A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses.
A subclass of crystallins that provides the majority of refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Alpha-crystallins also act as molecular chaperones that bind to denatured proteins, keep them in solution and thereby maintain the translucency of the lens. The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits.
A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION.
The basic subunit of beta-crystallins.
The acidic subunit of beta-crystallins.
A subclass of crystallins that found in the lens (LENS, CRYSTALLINE) of VERTEBRATES. Gamma-crystallins are similar in structure to BETA-CRYSTALLINS in that they both form into a Greek key-like structure. They are composed of monomeric subunits.
A class of crystallins that provides refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Beta-crystallins are similar in structure to GAMMA-CRYSTALLINS in that they both contain Greek key motifs. Beta-crystallins exist as oligomers formed from acidic (BETA-CRYSTALLIN A CHAIN) and basic (BETA-CRYSTALLIN B CHAIN) subunits.
One of the subunits of alpha-crystallins. Unlike ALPHA-CRYSTALLIN B CHAIN the expression of ALPHA-CRYSTALLIN A CHAIN is limited primarily to the lens (LENS, CRYSTALLINE).
One of the alpha crystallin subunits. In addition to being expressed in the lens (LENS, CRYSTALLINE), alpha-crystallin B chain has been found in a variety of tissues such as HEART; BRAIN; MUSCLE; and KIDNEY. Accumulation of the protein in the brain is associated with NEURODEGENERATIVE DISEASES such as CREUTZFELDT-JAKOB SYNDROME and ALEXANDER DISEASE.
A subclass of crystallins found in the lens (LENS, CRYSTALLINE) in BIRDS and REPTILES. They are inactive forms of the enzyme argininosuccinate lyase.
Partial or complete opacity on or in the lens or capsule of one or both eyes, impairing vision or causing blindness. The many kinds of cataract are classified by their morphology (size, shape, location) or etiology (cause and time of occurrence). (Dorland, 27th ed)
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease ARGININOSUCCINIC ACIDURIA in man. EC
One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.
Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Proteins prepared by recombinant DNA technology.
Maf proto-oncogene protein is the major cellular homolog of the V-MAF ONCOGENE PROTEIN. It was the first of the mammalian MAF TRANSCRIPTION FACTORS identified, and it is induced in activated T-LYMPHOCYTES and regulates GENETIC TRANSCRIPTION of INTERLEUKIN-4. c-maf is frequently translocated to an immunoglobulin locus in MULTIPLE MYELOMA.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Polyacrylamide gel electrophoresis under conditions in which the components, such as PROTEINS, being separated can remain in their naturally folded state.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.
Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.

Decreased heat stability and increased chaperone requirement of modified human betaB1-crystallins. (1/136)

PURPOSE: To determine how deamidation and partial loss of the N- and C-terminal extensions alter the heat stability of betaB1-crystallin. METHODS: Human lens betaB1, a deamidated betaB1, Q204E, and alphaA-crystallins were expressed. Truncated betaB1 was generated by proteolytic removal of part of its terminal extensions. The aggregation and precipitation of these proteins due to heating was monitored by circular dichroism and light scattering. The effect of heat on the stability of both monomers and oligomers was investigated. The flexibility of the extensions in wild type and deamidated betaB1 was assessed by 1H NMR spectroscopy. RESULTS: With heat, deamidated betaB1 precipitated more readily than wild type betaB1. Similar effects were obtained for either monomers or oligomers. Flexibility of the N-terminal extension in deamidated betaB1 was significantly reduced compared to the wild type protein. Truncation of the extensions further increased the rate of heat-induced precipitation of deamidated betaB1. The presence of the molecular chaperone, alphaA-crystallin, prevented precipitation of modified betaB1s. More alphaA was needed to chaperone the truncated and deamidated betaB1 than deamidated betaB1 or truncated betaB1. CONCLUSIONS: Deamidation and truncation of betaB1 led to destabilization of the protein and decreased stability to heat. Decreased stability of lens crystallins may contribute to their insolubilization and cataract formation.  (+info)

Quantification of chick lens alphaA- and delta-crystallins in experimentally induced ametropia. (2/136)

PURPOSE: The role of the lens in experimentally induced ametropia is not known. A recent study of the chick lens demonstrated optical quality deterioration with the induction of refractive errors, without alteration in lens morphology, size or shape. A change in lens gradient of refractive index (which is dependent on alpha-, beta-, and delta-crystallin concentration and arrangement), could underlie this observation. The purpose of this work was to quantify the concentrations of alphaA- and delta-crystallin in lenses from chick eyes with induced high myopia or hyperopia. METHODS: White Leghorn chicks were unilaterally fitted on the day of hatching either with translucent plastic goggles to induce form-deprivation myopia (n=21) or with +15 D defocus goggles to induce hyperopia (n=14). The ungoggled contralateral eyes were used as controls. The chicks were refracted twice, once on the day of hatching and again seven days later, using streak retinoscopy. On day 7 chicks were sacrificed, lenses decapsulated, and soluble proteins were isolated. Western blot assays were optimized and used to assess crystallin concentration. RESULTS: Analysis revealed no significant difference in alphaA- or delta-crystallin concentration in lenses from eyes induced with form-deprivation myopia and hyperopia as compared to their respective control eyes. Analysis of the difference in medians of delta-crystallin between the control and treated groups of the myopia and hyperopia experiments revealed significance (p=0.030). CONCLUSIONS: This study suggests that with the induction of ametropia, the increased lens spherical aberration previously noted is not due to a change in the absolute concentration of lens alphaA- or delta-crystallin. However, results suggest that the myopic and hyperopic treatments had different effects on lens delta-crystallin concentration. Further investigation is necessary to expand the current knowledge of the role played by the lens in experimental ametropia.  (+info)

Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens. (3/136)

BACKGROUND: One approach to resolving some of the in vivo functions of alpha-crystallin is to generate animal models where one or both of the alpha-crystallin gene products have been eliminated. In the single alpha-crystallin knockout mice, the remaining alpha-crystallin may fully or partially compensate for some of the functions of the missing protein, especially in the lens, where both alpha A and alpha B are normally expressed at high levels. The purpose of this study was to characterize gross lenticular morphology in normal mice and mice with the targeted disruption of alpha A- and alpha B-crystallin genes (alpha A/BKO). METHODS: Lenses from 129SvEvTac mice and alpha A/BKO mice were examined by standard scanning electron microscopy and confocal microscopy methodologies. RESULTS: Equatorial and axial (sagittal) dimensions of lenses for alpha A/BKO mice were significantly smaller than age-matched wild type lenses. No posterior sutures or fiber cells extending to the posterior capsule of the lens were found in alpha A/BKO lenses. Ectopical nucleic acid staining was observed in the posterior subcapsular region of 5 wk and anterior subcapsular cortex of 54 wk alpha A/BKO lenses. Gross morphological differences were also observed in the equatorial/bow, posterior and anterior regions of lenses from alpha A/BKO mice as compared to wild mice. CONCLUSION: These results indicated that both alpha A- and alpha B-crystallin are necessary for proper fiber cell formation, and that the absence of alpha-crystallin can lead to cataract formation.  (+info)

