteins and how changes in the distribution of proteins could be reflected in diseases such as cancer. Professor Mathias Uhlén of the Department of Proteomics at the Royal Institute of Technology in Stockholm, who is leading the project, said, “We are trying to map the building blocks of life.”
The project is hugely ambitious, relying on the selective identification and mapping of thousands of proteins, many of whose function is not yet known, and has required the development of a massive infrastructure to enable the proteins to be identified in a realistic period of time.
Uhlén was describing the human protein atlas at the European Science Foundation’s 3rd Functional Genomics Conference in Innsbruck, Austria, on 1-4 October. Functional genomics describes the way in which genes and their products, proteins, interact together in complex networks in living cells. If these interactions are abnormal, diseases can result. The Innsbruck meeting brought together more than 450 scientists from across Europe to discuss recent advances in the role of functional genomics in disease.
The protein atlas team first uses the human genome – the sequence of all the 20000 or so genes in human cells – to encode individual proteins. They then develop ‘antibodies’ – protein molecules that recognise specific targets – against each of these proteins. The antibody that recognises a given protein is then labelled with a marker to render it visible under a microscope and is exposed to samples of different tissues and cells. The antibody binds to the proteins and in this way the location of the protein can be detected.
“To do this systematically requires a lot of automation and robotics,” Uhlén said.
“We have six software engineers writing codes just to keep track on the samples. The project is generating 400 gigabytes of data every day.”
There is a 100-strong team working on the project, with a site due to be set up soon in India, and with antibody-producing sites in Korea and China.
“To get an idea of how far we have come, in our first year we produced one antibody,” said Uhlén.
“This year we are hoping we can make 3000.”
The programme was launched in 2003, and with sufficient funding the first full version of the atlas could be available by 2014, Uhlén believes.
The team has so far mapped the location of around 5000 proteins in human cells and tissues. The researchers are also investigating whether certain common cancers – colon, prostate, lung and breast – have different protein profiles to normal tissue. In this way new ‘biomarkers’ could be identified – molecules which indicate that a tissue or cell is in a diseased state, which could alert doctors to the early stages of a disease.
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ZenMaster
Posted by ZenMaster at Saturday, October 18, 2008
Labels: human, proteome, research, Sweden 0 comments
Primer on Mitochondria

1. What are mitochondria and where are they found?
Mitochondria are bean-shaped compartments within cells that supply energy. These compartments, a type of membrane-bound organelle, are found in eukaryotes — organisms whose cells have nuclei, the home of the genome. Multicellular organisms (humans, mice, fish, etc.) as well as some unicellular ones, like yeast, are counted as eukaryotes. Bacteria, though, are not: They are considered prokaryotes for their lack of organelles, including mitochondria and nuclei.
Intriguingly, mitochondria vary widely across organisms and even within an organism. Drastic differences can exist in the number of mitochondria per cell, their size and morphology, and even their biochemical capabilities. For example, fatty acids readily broken down by mitochondria in muscle, but not brain tissue. Because of a lack of molecular knowledge about mitochondria and their resident proteins, the basis for such differences is largely unclear.
2. What do mitochondria do?
Although mitochondria are perhaps best known for their roles in energy metabolism, they also participate in a plethora of other key biological processes. These include critical functions such as programmed cell death (or “apoptosis”), a normal mechanism through which old or damaged cells can be eliminated.
Defects in mitochondria are associated with more than 50 human diseases, ranging from in-born errors of metabolism in infants to neurodegeneration in adults. Moreover, several common diseases, such as cancer and type 2 diabetes, have been associated with mitochondrial dysfunction. Prescription drugs can also disrupt mitochondria. Such drug-induced toxicity is a reason why some drugs are pulled from the market and why some potential drugs fail the clinical trial process.
3. Where do mitochondria come from?
Mitochondria, it turns out, have their own tiny genome. And in humans, this mitochondrial DNA is inherited solely from the mother. Such maternal inheritance arises because mitochondria from sperm are lost following fertilization, while those contributed by the egg persist. Because it is maternally inherited, mitochondrial DNA can provide clues about human history, including the most recent common matrilineal ancestor of living humans (so-called “Mitochondrial Eve”.)
