| Discipline | Biochemistry |
|---|---|
| Language | English |
| Publication details | |
| History | 1947–present |
| Publisher | |
| Frequency | 100/year |
| Hybrid | |
| Standard abbreviations | |
| ISO 4 | Biochim. Biophys. Acta |
| Indexing | |
| ISSN | 0006-3002 |
| Links | |
Biochimica et Biophysica Acta (BBA) is a peer-reviewed scientific journal in the field of biochemistry and biophysics that was established in 1947. The journal is published by Elsevier with a total of 100 annual issues in ten specialised sections.
Biochimica et Biophysica Acta was first published in 1947 and was the first international journal to be devoted to the joint fields of biochemistry and biophysics. [1] Published by Elsevier in cooperation with Interscience, it was the first international journal to be launched by Elsevier. [1] The journal first made a profit in 1951. [1]
Early papers were published in English, French, and German, with summaries in all three languages. [2] The majority of papers in the first volume originated in northern and western Europe, with a minority from the US and elsewhere; contributors included William Astbury, Jean Brachet, Hubert Chantrenne, Pierre Desnuelle, Claude Fromageot, Heinz Holter, Raymond Jeener, Felix Haurowitz, Edgar Lederer, Kaj Linderstrøm-Lang, Roger Vendrely, Jean-Marie Wiame, and Ralph W.G. Wyckoff. [3]
Important papers from these early years include "Studies on the structure of ribonucleic acids" by Boris Magasanik and Erwin Chargaff (1951), [4] part of the evidence on which Watson and Crick's model of the structure of DNA was based, and "Enzymic synthesis of deoxyribonucleic acid" by Arthur Kornberg and colleagues (1956), [5] an early report on the isolation of DNA polymerase I. [1]
Biochimica et Biophysica Acta was published as a single title until 1962, when additional sections began to be published alongside the main journal: first Specialized Section on Nucleic Acids and Related Subjects and then, from 1963, Specialized Section on Enzymological Subjects and Specialized Section on Lipids and Related Subjects. [6]
In 1964, the main journal became Biochimica et Biophysica Acta (BBA) - General Subjects, and was published alongside the three established sections plus Specialized Section on Biophysical Subjects and Specialized Section on Mucoproteins and Mucopolysaccharides . In 1965, the specialist sections were renamed, becoming Biophysics including Photosynthesis, Nucleic Acids and Protein Synthesis, Enzymology and Biological Oxidation, Lipids and Lipid Metabolism and Mucoproteins and Mucopolysaccharides (ceased in 1965). In 1967, Biophysics including Photosynthesis split into Bioenergetics and Biomembranes, and Enzymology and Biological Oxidation split into Enzymology and Protein Structure; the latter pair rejoined in 1982 to become Protein Structure and Molecular Enzymology. Further sections were Molecular Cell Research, launched in 1982, and Molecular Basis of Disease, launched in 1990. [6]
In addition to the specialised research sections, three review sections were launched in the early 1970s: Reviews on Biomembranes (1972–2000), Reviews on Bioenergetics (1973–87) and Reviews on Cancer (from 1974). The former two were later incorporated into the respective research sections. [6]
Further name changes are given in the table in the following section.