Reduced survival of lens epithelial cells in the alphaA-crystallin-knockout mouse. (4/136)

alphaA-Crystallin (alphaA) is a molecular chaperone expressed preferentially in the lens. alphaA transcripts are first detected during the early stages of lens development and its synthesis continues as the lens grows throughout life. alphaA(-/-) mouse lenses are smaller than controls, and lens epithelial cells derived from these mice have diminished growth in culture. In the current work, we tested the hypothesis thatalphaA prevents cell death at a specific stage of the cell cycle in vivo. Seven-day-old 129Sv (wild-type) and alphaA(-/-) mice were injected with 5-bromo-2'-deoxyuridine (BrdU) to label newly synthesized DNA in proliferating cells. To follow the fate of the labeled cells, wholemounts of the capsule epithelial explants were made at successive times after the BrdU pulse, and the labeling index was determined. Immunofluorescence and confocal microscopy showed that both wild-type and alphaA(-/-) cells had a 3-hour labeling index of 4.5% in the central region of the wholemount, indicating that the number of cells in S phase was the same. Twenty-four hours after the pulse, individual cells labeled with BrdU had divided and BrdU-labeled cells were detected in pairs. The 24-hour labeling index in the wild-type lens was 8.6%, but in the alphaA(-/-) lens it was significantly lower, suggesting that some of the cells failed to divide and/or that the daughter cells died during mitosis. TUNEL labeling was rarely detected in the wild-type lens, but was significant and always detected in pairs in the alphaA(-/-) wholemounts. Dual labeling with TUNEL and BrdU also suggested that the labeled cells were dying in pairs in the alphaA(-/-) lens epithelium. Immunolabeling of wholemounts with beta-tubulin antibodies indicated that the anaphase spindle in a significant proportion of alphaA(-/-) cells was not well organized. Examination of the cellular distribution of alphaA in cultured lens epithelial cells showed that it was concentrated in the intercellular microtubules of cells undergoing cytokinesis. These data suggest that alphaA expression in vivo protects against cell death during mitosis in the lens epithelium, and the smaller size of the alphaA(-/-) lens may be due to a decrease in the net production of epithelial cells.  (+info)

Alteration of protein-protein interactions of congenital cataract crystallin mutants. (5/136)

PURPOSE: A recent study demonstrated the presence of protein-protein interactions among lens crystallins in a mammalian cell two-hybrid system assay and speculated about the significance of these interactions for protein solubility and lens transparency. The current study extends those findings to the following crystallin genes involved in some congenital cataracts: CRYAA (R116C), CRYAB (R120G), and CRYGC (T5P). METHODS: A mammalian two-hybrid system was used to assay the protein-protein interactions. Congenital cataract crystallin genes were cloned and fused into the two-hybrid system vectors (target and prey proteins). Together, with the third vector containing a reporter gene, chloramphenicol acetyltransferase (CAT), they were cotransfected into human HeLa cells. The presence of protein-protein interactions and the strength of these interactions were assayed by CAT ELISA. RESULTS: The pattern of changes in protein-protein interactions of those congenital cataract gene products with the three major crystallins, alphaA- or alphaB-, betaB2-, and gammaC-crystallins, differed. For the T5P gammaC-crystallin, most of the interactions were decreased; for the R116C alphaA-crystallin, the interactions with betaB2- and gammaC-crystallin decreased and those with alphaB-crystallin and heat-shock protein (Hsp)27 increased; and for the R120G alphaB-crystallin, the interactions with alphaA- and alphaB-crystallin decreased, but those with betaB2- and gammaC-crystallin increased slightly. An attempt was made to interpret the results on the basis of conformational change and disruption of dimeric interaction involving beta-strands. CONCLUSIONS: The results clearly indicate that crystallin mutations involved in congenital cataracts altered protein-protein interactions, which may contribute to decreased protein solubility and formation of cataract.  (+info)

Immunological detection of D-beta-aspartate-containing protein in lens-derived cell lines. (6/136)

PURPOSE: Although the presence of biologically uncommon D-beta-aspartate (D-beta-Asp) in lens protein is thought to be related to aging, we recently found this isomer in lens alphaA-crystallin from human newborns. The objective of this study was to examine whether D-beta-Asp occurs in protein from lens-derived cell lines. METHODS: We examined the expression of D-beta-Asp-containing protein in the lens-derived cell lines alphaTN4-1 and N/N1003A, by western blot and immunoprecipitation analysis using a polyclonal antibody against Gly-Leu-D-beta-Asp-Ala-Thr-Gly-Leu-D-beta-Asp-Ala-Thr-Gly-Leu-D-beta-Asp-Ala-Thr (peptide 3R), which corresponds to three repeats of positions 149-153 in human alphaA-crystallin. The anti-peptide 3R antibody, prepared in a previous study, is a useful tool for investigating D-beta-Asp-containing peptides. RESULTS: Western immunoblot and immunoprecipitation analysis showed that a 50 kDa protein in N/N1003A cells was strongly immunoreactive with the anti-peptide 3R antibody. Antibodies against alphaA- and alphaB-crystallin also stained this protein. On the other hand, the alphaTN4-1 cell line only expressed proteins of about 20 kDa, which also reacted to antibodies against alphaA-crystallin and alphaB-crystallin. CONCLUSIONS: The results indicate that the N/N1003A cell line expressed a 50 kDa D-beta-Asp-containing protein, which may share a common amino acid sequence with alphaA- and alphaB-crystallin.  (+info)

Induction of the differentiation of lentoids from primate embryonic stem cells. (7/136)

PURPOSE: To produce lens cells from primate embryonic stem (ES) cells in a reproducible, controlled manner. METHODS: Cynomologus monkey ES cells were induced to differentiate by stromal cell-derived inducing activity (SDIA). The lentoids produced by this treatment were processed for immunohistochemical and immunoblotting analysis. The effect of varying the concentration of fibroblast growth factor (FGF)-2 and the density of the ES colonies plated during the differentiation process were also examined. RESULTS: After a 2- to 3-week induction period, lentoids were produced by a subpopulation of ES colonies. Western blot analysis and immunohistochemistry revealed that these lentoids expressed alphaA-crystallin and Pax6. The number of lentoids resulting from treatment increased with increasing FGF-2 concentration and plated colony density. CONCLUSIONS: The differentiation of primate ES cells into lentoids can be achieved by treatment with SIDA. ES cells can be used to facilitate a greater understanding of the mechanisms functioning in differentiation in vivo and in vitro.  (+info)

Pathogenesis of axonal dystrophy and demyelination in alphaA-crystallin-expressing transgenic mice. (8/136)

