Cell Press

Last updated
Cell Press
Parent company Elsevier
Founded1986;34 years ago (1986)
FounderBenjamin Lewin
Country of originUnited States
Headquarters location Cambridge, Massachusetts, U.S.
Key peopleEmilie Marcus, CEO and editor-in-chief, Cell
Keith Wollman, VP of Operations
Joanne Sheppard, VP of Business Development
Meredith Adinolfi, Production Director
Deborah Sweet, Publishing Director
Peter Lee, Publishing Director
Elena Porro, Publishing Director
Jonathan Atkinson, Marketing Director
Jonathan Christison, Commercial Sales Director
Publication types Scientific journals
Official website www.cell.com

Cell Press, an imprint of Elsevier, is a publisher of biomedical journals, including Cell and Neuron .



Benjamin Lewin founded Cell in January 1974, under the aegis of MIT Press. He then bought the title and established an independent Cell Press in 1986. The company spun off new journals as follows: Neuron in March 1988; Immunity in April 1994; and Molecular Cell in December 1997. Benjamin Lewin left in October 1999, after having sold Cell Press to Elsevier the previous April.

Since that time, Cell Press has launched a number of new titles: Developmental Cell in July 2001; Cancer Cell in February 2002; Cell Metabolism in January 2005; Cell Host & Microbe in March 2007; Cell Stem Cell in July 2007; Cell Systems in July 2015; Chem in July 2016; Joule in September 2017; iScience in March 2018; and One Earth in September 2019.

Meanwhile, three additional Elsevier journals have joined the Cell Press group: Current Biology launched in January 1996, which became part of Cell Press in early 2001; Cell Chemical Biology (formerly titled Chemistry & Biology) launched on April 15, 1994 and joined Cell Press in January 2002; and Structure launched in 1993, which merged with the journal Folding & Design in early 1999. At that point, the name changed to Structure with Folding & Design but reverted to Structure at the beginning of 2001, when the journal joined Cell Press.

In October 1995, Cell.com was launched and included tables of contents, abstracts, and information for authors and subscribers. Full-text online versions at Cell.com, Neuron.org, and Immunity.com were launched in July 1997.

See also

Related Research Articles

Antibody Immune system protein

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region. Each tip of the "Y" of an antibody contains a paratope that is specific for one particular epitope on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly. Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance. The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region, which contains a conserved glycosylation site involved in these interactions. The production of antibodies is the main function of the humoral immune system.

Messenger RNA RNA that is read by the ribosome to produce a protein

In molecular biology, messenger RNA (mRNA) is a single-stranded molecule of RNA that corresponds to the genetic sequence of a gene, and is read by a ribosome in the process of synthesizing a protein.

Cerebral cortex Outer layer of the cerebrum of the mammalian brain

The cerebral cortex, also known as the cerebral mantle, is the outer layer of neural tissue of the cerebrum of the brain in humans and other mammals. The cerebral cortex mostly consists of the six-layered neocortex, with just ten per cent consisting of allocortex. It is separated into two cortices, by the longitudinal fissure that divides the cerebrum into the left and right cerebral hemispheres. The two hemispheres are joined beneath the cortex by the corpus callosum. The cerebral cortex is the largest site of neural integration in the central nervous system. It plays a key role in attention, perception, awareness, thought, memory, language, and consciousness.

Action potential Process by which neurons communicate with each other by changes in their membrane potentials

In physiology, an action potential (AP) occurs when the membrane potential of a specific cell location rapidly rises and falls: this depolarization then causes adjacent locations to similarly depolarize. Action potentials occur in several types of animal cells, called excitable cells, which include neurons, muscle cells, endocrine cells, glomus cells, and in some plant cells.


Histamine is an organic nitrogenous compound involved in local immune responses, as well as regulating physiological function in the gut and acting as a neurotransmitter for the brain, spinal cord, and uterus. Histamine is involved in the inflammatory response and has a central role as a mediator of itching. As part of an immune response to foreign pathogens, histamine is produced by basophils and by mast cells found in nearby connective tissues. Histamine increases the permeability of the capillaries to white blood cells and some proteins, to allow them to engage pathogens in the infected tissues. It consists of an imidazole ring attached to an ethylamine chain; under physiological conditions, the amino group of the side-chain is protonated.

An epitope, also known as antigenic determinant, is the part of an antigen that is recognized by the immune system, specifically by antibodies, B cells, or T cells. For example, the epitope is the specific piece of the antigen to which an antibody binds. The part of an antibody that binds to the epitope is called a paratope. Although epitopes are usually non-self proteins, sequences derived from the host that can be recognized are also epitopes.