But there are, in fact, paternal contributions to mitochondria. The parts of the mitochondria that are derived from nuclear genes actually come from both parents (see below). This follows a core principle of human genetics: of the 23 pairs of chromosomes that make up your nuclear genome, roughly half come from Mom and the other half from Dad.
Evolutionarily speaking, mitochondria have a very interesting history. They are descendants of an ancient bacterium — a relative of the modern bacterial species, Rickettsia prowazekii — that some 2 billion years ago was enveloped by another cell. That moment marked the beginning of a long and mutually beneficial relationship with eukaryotic cells, known as endosymbiosis. As a result of such “co-habitation”, eukaryotic cells and mitochondria have evolved and adapted to life together, such that now, neither can survive alone.
4. Where do the proteins in mitochondria come from?
Because of the organelle’s unusual past, the molecular pieces that make up mitochondria have undergone some shuffling of their own. Mitochondria carry a small circular genome, a vestige of their days as free-living bacteria that has been winnowed during evolution to just a few protein-coding genes.
The human mitochondrial genome was decoded in 1981, a full 20 years before the human genome itself was decoded. The organelle’s genome consists of roughly 16,000 chemical units called base pairs, much smaller than the nuclear genome’s 3 billion base pairs. The mitochondrial genome includes just 37 genes: 13 genes that encode proteins and 24 additional non-protein coding genes.
The rest of the genes required for a functioning mitochondrion, roughly 1,200 to 1,500 in total, now reside in the nucleus. Identifying these genes from DNA sequence data alone has proven immensely difficult, which is why other large-scale approaches — namely proteomics and computational methods — are required to pinpoint them.
See also:
MitoCarta - Protein Catalogue for Mitochondria
CellNEWS - Friday, 11 July 2008
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ZenMaster
Posted by ZenMaster at Friday, July 11, 2008
Labels: DNA, evolution, genome, human, mitochondria, nucleus, proteome, research, sequence 0 comments
Researchers unveil near-complete protein catalogue for mitochondria
Friday, 11 July 2008

Imagine trying to figure out how your car's power train works from just a few of its myriad components: It would be nearly impossible. Scientists have long faced a similar challenge in understanding cells' tiny powerhouses — called "mitochondria" — from scant knowledge of their molecular parts.
Now, an international team of researchers has created the most comprehensive "parts list" to date for mitochondria, a compendium that includes nearly 1,100 proteins. By mining this critical resource, the researchers have already gained deep insights into the biological roles and evolutionary histories of several key proteins. In addition, this careful cataloguing has identified a mutation in a novel protein-coding gene as the cause behind one devastating mitochondrial disease. A full description of the work appears in the July 11 print edition of the journal Cell.
"For years, a fundamental question in cell biology has gone largely unanswered — what proteins function in mitochondria?" said Vamsi Mootha, an associate member at the Broad Institute of Harvard and MIT and a Harvard Medical School assistant professor at Massachusetts General Hospital, who led the study.
"By creating a comprehensive list, we now have a valuable resource that has already helped enhance our understanding of mitochondrial biology and disease."
Mitochondria are linchpins of cellular life, found within the cells of all eukaryotes from yeast to humans. These miniaturized organs ("organelles") are well known for their role in providing cellular energy. They have also been implicated in a wide range of normal and disease processes, including diabetes, neuro-degeneration, cancer, drug toxicity and aging.
Although mitochondria have their own genome — a vestige from their days as free-living bacteria — the vast majority of the critical mitochondrial proteins are derived not from their genome, but rather from the nuclear genome. However, even with the wealth of genome sequence data now available, scientists have struggled to identify which genes encode the roughly 1,200 proteins that make up a functional mitochondrion.