We recently described a transgenic mouse strain overexpressing hamster alphaA-crystallin, a small heat shock protein, under direction of the hamster vimentin promoter. As a result myelin was degraded and axonal dystrophy in both central nervous system (especially spinal cord) and peripheral nervous system occurred. Homozygous transgenic mice developed hind limb paralysis after 8 weeks of age and displayed progressive loss of myelin and axonal dystrophy in both the central and peripheral nervous system with ongoing age. Pathologically the phenotype resembled, to a certain extent, neuroaxonal dystrophy. The biochemical findings presented in this paper (activity of the enzymes superoxide dismutase, catalase and transglutamase, myelin protein zero expression levels and blood sugar levels) confirm this pathology and exclude other putative pathologies like Amyothrophic Lateral Sclerosis and Hereditary Motor and Sensory Neuropathy. Consequently, an excessive cytoplasmic accumulation of the transgenic protein or a disturbance of the normal metabolism are considered to cause the observed neuropathology. Therefore, extra-ocular alphaA-crystallin-expressing transgenic mice may serve as a useful animal model to study neuroaxonal dystrophy.  (+info)

Crystallins are the major proteins found in the lens of the eye in vertebrates. They make up about 90% of the protein content in the lens and are responsible for maintaining the transparency and refractive properties of the lens, which are essential for clear vision. There are two main types of crystallins, alpha (α) and beta/gamma (β/γ), which are further divided into several subtypes. These proteins are highly stable and have a long half-life, which allows them to remain in the lens for an extended period of time. Mutations in crystallin genes have been associated with various eye disorders, including cataracts and certain types of glaucoma.

Alpha-crystallins are small heat shock proteins found in the lens of the eye. They are composed of two subunits, alpha-A and alpha-B, which can form homo- or hetero-oligomers. Alpha-crystallins have chaperone-like activity, helping to prevent protein aggregation and maintain transparency of the lens. Additionally, they play a role in maintaining the structural integrity of the lens and protecting it from oxidative stress. Mutations in alpha-crystallin genes have been associated with certain forms of cataracts and other eye diseases.

The crystalline lens is a biconvex transparent structure in the eye that helps to refract (bend) light rays and focus them onto the retina. It is located behind the iris and pupil and is suspended by small fibers called zonules that connect it to the ciliary body. The lens can change its shape to accommodate and focus on objects at different distances, a process known as accommodation. With age, the lens may become cloudy or opaque, leading to cataracts.

Beta-crystallin B chain is a protein that forms part of the beta-crystallin complex, which is a major structural component of the vertebrate eye lens. The beta-crystallins are organized into two subgroups, beta-A and beta-B, based on their structural and genetic characteristics.

The beta-B crystallin proteins are encoded by four genes (CRYBB1, CRYBB2, CRYBB3, and CRYBB4) that are located in a cluster on chromosome 22 in humans. These proteins have a molecular weight of approximately 25 kDa and are composed of four distinct domains: an N-terminal domain, two Greek key motifs, and a C-terminal domain.

The beta-crystallin B chain proteins play important roles in maintaining the transparency and refractive properties of the eye lens. Mutations in these genes have been associated with various forms of cataracts, which are clouding of the eye lens that can lead to vision loss.

Beta-crystallin A chain is a protein that is a component of the beta-crystallin complex, which is a major structural element of the vertebrate eye lens. The beta-crystallins are organized into two subfamilies, called beta-A and beta-B, based on their primary structures.

The beta-crystallin A chain is a polypeptide chain that contains approximately 100 amino acids and has a molecular weight of around 12 kilodaltons. It is encoded by the CRYBA1 gene in humans. The protein is characterized by four conserved domains, called Greek key motifs, which are involved in the formation of the quaternary structure of the beta-crystallin complex.

Mutations in the CRYBA1 gene have been associated with various forms of congenital cataracts, which are clouding of the eye lens that can lead to visual impairment or blindness. The precise function of beta-crystallins is not fully understood, but they are thought to play a role in maintaining the transparency and refractive properties of the eye lens.

Gamma-crystallins are a type of structural protein found in the lens of the eye. They are part of the crystallin family, which also includes alpha- and beta-crystallins. These proteins are responsible for maintaining the transparency and refractive properties of the lens, allowing light to pass through and focus on the retina. Mutations in the genes that encode gamma-crystallins have been associated with various forms of cataracts, which are clouding of the lens that can impair vision. Gamma-crystallins are primarily expressed during embryonic development and decrease in expression after birth.

Beta-crystallins are proteins that make up a significant portion of the lens in our eyes. They are part of the crystallin family, which also includes alpha- and gamma-crystallins. These proteins are essential for maintaining the transparency and refractive properties of the eye's lens, allowing us to focus light onto the retina.

Beta-crystallins are organized into two subgroups: beta-A and beta-B. Each subgroup is made up of several different proteins called isoforms, which vary slightly in their amino acid sequences. These isoforms are produced by alternative splicing of the beta-crystallin genes during gene expression.

Mutations in the genes that encode beta-crystallins have been associated with various eye disorders, including cataracts and certain inherited forms of blindness. Cataracts are characterized by the clouding or opacification of the lens, which can lead to vision loss if not treated surgically. Inherited forms of blindness such as congenital nuclear cataracts and retinal degeneration have also been linked to mutations in beta-crystallin genes.

Overall, beta-crystallins play a crucial role in maintaining the health and function of our eyes, and their dysregulation can contribute to various eye disorders.

Alpha-Crystallin A Chain is a protein that is part of the alpha-crystallin family, which are small heat shock proteins. These proteins play a role in protecting cells from stress and aggregation of other proteins. Alpha-Crystallin A Chain is found in various tissues, including the eye lens, where it helps maintain lens transparency and prevent cataracts. Mutations in the gene that encodes alpha-Crystallin A Chain have been associated with certain inherited forms of cataracts.

Alpha-Crystallin B chain is a protein that is a component of the eye lens. It is one of the two subunits of the alpha-crystallin protein, which is a major structural protein in the lens and helps to maintain the transparency and refractive properties of the lens. Alpha-Crystallin B chain is produced by the CRYAB gene and has chaperone-like properties, helping to prevent the aggregation of other proteins and contributing to the maintenance of lens clarity. Mutations in the CRYAB gene can lead to various eye disorders, including cataracts and certain types of glaucoma.

Delta-crystallins are a subclass of crystallin proteins found in the lens of the eye. They are part of the beta/gamma-crystallin family, which are structural proteins that make up the majority of the protein content in the vertebrate lens. These proteins play an important role in maintaining the transparency and refractive properties of the lens, allowing for clear vision.

Delta-crystallins specifically refer to two proteins, delta1-crystallin and delta2-crystallin, which are expressed in a tissue-specific manner in the eye lens. They share a similar structure with other beta/gamma-crystallins but have distinct functional differences. Delta-crystallins have been found to have chaperone-like activity, helping to prevent protein misfolding and aggregation in the lens. Additionally, delta2-crystallin has been shown to have antioxidant properties, which may help protect the eye lens from oxidative damage.

Mutations in delta-crystallin genes have been associated with various forms of cataracts, which are clouding of the eye lens that can lead to vision loss. Understanding the structure and function of delta-crystallins is important for developing potential therapies for cataracts and other eye diseases.