As of 2014, Biochimica et Biophysica Acta encompasses ten specialised sections with a total of 100 annual issues in ten volumes. Over 16,000 pages were published in 2011. The journal sections are published separately, with one annual volume per section (two for Reviews on Cancer), but form part of the volume numbering for Biochimica et Biophysica Acta. [6] Sections are available individually or as part of a combined subscription. All papers are in English. [7] The overall editor-in-chief is Ulrich Brandt (Goethe University Frankfurt, Germany). [8]
The sections published in 2014 were as follows: [6]
| Name | ISSN | Annual issues | Impact factor [9] | Notes |
|---|---|---|---|---|
| BBA – Bioenergetics [10] | ISSN 0005-2728 | 12 | 4.428 | Commenced 1967; formerly part of BBA – Biophysics including Photosynthesis (1965–1966). Incorporates BBA – Reviews on Bioenergetics |
| BBA – Biomembranes [11] | ISSN 0005-2736 | 12 | 4.019 | Commenced 1967; formerly part of BBA – Biophysics including Photosynthesis (1965–66). Incorporates BBA – Reviews on Biomembranes |
| BBA – Gene Regulatory Mechanisms [12] | ISSN 1874-9399 | 12 | 6.304 | Commenced 2008; continuation of BBA – Gene Structure and Expression (0167-4781; 1982–2007), BBA – Nucleic Acids and Protein Synthesis (1963–1981) and BBA – Specialized Section on Nucleic Acids and Related Subjects (1962–64) |
| BBA – General Subjects [13] | ISSN 0304-4165 | 12 | 4.117 | Commenced 1964; continuation of Biochimica et Biophysica Acta |
| BBA – Molecular and Cell Biology of Lipids [14] | ISSN 1388-1981 | 12 | 5.228 | Commenced 1998; continuation of BBA – Lipids and Lipid Metabolism (1965–98) and BBA – Specialized Section on Lipids and Related Subjects (1963–64) |
| BBA – Molecular Basis of Disease [15] | ISSN 0925-4439 | 12 | 6.633 | Commenced 1990 |
| BBA – Molecular Cell Research [16] | ISSN 0167-4889 | 12 | 5.011 | Commenced 1982 |
| BBA – Proteins and Proteomics [17] | ISSN 1570-9639 | 12 | 4.125 | Commenced 2002; continuation of BBA – Protein Structure and Molecular Enzymology (1982–2002), BBA – Enzymology (1967–81), BBA – Protein Structure (1967–81), BBA – Enzymology and Biological Oxidation (1965–66), BBA – Specialized Section on Enzymological Subjects (1963–64) |
| BBA – Reviews on Cancer [18] | ISSN 0304-419X | 4 | 11.414 | Commenced 1974 |
BBA is abstracted and indexed by BIOSIS, Chemical Abstracts Service, Current Contents/Life Sciences, EMBASE, EMBiology, Index Chemicus, MEDLINE/Index Medicus, Science Citation Index, and Sociedad Iberoamericana de Informacion Cientifica. [19]
Articles are available online as PDFs and HTML; access is largely limited to subscribers, with a small number of sponsored open-access articles.
Lipid-anchored proteins are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. They are a type of proteolipids.
Antimicrobial peptides (AMPs), also called host defence peptides (HDPs) are part of the innate immune response found among all classes of life. Fundamental differences exist between prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antimicrobials which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize biological membranes, can form transmembrane channels, and may also have the ability to enhance immunity by functioning as immunomodulators.
Monensin is a polyether antibiotic isolated from Streptomyces cinnamonensis. It is widely used in ruminant animal feeds.
In biology, membrane fluidity refers to the viscosity of the lipid bilayer of a cell membrane or a synthetic lipid membrane. Lipid packing can influence the fluidity of the membrane. Viscosity of the membrane can affect the rotation and diffusion of proteins and other bio-molecules within the membrane, there-by affecting the functions of these things.
Lanosterol 14α-demethylase (CYP51A1) is the animal version of a cytochrome P450 enzyme that is involved in the conversion of lanosterol to 4,4-dimethylcholesta-8(9),14,24-trien-3β-ol. The cytochrome P450 isoenzymes are a conserved group of proteins that serve as key players in the metabolism of organic substances and the biosynthesis of important steroids, lipids, and vitamins in eukaryotes. As a member of this family, lanosterol 14α-demethylase is responsible for an essential step in the biosynthesis of sterols. In particular, this protein catalyzes the removal of the C-14α-methyl group from lanosterol. This demethylation step is regarded as the initial checkpoint in the transformation of lanosterol to other sterols that are widely used within the cell.
Peridinin is a light-harvesting apocarotenoid, a pigment associated with chlorophyll and found in the peridinin-chlorophyll-protein (PCP) light-harvesting complex in dinoflagellates, best studied in Amphidinium carterae.
In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase (EC 1.14.13.96) is an enzyme that catalyzes the chemical reaction
A lipopeptide is a molecule consisting of a lipid connected to a peptide. They are able to self-assemble into different structures. Many bacteria produce these molecules as a part of their metabolism, especially those of the genus Bacillus, Pseudomonas and Streptomyces. Certain lipopeptides are used as antibiotics. Due to the structural and molecular properties such as the fatty acid chain, it poses the effect of weakening the cell function or destroying the cell. Other lipopeptides are toll-like receptor agonists. Certain lipopeptides can have strong antifungal and hemolytic activities. It has been demonstrated that their activity is generally linked to interactions with the plasma membrane, and sterol components of the plasma membrane could play a major role in this interaction. It is a general trend that adding a lipid group of a certain length to a lipopeptide will increase its bactericidal activity. Lipopeptides with a higher amount of carbon atoms, for example 14 or 16, in its lipid tail will typically have antibacterial activity as well as anti-fungal activity. Therefore, an increase in the alkyl chain can make lipopeptides soluble in water. As well, it opens the cell membrane of the bacteria, so antimicrobial activity can take place.