Researchers from the Broad Institute, Harvard Medical School, and Massachusetts General Hospital worked together to address this problem, drawing on the power of a multi-faceted approach that includes large-scale, mass spectrometry-based proteomics to measure proteins in mitochondria from a variety of tissues; computational methods to help identify those proteins that cannot be reliably detected; and microscopy to confirm within human cells the localization of presumptive mitochondrial proteins.
"The technologies and analytical methods for measuring proteins on a large scale are really transforming what we can learn about human biology," said Steve Carr, director of the Proteomics Platform at the Broad Institute and a co-author of the Cell paper.
"By applying them to mitochondria isolated from fourteen different mouse tissues, we've completed one of the most comprehensive proteomic analyses of any organelle to date."
As a result of their analyses, the researchers identified a total of 1,098 mitochondrial proteins to form a compendium they have named "MitoCarta," and which is available to the entire scientific community.
Notably, about one-third of this inventory has not been previously linked to the organelle.
To shed light on the functions of the newly uncovered mitochondrial proteins, the researchers compared the proteins' corresponding gene sequences across hundreds of species, from humans and fish to fungi and bacteria.
"Proteins with similar roles often share similar histories, meaning they're gained or lost together during evolution," said Mootha.
"We decided to use this tendency to our advantage to decipher how some mitochondrial proteins work."
By examining the organelle's proteins through this evolutionary lens, the researchers uncovered a striking pattern. A group of key mitochondrial proteins, known to be absent in yeast but otherwise present among eukaryotes, are actually missing from several other single-celled species. In organisms that have them, including humans and other mammals, these proteins contribute to a boot-shaped, multi-protein structure, which forms the gateway to a critical step in the energy-generation process. By virtue of these proteins' shared — and unusual — past, Mootha and his colleagues were able to identify several additional proteins that are also associated with this crucial mitochondrial structure, known as complex I.
In addition to offering insights into mitochondrial biology, these discoveries also paved the way for a breakthrough in understanding mitochondrial disease. For decades, doctors have diagnosed patients with deficiencies in complex I function. These disorders affect about 1 in 5,000 newborns, are genetic in origin, and are lethal in the first few years of life. Yet for many cases a culprit gene cannot be found.
However, thanks to MitoCarta and its corresponding evolutionary analyses, the researchers and their collaborators at the University of Melbourne and Royal Children's Hospital in Australia identified a mutation in a novel gene, called C8orf38, as one cause of complex I disease.
"Our finding underscores the power of this protein catalogue to open new vistas on disease," said Mootha.
"It promises to shed light not only on rare metabolic diseases, but common diseases as well."
Data access:
The mitochondrial protein compendium (MitoCarta) is freely available to researchers on the web.
In addition, all of the raw mass spectrometry files are available for download.
About the Broad Institute of MIT and Harvard
The Broad Institute of MIT and Harvard was founded in 2003 to bring the power of genomics to biomedicine. It pursues this mission by empowering creative scientists to construct new and robust tools for genomic medicine, to make them accessible to the global scientific community, and to apply them to the understanding and treatment of disease.
The Institute is a research collaboration that involves faculty, professional staff and students from throughout the MIT and Harvard academic and medical communities. It is jointly governed by the two universities.
Organized around Scientific Programs and Scientific Platforms, the unique structure of the Broad Institute enables scientists to collaborate on transformative projects across many scientific and medical disciplines.
Reference:
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
David J. Pagliarini, Sarah E. Calvo, Betty Chang, Sunil A. Sheth, Scott B. Vafai, Shao-En Ong, Geoffrey A. Walford, Canny Sugiana, Avihu Boneh, William K. Chen, David E. Hill, Marc Vidal, James G. Evans, David R. Thorburn, Steven A. Carr, and Vamsi K. Mootha
Cell, Vol 134, 112-123, 11 July 2008
See also:
Primer on Mitochondria
CellNEWS - Friday, 11 July 2008
.........
ZenMaster
Posted by ZenMaster at Friday, July 11, 2008
Labels: DNA, genome, human, mitochondria, nucleus, proteome, research, sequence 0 comments