A cataract is a clouding of the natural lens in the eye that affects vision. This clouding can cause vision to become blurry, faded, or dim, making it difficult to see clearly. Cataracts are a common age-related condition, but they can also be caused by injury, disease, or medication use. In most cases, cataracts develop gradually over time and can be treated with surgery to remove the cloudy lens and replace it with an artificial one.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Polymerase Chain Reaction (PCR) is a laboratory technique used to amplify specific regions of DNA. It enables the production of thousands to millions of copies of a particular DNA sequence in a rapid and efficient manner, making it an essential tool in various fields such as molecular biology, medical diagnostics, forensic science, and research.

The PCR process involves repeated cycles of heating and cooling to separate the DNA strands, allow primers (short sequences of single-stranded DNA) to attach to the target regions, and extend these primers using an enzyme called Taq polymerase, resulting in the exponential amplification of the desired DNA segment.

In a medical context, PCR is often used for detecting and quantifying specific pathogens (viruses, bacteria, fungi, or parasites) in clinical samples, identifying genetic mutations or polymorphisms associated with diseases, monitoring disease progression, and evaluating treatment effectiveness.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Argininosuccinate Lyase is an enzyme that plays a crucial role in the urea cycle, which is the metabolic pathway responsible for eliminating excess nitrogen waste from the body. This enzyme is responsible for catalyzing the conversion of argininosuccinate into arginine and fumarate.

The urea cycle occurs primarily in the liver and helps to convert toxic ammonia, a byproduct of protein metabolism, into urea, which can be safely excreted in urine. Argininosuccinate lyase is essential for this process, as it helps to convert argininosuccinate, an intermediate compound in the cycle, into arginine, which can then be recycled back into the urea cycle or used for other physiological processes.

Deficiencies in argininosuccinate lyase can lead to a rare genetic disorder known as citrullinemia, which is characterized by elevated levels of citrulline and ammonia in the blood, as well as neurological symptoms such as seizures, developmental delays, and intellectual disability. Treatment for citrullinemia typically involves a low-protein diet, supplementation with arginine and other essential amino acids, and in some cases, liver transplantation.

Adrenergic receptors are a type of G protein-coupled receptor that bind and respond to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Alpha adrenergic receptors (α-ARs) are a subtype of adrenergic receptors that are classified into two main categories: α1-ARs and α2-ARs.

The activation of α1-ARs leads to the activation of phospholipase C, which results in an increase in intracellular calcium levels and the activation of various signaling pathways that mediate diverse physiological responses such as vasoconstriction, smooth muscle contraction, and cell proliferation.

On the other hand, α2-ARs are primarily located on presynaptic nerve terminals where they function to inhibit the release of neurotransmitters, including norepinephrine. The activation of α2-ARs also leads to the inhibition of adenylyl cyclase and a decrease in intracellular cAMP levels, which can mediate various physiological responses such as sedation, analgesia, and hypotension.

Overall, α-ARs play important roles in regulating various physiological functions, including cardiovascular function, mood, and cognition, and are also involved in the pathophysiology of several diseases, such as hypertension, heart failure, and neurodegenerative disorders.

Hypoxia-Inducible Factor 1 (HIF-1) is a transcription factor that plays a crucial role in the body's response to low oxygen levels, also known as hypoxia. HIF-1 is a heterodimeric protein composed of two subunits: an alpha subunit (HIF-1α) and a beta subunit (HIF-1β).

The alpha subunit, HIF-1α, is the regulatory subunit that is subject to oxygen-dependent degradation. Under normal oxygen conditions (normoxia), HIF-1α is constantly produced in the cell but is rapidly degraded by proteasomes due to hydroxylation of specific proline residues by prolyl hydroxylase domain-containing proteins (PHDs). This hydroxylation reaction requires oxygen as a substrate, and under hypoxic conditions, the activity of PHDs is inhibited, leading to the stabilization and accumulation of HIF-1α.

Once stabilized, HIF-1α translocates to the nucleus, where it heterodimerizes with HIF-1β and binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes. This binding results in the activation of gene transcription programs that promote cellular adaptation to low oxygen levels. These adaptive responses include increased erythropoiesis, angiogenesis, glucose metabolism, and pH regulation, among others.

Therefore, HIF-1α is a critical regulator of the body's response to hypoxia, and its dysregulation has been implicated in various pathological conditions, including cancer, cardiovascular disease, and neurodegenerative disorders.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Proto-oncogene proteins, such as c-MAF, are normal cellular proteins that play crucial roles in various biological processes including cell growth, differentiation, and apoptosis (programmed cell death). When these genes undergo mutations or become overexpressed, they can transform into oncogenes, which contribute to the development of cancer.

The c-MAF protein is a transcription factor that regulates gene expression by binding to specific DNA sequences. It belongs to the basic region-leucine zipper (bZIP) family of transcription factors and plays essential roles in immune system function, cell cycle regulation, and tumorigenesis.

In cancer, c-MAF can contribute to tumor development and progression by promoting cell proliferation, survival, and angiogenesis (the formation of new blood vessels). Dysregulation of c-MAF has been implicated in various types of cancer, such as multiple myeloma, lung cancer, and breast cancer.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Native polyacrylamide gel electrophoresis (PAGE) is not a medical term per se, but rather a technique used in molecular biology and genetics. However, I can certainly provide you with a definition of this term:

Native PAGE is a laboratory method used to separate and analyze proteins based on their charge and size. This technique utilizes a polyacrylamide gel matrix, which serves as a molecular sieve, through which the protein mixtures are electrophoretically separated under native (non-denaturing) conditions. As a result, the proteins maintain their natural charges, shapes, and interactions during the separation process. This method is particularly useful for studying protein-protein interactions, enzyme activity, and protein complexes.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

The alpha7 nicotinic acetylcholine receptor (α7nAChR) is a type of cholinergic receptor found in the nervous system that is activated by the neurotransmitter acetylcholine. It is a ligand-gated ion channel that is widely distributed throughout the central and peripheral nervous systems, including in the hippocampus, cortex, thalamus, and autonomic ganglia.

The α7nAChR is composed of five subunits arranged around a central pore, and it has a high permeability to calcium ions (Ca2+). When acetylcholine binds to the receptor, it triggers a conformational change that opens the ion channel, allowing Ca2+ to flow into the cell. This influx of Ca2+ can activate various intracellular signaling pathways and have excitatory or inhibitory effects on neuronal activity, depending on the location and function of the receptor.

The α7nAChR has been implicated in a variety of physiological processes, including learning and memory, attention, sensory perception, and motor control. It has also been studied as a potential therapeutic target for various neurological and psychiatric disorders, such as Alzheimer's disease, schizophrenia, and pain.

Immunoglobulin light chains are the smaller protein subunits of an immunoglobulin, also known as an antibody. They are composed of two polypeptide chains, called kappa (κ) and lambda (λ), which are produced by B cells during the immune response. Each immunoglobulin molecule contains either two kappa or two lambda light chains, in association with two heavy chains.