Phospholipid scramblase 3 is an enzyme that in humans is encoded by the PLSCR3 gene. Like the other phospholipid scramblase family members, PLS3 is a type II plasma membrane protein that is rich in proline and integral in apoptosis, or programmed cell death. The regulation of apoptosis is critical for both cell development and tissue homeostasis
Tricarboxylate transport protein, mitochondrial, also known as tricarboxylate carrier protein and citrate transport protein (CTP), is a protein that in humans is encoded by the SLC25A1 gene. SLC25A1 belongs to the mitochondrial carrier gene family SLC25. High levels of the tricarboxylate transport protein are found in the liver, pancreas and kidney. Lower or no levels are present in the brain, heart, skeletal muscle, placenta and lung.
Prostasomes are extracellular vesicles secreted by the prostate gland epithelial cells into seminal fluid. They possess an unusual lipid composition and a tight and highly ordered structure of their lipid bilayer membrane, resembling that of lipid raft domains. Prostasomes appear to improve sperm motility and protect against attacks from the female immune defense during the passage to the egg.
In the field of enzymology, a proton ATPase, or H+-ATPase, is an enzyme that catalyzes the following chemical reaction:
Protein–lipid interaction is the influence of membrane proteins on the lipid physical state or vice versa.
One property of a lipid bilayer is the relative mobility (fluidity) of the individual lipid molecules and how this mobility changes with temperature. This response is known as the phase behavior of the bilayer. Broadly, at a given temperature a lipid bilayer can exist in either a liquid or a solid phase. The solid phase is commonly referred to as a “gel” phase. All lipids have a characteristic temperature at which they undergo a transition (melt) from the gel to liquid phase. In both phases the lipid molecules are constrained to the two dimensional plane of the membrane, but in liquid phase bilayers the molecules diffuse freely within this plane. Thus, in a liquid bilayer a given lipid will rapidly exchange locations with its neighbor millions of times a second and will, through the process of a random walk, migrate over long distances.
Biophysical chemistry is a physical science that uses the concepts of physics and physical chemistry for the study of biological systems. The most common feature of the research in this subject is to seek an explanation of the various phenomena in biological systems in terms of either the molecules that make up the system or the supra-molecular structure of these systems. Apart from the biological applications, recent research showed progress in the medical field as well.
The enzyme exo-(1→4)-α-D-glucan lyase (EC 4.2.2.13, α-(1→4)-glucan 1,5-anhydro-D-fructose eliminase, α-1,4-glucan exo-lyase, α-1,4-glucan lyase, GLase) is an enzyme with systematic name (1→4)-α-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming). This enzyme catalyses the following chemical reaction
The Canadian Journal of Biochemistry and Physiology is a defunct peer-reviewed scientific journal of biochemistry and physiology established in 1954 as the continuation of the Canadian Journal of Medical Sciences and published by NRC Research Press. In 1964 it split into two different journals Canadian Journal of Biochemistry and Canadian Journal of Physiology and Pharmacology.
Sunil Kumar Podder was an Indian molecular biologist and biophysicist, known for his biophysical studies on Ligand. Focusing his researches on the recognition processes in biological systems and their chemical specificity, he proposed a model for measuring the specificity using free energy of association of amino acids of proteins with nucleic acid bases.
Roland Winter is a biophysical chemist who studies the structure, dynamics, energetics, and phase behavior of biological membranes and proteins. He was dean of the Department of Chemistry and Chemical Biology at Technical University of Dortmund, Germany.
A single-pass membrane protein also known as single-spanning protein or bitopic protein is a transmembrane protein that spans the lipid bilayer only once. These proteins may constitute up to 50% of all transmembrane proteins, depending on the organism, and contribute significantly to the network of interactions between different proteins in cells, including interactions via transmembrane alpha helices. They usually include one or several water-soluble domains situated at the different sides of biological membranes, for example in single-pass transmembrane receptors. Some of them are small and serve as regulatory or structure-stabilizing subunits in large multi-protein transmembrane complexes, such as photosystems or the respiratory chain. More than 2300 single-pass membrane proteins were identified in the human genome.
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