Protein disulfide-isomerase

Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.

Modelling biological systems is a significant task of systems biology and mathematical biology. Computational systems biology aims to develop and use efficient algorithms, data structures, visualization and communication tools with the goal of computer modelling of biological systems. It involves the use of computer simulations of biological systems, including cellular subsystems, to both analyze and visualize the complex connections of these cellular processes.

Cell is a peer-reviewed scientific journal publishing research papers across a broad range of disciplines within the life sciences. Areas covered include molecular biology, cell biology, systems biology, stem cells, developmental biology, genetics and genomics, proteomics, cancer research, immunology, neuroscience, structural biology, microbiology, virology, physiology, biophysics, and computational biology. The journal was established in 1974 by Benjamin Lewin and is published twice monthly by Cell Press, an imprint of Elsevier.

DNA clamp

A DNA clamp, also known as a sliding clamp or β-clamp, is a protein complex that serves as a processivity-promoting factor in DNA replication. As a critical component of the DNA polymerase III holoenzyme, the clamp protein binds DNA polymerase and prevents this enzyme from dissociating from the template DNA strand. The clamp-polymerase protein–protein interactions are stronger and more specific than the direct interactions between the polymerase and the template DNA strand; because one of the rate-limiting steps in the DNA synthesis reaction is the association of the polymerase with the DNA template, the presence of the sliding clamp dramatically increases the number of nucleotides that the polymerase can add to the growing strand per association event. The presence of the DNA clamp can increase the rate of DNA synthesis up to 1,000-fold compared with a nonprocessive polymerase.

Neuromorphology is the study of nervous system form, shape, and structure. The study involves looking at a particular part of the nervous system from a molecular and cellular level and connecting it to a physiological and anatomical point of view. The field also explores the communications and interactions within and between each specialized section of the nervous system. Morphology is distinct from morphogenesis. Morphology is the study of the shape and structure of biological organisms, while morphogenesis is the study of the biological development of the shape and structure of organisms. Therefore, neuromorphology focuses on the specifics of the structure of the nervous system and not the process by which the structure was developed. Neuromorphology and morphogenesis, while two different entities, are nonetheless closely linked.

Protein domain Conserved part of a protein

A protein domain is a conserved part of a given protein sequence and tertiary structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three-dimensional structure and often can be independently stable and folded. Many proteins consist of several structural domains. One domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins.

Survival of motor neuron

Survival of motor neuron or survival motor neuron (SMN) is a protein that in humans is encoded by the SMN1 and SMN2 genes.


DNA-binding protein Ikaros also known as Ikaros family zinc finger protein 1 is a protein that in humans is encoded by the IKZF1 gene.

Small nuclear ribonucleoprotein polypeptide F

Small nuclear ribonucleoprotein F is a protein that in humans is encoded by the SNRPF gene.

Natural computing, also called natural computation, is a terminology introduced to encompass three classes of methods: 1) those that take inspiration from nature for the development of novel problem-solving techniques; 2) those that are based on the use of computers to synthesize natural phenomena; and 3) those that employ natural materials to compute. The main fields of research that compose these three branches are artificial neural networks, evolutionary algorithms, swarm intelligence, artificial immune systems, fractal geometry, artificial life, DNA computing, and quantum computing, among others.

Benjamin Lewin is a molecular biologist who founded the journal Cell and authored the textbook Genes. He is credited with building Cell into a cutting-edge journal of exciting biology in a very short time rivaling Nature and Science.

Avadhesha Surolia is a Glycobiologist at Indian Institute of Science (IISc), Bangalore. Presently, he is an Honorary Professor at the Molecular Biophysics Unit (MBU), IISc and holds the Bhatnagar fellowship of the Council of Scientific and Industrial Research (CSIR), India. He is known for his work on lectin structure and interactions, orientation and dynamics of cell surface carbohydrate receptors and protein folding, diabetes, anti-malarials and anti-cancer agents based on curcumin, flavonoids, etc. In addition, neuropathic pain, neurodegenerative disorders and the link between immunity and obsessive compulsive disorder are areas of his current interest

Jayant Bhalchandra Udgaonkar is an Indian biochemist, molecular biologist, academic and the Director of the Indian Institute of Science Education and Research, Pune. He was previously a senior professor at the National Centre for Biological Sciences. A J. C. Bose National Fellow, he is known for his studies on protein folding. He is an elected fellow of the Indian Academy of Sciences, Indian National Science Academy and The World Academy of Sciences. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 2000, for his contributions to biological sciences. He is the son of noted scientist Padmabhushan Bhalchandra Udgaonkar.