Light chains play a crucial role in the antigen-binding site of an antibody, where they contribute to the specificity and affinity of the interaction between the antibody and its target antigen. In addition to their role in immune function, abnormal production or accumulation of light chains can lead to various diseases, such as multiple myeloma and amyloidosis.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Immunoglobulin heavy chains are proteins that make up the framework of antibodies, which are Y-shaped immune proteins. These heavy chains, along with light chains, form the antigen-binding sites of an antibody, which recognize and bind to specific foreign substances (antigens) in order to neutralize or remove them from the body.

The heavy chain is composed of a variable region, which contains the antigen-binding site, and constant regions that determine the class and function of the antibody. There are five classes of immunoglobulins (IgA, IgD, IgE, IgG, and IgM) that differ in their heavy chain constant regions and therefore have different functions in the immune response.

Immunoglobulin heavy chains are synthesized by B cells, a type of white blood cell involved in the adaptive immune response. The genetic rearrangement of immunoglobulin heavy chain genes during B cell development results in the production of a vast array of different antibodies with unique antigen-binding sites, allowing for the recognition and elimination of a wide variety of pathogens.

Alpha-crystallin A chain is a protein that in humans is encoded by the CRYAA gene. Crystallins are separated into two classes: ... Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins ... Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is ... the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an ...
... the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Alpha B chain crystallins (αBC) can be induced by heat shock, ... Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. These ... Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is ... Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene. It is part of the small heat shock protein ...
... alpha-crystallin a chain MeSH D12.776.306.366.100.300 - alpha-crystallin b chain MeSH D12.776.306.366.300.100 - beta-crystallin ... beta-crystallin b chain MeSH D12.776.331.199.750.500 - succinate dehydrogenase MeSH D12.776.377.715.085.050 - alpha 1- ... immunoglobulin heavy chains MeSH D12.776.377.715.548.705.500.350 - immunoglobulin alpha-chains MeSH D12.776.377.715.548.705. ... cholesterol 7 alpha-hydroxylase MeSH D12.776.422.220.453.915.212 - cholesterol side-chain cleavage enzyme MeSH D12.776.422.220. ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... "Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human beta-crystallin gene CRYBB2 ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... Beta-crystallin B2 is a protein that in humans is encoded by the CRYBB2 gene. Crystallins are separated into two classes: taxon ...
... alpha 1 CPT2: carnitine palmitoyltransferase II CRYZ: Crystallin zeta CSDE1: Cold shock domain containing E1 CYP4B1 (1p33) ... heavy chain 14 DUSP10 (1q41) DUSP27: encoding protein Dual specificity phosphatase 27 (putative) ECM1 (1q21) EDEM3: ER ... 1 alpha subcomplex, 4, 9kda, pseudogene 1 NGF: Nerve Growth Factor NOL9: Nucleolar protein 9 NRAS (1p13) NOTCH2 (1p12) OLFML3: ... encoding TNF alpha induced protein 8 like 2 TNFSF18 (1q25) TNNT2: cardiac troponin T2 TOR1AIP1: Torsin-1A-interacting protein 1 ...
... encoding alpha-2 chain of collagen VI COL18A1: encoding alpha-1 chain of collagen XVIII CRYAA: encoding alpha-crystallin A ... encoding GA-binding protein alpha chain GART: encoding enzyme trifunctional purine biosynthetic protein adenosine-3 GATD3A: ... encoding interferon alpha/beta receptor 1 IFNAR2: encoding interferon alpha/beta receptor 2 IFNGR2: encoding interferon gamma ... chain CRYZL1: encoing protein crystallin zeta-like 1 CSTB: encoding protein cystatin-B CXADR: encoding protein coxsackievirus ...
... rho crystallin, and many others. All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide ... Some proteins of this family contain a potassium channel beta chain regulatory domain; these are reported to have ... The fold comprises a parallel beta-8/alpha-8-barrel, which contains a novel NADP-binding motif. The binding site is located in ...
Bsibsi M, Holtman IR, Gerritsen WH, Eggen BJ, Boddeke E, van der Valk P, van Noort JM, Amor S (2013). "Alpha-B-Crystallin ... free light chains (FLC). Several authors have reported that they are comparable or even better than oligoclonal bands. Multiple ...
The N-terminal domain I (aa ~1-195) contains attachment sites for HS chains. Although HS chains are not required for correct ... To this end, a transgenic mouse line was created expressing porcine TGF-β1 under the lens-specific αA-crystallin promoter and ... In a mouse model of Alzheimer's plaque formation, IL-1-alpha effects an increase in perlecan expression in response to brain ... Domain V also has attachment sites for HS/CS chains. Thus, perlecan core protein and HS chains could modulate matrix assembly, ...
... alpha 1 Collagen, type XIX, alpha 1 Collagen, type XXV, alpha 1 Collagen, type XXVII, alpha 1 Crystallin, beta A1 Cyclic ... DP alpha 1 Major histocompatibility complex, class II, DQ alpha 1 Myosin light chain A1, an actin-binding protein NADH ... alpha 1 collagen, type II, alpha 1 Collagen, type III, alpha 1 Collagen, type IV, alpha 1 Collagen, type V, alpha 1 Collagen, ... type VI, alpha 1 Collagen, type VII, alpha 1 Collagen, type VIII, alpha 1 Collagen, type IX, alpha 1 Collagen, type X, alpha 1 ...
Shum WK, Maleknia SD, Downard KM (September 2005). "Onset of oxidative damage in alpha-crystallin by radical probe mass ... The rate or level of oxidation at the reactive amino acid side chains (Met, Cys, Trp, Tyr, Phe, His, Pro and Leu) provides a ... The mechanisms of side chain oxidation were explored by performing the radiolysis reactions in 18O-labeled water. A critical ... Downard KM, Kokabu Y, Ikeguchi M, Akashi S (November 2011). "Homology-modelled structure of the βB2B3-crystallin heterodimer ...
The cause is lens hardening by decreasing levels of alpha-crystallin, a process which may be sped up by higher temperatures. ... The authors propose that mtDNA mutations lead to respiratory-chain-deficient cells and thence to apoptosis and cell loss. They ... the Growth hormone/Insulin-like growth factor 1 signalling pathway the activity levels of the electron transport chain in ...
The propeptide region has an open-sandwich antiparallel-alpha/antiparallel-beta fold, with two alpha-helices and four beta- ... is a double-chain inhibitor consisting of an 11-residue and a 41-residue chain. The Carboxypeptidase inhibitor I68 family ... The yeast killer toxin structure was thought to be a precursor of the two-domain beta gamma-crystallin proteins, because of its ... It forms an alpha-helical domain that runs through the substrate-binding site, preventing access. Removal of this region by ...
Domain 2 contains one small beta sheet, nine alpha helices, and the carboxyl terminus. Three of the nine alpha helices on one ... δ-crystallins are the major structural eye lens water-soluble proteins of most birds, reptiles, and some other vertebrates. ... ASL is composed of four identical monomers; each monomer consisting of a single polypeptide chain between 49 and 52 kDa, ... Two dimers then associate by way of alpha helix, one from each monomer, to form a central 20-helix core. The association of all ...
Silva, R.A.G.D., *Nguyen, J.Y., and Decatur, S.M. (2002) "Probing the Effects of Side Chains on the Conformation and Stability ... "Formation of Amyloid Fibrils in Vitro by Human γd-crystallin and its Isolated Domains," Molecular Vision 14:81-89. Decatur, S.M ... "Two dimensional infrared measurements of the coupling of the amide modes of an alpha helix," Chemical Physics Letters 382: 586- ... "Twodimensional IR Spectroscopy and Segmental 13C Labeling reveals the Domain Structure of Human γδ-crystallin amyloid fibrils ...
These compounds are thought to act as bidentate nucleophiles that attack the adjacent carbonyls in the alpha-dicarbonyl ... and crystallin of the eyes. Covalent protein cross-links irreversibly link proteins together in the ECM of tissues. Glucosepane ... This then condenses with the arginine side chain to yield glucosepane in nucleophilic addition-elimination reactions of the ... such as collagen in the skin and crystallin in the eyes. Skin collagen, for instance, has a half-life of fifteen years. Because ...
The translation of reticulocyte 9S RNA in frog oocytes gives rise to alpha and beta globin chains. Communication to FEBS ... Berns, A. J. M.; Kraaikamp, M. Van; Bloemendal, H.; Lane, C. D. (1972). "Calf Crystallin Synthesis in Frog Cells: The ...
... cholesterol side-chain cleavage enzyme MeSH D08.244.453.915.400 - 25-hydroxyvitamin d3 1-alpha-hydroxylase MeSH D08.244.453.915 ... delta-crystallins MeSH D08.811.520.232.400 - ammonia-lyases MeSH D08.811.520.232.400.200 - aspartate ammonia-lyase MeSH D08.811 ... cholesterol side-chain cleavage enzyme MeSH D08.811.682.690.708.170.915.400 - 25-hydroxyvitamin d3 1-alpha-hydroxylase MeSH ... cholesterol 7 alpha-hydroxylase MeSH D08.811.682.690.708.783.212 - cholesterol side-chain cleavage enzyme MeSH D08.811.682.690. ...
... and aspartate side-chains, with a glutamate side-chain playing a secondary role. These side-chains, to be specific Arg359, ... and Asp477 forms hydrogen bonds with the alpha hydroxyl group on the substrate, where it works to effectively bind the ... in the mammalian cornea by the stromal keratocytes and epithelial cells and is reputed to be one of the corneal crystallins. ... To be specific, the His 263 and His30 side-chains form hydrogen bonds to the aldehyde end of the substrate, which is deepest ...
Ecroyd H, Carver JA (January 2009). "Crystallin proteins and amyloid fibrils". Cellular and Molecular Life Sciences. 66 (1): 62 ... Badar T, D'Souza A, Hari P (2018). "Recent advances in understanding and treating immunoglobulin light chain amyloidosis". ... "Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein". Proceedings of the ... In immunoglobulin light chain amyloidosis (AL amyloidosis), chemotherapy can be used to lower the number of the blood cells ...
... alpha-crystallin, with molten globule states of bovine alpha-lactalbumin". The Journal of Biological Chemistry. 272 (44): 27722 ... These bacteria produce short chain fatty acids (SCFA) which improve the gut biome. In a controlled study, the group that ate a ... March 1995). "Lactation is disrupted by alpha-lactalbumin deficiency and can be restored by human alpha-lactalbumin gene ... alpha-Lactalbumin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human LALBA genome location and ...
"Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the ... Oligomerization is a chemical process that converts individual molecules into a chain consisting of a finite number of ... leading to a chain reaction akin to a prion infection. The oligomers are toxic to nerve cells. The other protein implicated in ... "Beta-amyloid exhibits antagonistic effects on alpha 7 nicotinic acetylcholine receptors in orchestrated manner". Journal of ...
Genes associated with the development of lens include crystallin genes. Although crystallins are highly conserved proteins ... The coding regions of the CRYAA and CRYAB gene were amplified using polymerase chain reaction and subjected to restriction ... In this study, we screened for polymorphisms in crystallin alpha A (CRYAA) and alpha B (CRYAB) genes in 200 patients over 40 ... A silent mutation in human alpha-A crystallin gene in patients with age-related nuclear or cortical cataract Bharani K ...
"γ-crystallins are highly specialized proteins of the vertebrate eye lens where they survive without turnover under high ... alpha-Crystallin B Chain / chemistry Actions. * Search in PubMed * Search in MeSH ... Zebrafish alpha-crystallins: protein structure and chaperone-like activity compared to their mammalian orthologs. Dahlman JM, ... Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins. Zhao H, Chen Y, Rezabkova L, Wu Z, Wistow G, ...
alpha-crystallin B chain. *crystallin, alpha B. *heat shock protein beta-5 ... Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins ... Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is ... the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an ...
7. Alpha-crystallin B chains enhance cell migration in basal-like 2 triple-negative breast cancer cells.. Yang L; Higashisaka K ... 3. Fluorouracil exacerbates alpha-crystallin B chain-mediated cell migration in triple-negative breast cancer cell lines.. Yang ... Increased alpha-B-crystallin expression in mammary metaplastic carcinomas.. Chan SK; Lui PC; Tan PH; Yamaguchi R; Moriya T; Yu ... Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 ...
alpha-Crystallin B Chain Entry term(s). B Chain, alpha-Crystallin B Subunit alpha-Crystallin Crystallins, alpha B Chain ... alpha B Crystallin alpha B-Crystallin alpha Crystallin B Chain alpha Crystallin, B Subunit alpha-Crystallin, B Subunit ... alpha B Crystallin. alpha B-Crystallin. alpha Crystallin B Chain. alpha Crystallin, B Subunit. alpha-Crystallin, B Subunit. ... Chaîne B de la cristalline alpha Entry term(s):. B Chain, alpha-Crystallin. B Subunit alpha-Crystallin. Crystallins, alpha B ...
alpha-Crystallins [D12.776.580.157] * alpha-Crystallin A Chain [D12.776.580.157.149] * alpha-Crystallin B Chain [D12.776. ... Crystallins, alpha B Chain Rosenthal Fiber Component alpha B-Crystallin alpha-Crystallin, B Subunit Registry Number. 0. ... Crystallins [D12.776.306.366] * alpha-Crystallins [D12.776.306.366.100] * alpha-Crystallin A Chain [D12.776.306.366.100.149] ... 2003; for ALPHA B-CRYSTALLIN see CRYSTALLINS 1998-2002. History Note. 2003; for ALPHA B-CRYSTALLIN use CRYSTALLINS 1998-2002. ...
alpha-Crystallins [D12.776.580.157] * alpha-Crystallin A Chain [D12.776.580.157.149] * alpha-Crystallin B Chain [D12.776. ... Crystallins, alpha B Chain Rosenthal Fiber Component alpha B-Crystallin alpha-Crystallin, B Subunit Registry Number. 0. ... Crystallins [D12.776.306.366] * alpha-Crystallins [D12.776.306.366.100] * alpha-Crystallin A Chain [D12.776.306.366.100.149] ... 2003; for ALPHA B-CRYSTALLIN see CRYSTALLINS 1998-2002. History Note. 2003; for ALPHA B-CRYSTALLIN use CRYSTALLINS 1998-2002. ...
蛋白别名: Alpha-crystallin C chain; crystallin, alpha C; DHMN 2; E2-induced gene 1 protein; heat shock 22kDa protein 8; heat shock ... protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin ... Heavy Chain) Superclonal™ Recombinant Secondary Antibody, HRP (Product # A27036, 1:8000 dilution) using the iBright FL 1000 ( ... Heavy Chain) Superclonal™ Recombinant Secondary Antibody, HRP (Product # A27036, 1:10000 dilution). Densitometric analysis of ...
Alpha-crystallin A2 chain. Download download. Jump to section:. close. Descriptive Data ...
alpha-crystallin B chain. 6.4±0.5. 6. -. 2. 5.0±0.6. 5. 2.97. 3. ... spectrin alpha chain, non-erythrocytic 1. 4.3±0.3. 37. 16.92. 3. 3.3±0.3. 39. 14.23. 3. ... tubulin alpha-1C chain. 5.0±0.3. 6. 4.84. 3. 3.8±0.3. 4. 3.08. 3. ... tubulin alpha-4A chain. 5.7±1.0. 3. 1.51. 3. 4.6±0.3. 5. 3.85. 3. ...
C115115 P02511 Alpha-Crystallin B Chain C104205 P06733 Alpha-Enolase C16278 P02771 Alpha-Fetoprotein C101802 Q12800 Alpha- ... C30013 P02452 Collagen Alpha-1(I) Chain C75319 Q96IT5 Collagen Alpha-1(II) Chain C143055 P02461 Collagen Alpha-1(III) Chain ... Chain C17792 P39060 Collagen Alpha-1(XVIII) Chain C30015 P08123 Collagen Alpha-2(I) Chain C152984 P08572 Collagen Alpha-2(IV) ... Chain C177530 P05997 Collagen Alpha-2(V) Chain C26002 Q01955 Collagen Alpha-3(IV) Chain C150667 P12111 Collagen Alpha-3(VI) ...
... alpha crystallin. Thus, by using such messenger RNAs as templates, alpha crystallin polypeptide chains have been synthesized. ... Stauffer, J., Rothschild, C. , Wandel , T. , and Spector, A.: Transformation of alpha crystallin polypeptide chains with aging ... Studies with bovine alpha-crystallins have clearly demon- strated in the past that this large class of proteins is not ... Furthermore, the mRNAs have also served as templates for the sjmthesis of the alpha crystallin DNA utilizing a viral reverse ...
Here, we perform mass spectrometry experiments to study αB-crystallin and extract detailed information as to its oligomeric ... This provides a new means for understanding the polydispersity of αB-crystallin and a framework for interrogating other ... For this reason, quantitative studies of the molecular chaperone αB-crystallin, which populates a range of interconverting ... alpha-Crystallin A Chain, alpha-Crystallin B Chain ... αB-crystallin polydispersity is a consequence of unbiased ...
TAGS: crystallins, tissue membrane, phosphorylation, interleukins, alpha-crystallin b chain Invest. Ophthalmol. Vis. Sci.. 2023 ... Phosphorylation of αB-Crystallin Involves Interleukin-1β-Mediated Intracellular Retention in Retinal Müller Cells: A New ...
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as ... A chain-terminating mutation was found to cause type 2 cerulean cataracts. [provided by RefSeq, Jul 2008]. ... Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four ... crystallin, beta B2. Description. Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The ...
T variant mapped to the C-terminal extension domain of the Alpha-crystallin B chain, disrupting its function as a molecular ... We propose that our report potentially expands the complex phenotypic spectrum of alpha B-crystallinopathies with possible ... We specifically found an increase in proteins forming the tricarboxylic acid cycle and electron transport chain (ETC) complex ...
COL2A1 Monoclonal Antibody , G-AB-05735 , Gentaur AntibodiesOverview: This gene encodes the alpha-1 chain of type II collagen, ... Crystallin-alpha C Monoclonal Antibody , G-AB-05655 MSRP: Was: Now: $163.00 - $465.00 ... Beta tubulins are one of two core protein families (alpha and beta tubulins) that heterodimerize and assemble to... ... AFP Monoclonal Antibody , G-AB-07643 , Gentaur AntibodiesOverview: This gene encodes alpha-fetoprotein, a major plasma protein ...
... alpha(c) (2)beta(2), in which the alpha-amino groups of the alpha-chains have reacted with cyanate, and (iii) alpha(2)beta(c) ( ... PMID- 5166593 TI - Amino acid sequences around the cysteine residue of calf lens -crystallin. AB - 1. Calf lens alpha- ... 2. The values of n (the Hill constant) for alpha(c) (2)beta(c) (2), alpha(2)beta(c) (2) and alpha(c) (2)beta(2) were ( ... in which both the alpha-amino groups of the alpha- and beta-chains have reacted with cyanate, (ii) ...
4AWL_Chain_A. Robert Britton. 3DPX-017907 Solution Structure of the alpha-crystallin do.... jiwoo0925. ...
... alpha-Crystallin A Chain alpha-Crystallin B Chain alpha-Crystallins alpha-Cyclodextrins alpha-Defensins alpha-Endorphin alpha- ... alpha-Chains HLA-DP Antigens HLA-DP beta-Chains HLA-DQ alpha-Chains HLA-DQ Antigens HLA-DQ beta-Chains HLA-DR alpha-Chains HLA- ... alpha Catenin alpha Karyopherins Alpha Particles Alpha Rhythm alpha-2-Antiplasmin alpha-2-HS-Glycoprotein Alpha-Amanitin alpha- ... Fetoproteins alpha-Galactosidase alpha-Globins Alpha-Globulins alpha-Glucosidases alpha-L-Fucosidase alpha-Linolenic Acid alpha ...
Mark H Katz, MD is a member of the following medical societies: Alpha Omega Alpha, American Urological Association, ... Reverse transcription quantitative polymerase chain reaction (RT-PCR) for messenger RNA (CxBladder, Xpert) ... CRYAB (alpha B-crystallin) * CGNL1 (cingulin-like 1) * GPX3 (glutathione peroxidase 3) ... use reverse transcription polymerase chain reaction (RT-PCR) to detect messenger RNA (mRNA) in urine samples. ...
crystallin alpha B [Source:HGNC Symbol;.... 32243_g_at. 1410. CRYAB. crystallin alpha B [Source:HGNC Symbol;.... ... acyl-CoA dehydrogenase medium chain [So.... 37897_s_at. 7033. TFF3. trefoil factor 3 [Source:HGNC Symbol;Ac.... ...
Crystallin, lambda 1. −2.1 ± 0.39. 1.2 ± 0.15. Igfals. Insulin-like growth factor binding protein, acid labile subunit. −2.1 ± ... Quantitative reverse-transcription polymerase chain reaction (PCR). Total RNA was extracted from mouse liver tissues using TRI ... to peroxisome proliferator WY-14,643 in mouse liver are dependent upon peroxisome proliferator activated receptor alpha. Mutat ...
Transcriptional Activation of the Nonmuscle Myosin II Heavy Chain-A Gene by E-box Binding Proteins TFEC and TFE3 ... The transcriptional regulation of two putative corneal crystallins in the rabbit: ALDH1 and TKT ... Conditional expression of the human acid alpha-glucosidase (GAA) gene in GAA knockout mice ...
long-chain-enoyl-CoA hydratase activity. 2 Select filter option. metal ion binding. 2 Select filter option. RNA binding. 2 ... Lambda-crystallin homolog. 1 Select filter option. Methylglutaconyl-CoA hydratase, mitochondrial. 1 Select filter option. ... HADHATrifunctional enzyme subunit alpha, mitochondrial. help help. Gene Details. Gene Symbol: HADHA ... Acyl chain remodeling of CL. 1 Select filter option. Beta oxidation of butanoyl-CoA to acetyl-CoA. 1 Select filter option. Beta ...
... alpha-crystallin, phakinin, and gamma-crystallin proteins. We observed no EBOV-specific peptide sequences. ... reverse transcription-polymerase chain reaction and cataract surgery outcomes of Ebola survivors in Sierra Leone. EBioMedicine ... with the greatest numbers of peptide spectrum matches observed for beta-crystallin, ...
  • miR-491 exerts its role by directly targeting alphaB-crystallin (CRYAB) in OS. (cusabio.com)
  • Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. (expasy.org)
  • Alpha-crystallin A chain is a protein that in humans is encoded by the CRYAA gene. (wikipedia.org)
  • Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. (wikipedia.org)
  • Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. (wikipedia.org)
  • The protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. (thermofisher.cn)
  • This light-protein chain, which can be shed into serum, is called beta 2 microglobulin. (medscape.com)
  • Beta 2 microglobulin is an 11.8-kD protein (see first image below), which forms one of the chains of the major histocompatibility complex (MHC) class I molecule normally present on the surface of every nucleated cell in the human body. (medscape.com)
  • Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. (wikipedia.org)
  • alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. (wikipedia.org)
  • α-crystallin is an abundant constituent of the eye lens of most vertebrate species. (expasy.org)
  • SLBB domain, 4Fe-4S dicluster domain, RnfC Barrel sandwich hybrid domain, Respiratory-chain NADH dehydrogenase 51 Kd subunit [Interproscan]. (ntu.edu.sg)
  • Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. (wikipedia.org)
  • beta and gamma crystallins are also considered as a superfamily. (wikipedia.org)
  • These antigens have a heavy chain and an associated light chain. (medscape.com)
  • Alpha and beta families are further divided into acidic and basic groups. (wikipedia.org)
  • These dyes differ in the number of polyethylene glycol (PEG) chains attached to the core structure which is either a perylene derivate or a terrylene derivate. (cipsm.de)
  • Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. (wikipedia.org)
  • The coding regions of the CRYAA and CRYAB gene were amplified using polymerase chain reaction and subjected to restriction digestion. (nih.gov)
  • We propose that our report potentially expands the complex phenotypic spectrum of alpha B-crystallinopathies with possible effect of a CRYAB variant on the central nervous system. (bvsalud.org)
  • Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. (nih.gov)
  • Alpha and beta families are further divided into acidic and basic groups. (maayanlab.cloud)
  • In addition, fish γM-crystallins do not conserve the paired tryptophan residues found in each domain in mammalian γ-crystallins and in the related β-crystallins. (nih.gov)
  • From NCBI Gene: Mammalian lens crystallins are divided into alpha, beta, and gamma families. (nih.gov)
  • the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. (nih.gov)
  • One of the alpha crystallin subunits. (bvsalud.org)
  • Here, we perform mass spectrometry experiments to study αB-crystallin and extract detailed information as to its oligomeric distribution and exchange of subunits under a range of conditions. (ox.ac.uk)
  • This provides a new means for understanding the polydispersity of αB-crystallin and a framework for interrogating other heterogeneous protein assemblies. (ox.ac.uk)
  • Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). (maayanlab.cloud)
  • Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. (maayanlab.cloud)
  • Although crystallins are highly conserved proteins among vertebrates, a significant number of polymorphisms exist in human population. (nih.gov)
  • 10. Regulation of alphaB-crystallin gene expression by the transcription factor Ets1 in breast cancer. (nih.gov)
  • For this reason, quantitative studies of the molecular chaperone αB-crystallin, which populates a range of interconverting oligomeric states, have been difficult, and the physicochemical basis for its polydispersity has remained unknown. (ox.ac.uk)
  • Whole exome sequencing identified a heterozygous c.458C>T variant mapped to the C-terminal extension domain of the Alpha-crystallin B chain, disrupting its function as a molecular chaperone and its ability to suppress protein aggregation. (bvsalud.org)
  • beta and gamma crystallins are also considered as a superfamily. (maayanlab.cloud)
  • Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. (maayanlab.cloud)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human RAR Related Orphan Receptor Alpha (RORa) in Tissue homogenates, cell lysates and other biological fluids. (2sars.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human RAR Related Orphan Receptor Alpha (RORa) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (2sars.com)
  • Description: A sandwich ELISA kit for detection of RAR Related Orphan Receptor Alpha from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (2sars.com)
  • 18. Discovery of structure-based small molecular inhibitor of αB-crystallin against basal-like/triple-negative breast cancer development in vitro and in vivo. (nih.gov)
  • To gain insight into important, evolutionarily conserved properties and functionality of γ-crystallins, zebrafish (Danio rerio) γM2b and γM7 were compared with mouse γS and human γD. (nih.gov)
  • 1. αB-crystallin expression is correlated with phospho-ERK1/2 expression in human breast cancer. (nih.gov)
  • 12. alphaB-crystallin extracellularly suppresses ADP-induced granule secretion from human platelets. (nih.gov)
  • Solution Structure of the alpha-crystallin do. (nih.gov)
  • A chain-terminating mutation was found to cause type 2 cerulean cataracts. (maayanlab.cloud)
  • 13. Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells. (nih.gov)
  • CDC researchers have developed a reverse transcription/semi-nested polymerase chain reaction (RT-snPCR) assay for diagnosis of enterovirus infections within clinical specimens. (nih.gov)
  • 11. alphaB-crystallin is a marker of aggressive breast cancer behavior but does not independently predict for patient outcome: a combined analysis of two randomized studies. (nih.gov)
  • 17. Effect of hypoxia on the expression of αB-crystallin in head and neck squamous cell carcinoma. (nih.gov)