Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Molecular Sequence Data
Amino Acid Sequence
Two-Hybrid System Techniques
Amino Acid Motifs
src Homology Domains
Sequence Homology, Amino Acid
Protein Interaction Maps
Adaptor Proteins, Signal Transducing
Recombinant Fusion Proteins
Protein Structure, Secondary
Saccharomyces cerevisiae Proteins
Amino Acid Substitution
Promoter Regions, Genetic
Sequence Analysis, Protein
Gene Expression Regulation
Surface Plasmon Resonance
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Quaternary
Intracellular Signaling Peptides and Proteins
Green Fluorescent Proteins
Cell Cycle Proteins
Nuclear Localization Signals
LIM Domain Proteins
Fluorescence Resonance Energy Transfer
Electrophoresis, Polyacrylamide Gel
Nucleic Acid Conformation
Active Transport, Cell Nucleus
Nuclear Receptor Co-Repressor 1
Receptors, Cytoplasmic and Nuclear
Caenorhabditis elegans Proteins
Gene Expression Regulation, Developmental
Repetitive Sequences, Amino Acid
Nuclear Receptor Coactivator 2
Tumor Cells, Cultured
Gene Regulatory Networks
Structural Homology, Protein
Nuclear Receptor Coactivator 1
Polymerase Chain Reaction
Adaptor Proteins, Vesicular Transport
Sequence Analysis, DNA
Protein Processing, Post-Translational
Magnetic Resonance Spectroscopy
N-terminal segments are the functional domains of CLN3-encoded battenin for protein interactions. (1/3048)OBJECTIVE: Batten disease (BD), the juvenile form of neuronal ceroid lipofuscinosis (NCLs), is pathological characterized by finding lysosomal storage of autofluorescent lipofuscins with unique ultrastructural profiles. The gene underlying BD is designated CLN3 and encodes a protein, Battenin, of unknown function that localizes in lysosomes and/or mitochondria. Previously, we hypothesized that Battenin associates with other membrane protein(s) to form a membrane complex. Dysfunction of this complex could result in the pathological changes of BD, and possibly in other NCLs. Two such membranous proteins, the slow and fast Battenin-interactive proteins (BIPs and BIPf) of unknown functions, have been identified. In this study, we have characterized the functional domains of Battenin that interact with both BIP proteins. METHODS: Protein-protein interactions with a yeast two-hybrid system were employed. A "deletion assay" was employed to localize the interactive segment(s). Different lengths of cDNA sequences lacking exon 1-5 were used to express CLN3-encoded proteins lacking N-terminal segments in the yeast two-hybrid system. N-terminal exons of CLN3 were deleted with PCR-cloning strategies. RESULTS: We eliminated the possibility of interacting domains from the exon 7-encoded region because both Battenin and mBattenin interact with the BIP proteins. We have shown that peptide sequences encoded by exons 2 and 4 of CLN3 gene include the functional domains by which Battenin interacts with the BIP proteins. CONCLUSION: Our studies provide evidence that the N-terminus of Battenin is the functional domain for these protein interactions. (+info)
Separation of anti-proliferation and anti-apoptotic functions of retinoblastoma protein through targeted mutations of its A/B domain. (2/3048)BACKGROUND: The human retinoblastoma susceptibility gene encodes a nuclear phosphoprotein RB, which is a negative regulator of cell proliferation. The growth suppression function of RB requires an evolutionarily conserved A/B domain that contains two distinct peptide-binding pockets. At the A/B interface is a binding site for the C-terminal trans-activation domain of E2F. Within the B-domain is a binding site for proteins containing the LxCxE peptide motif. METHODOLOGY/PRINCIPLE FINDINGS: Based on the crystal structure of the A/B domain, we have constructed an RB-K530A/N757F (KN) mutant to disrupt the E2F- and LxCxE-binding pockets. The RB-K530A (K) mutant is sufficient to inactivate the E2F-binding pocket, whereas the RB-N757F (N) mutant is sufficient to inactivate the LxCxE-binding pocket. Each single mutant inhibits cell proliferation, but the RB-KN double mutant is defective in growth suppression. Nevertheless, the RB-KN mutant is capable of reducing etoposide-induced apoptosis. CONCLUSION/SIGNIFICANCE: Previous studies have established that RB-dependent G1-arrest can confer resistance to DNA damage-induced apoptosis. Results from this study demonstrate that RB can also inhibit apoptosis independent of growth suppression. (+info)
Insights into the molecular evolution of the PDZ/LIM family and identification of a novel conserved protein motif. (3/3048)The PDZ and LIM domain-containing protein family is encoded by a diverse group of genes whose phylogeny has currently not been analyzed. In mammals, ten genes are found that encode both a PDZ- and one or several LIM-domains. These genes are: ALP, RIL, Elfin (CLP36), Mystique, Enigma (LMP-1), Enigma homologue (ENH), ZASP (Cypher, Oracle), LMO7 and the two LIM domain kinases (LIMK1 and LIMK2). As conventional alignment and phylogenetic procedures of full-length sequences fell short of elucidating the evolutionary history of these genes, we started to analyze the PDZ and LIM domain sequences themselves. Using information from most sequenced eukaryotic lineages, our phylogenetic analysis is based on full-length cDNA-, EST-derived- and genomic- PDZ and LIM domain sequences of over 25 species, ranging from yeast to humans. Plant and protozoan homologs were not found. Our phylogenetic analysis identifies a number of domain duplication and rearrangement events, and shows a single convergent event during evolution of the PDZ/LIM family. Further, we describe the separation of the ALP and Enigma subfamilies in lower vertebrates and identify a novel consensus motif, which we call 'ALP-like motif' (AM). This motif is highly-conserved between ALP subfamily proteins of diverse organisms. We used here a combinatorial approach to define the relation of the PDZ and LIM domain encoding genes and to reconstruct their phylogeny. This analysis allowed us to classify the PDZ/LIM family and to suggest a meaningful model for the molecular evolution of the diverse gene architectures found in this multi-domain family. (+info)
Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. (4/3048)Regulation of biological processes often involves phosphorylation of intrinsically disordered protein regions, thereby modulating protein interactions. Initiation of DNA replication in yeast requires elimination of the cyclin-dependent kinase inhibitor Sic1 via the SCF(Cdc4) ubiquitin ligase. Intriguingly, the substrate adapter subunit Cdc4 binds to Sic1 only after phosphorylation of a minimum of any six of the nine cyclin-dependent kinase sites on Sic1. To investigate the physical basis of this ultrasensitive interaction, we consider a mean-field statistical mechanical model for the electrostatic interactions between a single receptor site and a conformationally disordered polyvalent ligand. The formulation treats phosphorylation sites as negative contributions to the total charge of the ligand and addresses its interplay with the strength of the favorable ligand-receptor contact. Our model predicts a threshold number of phosphorylation sites for receptor-ligand binding, suggesting that ultrasensitivity in the Sic1-Cdc4 system may be driven at least in part by cumulative electrostatic interactions. This hypothesis is supported by experimental affinities of Cdc4 for Sic1 fragments with different total charges. Thus, polyelectrostatic interactions may provide a simple yet powerful framework for understanding the modulation of protein interactions by multiple phosphorylation sites in disordered protein regions. (+info)
Evolution of function in the "two dinucleotide binding domains" flavoproteins. (5/3048)Structural and biochemical constraints force some segments of proteins to evolve more slowly than others, often allowing identification of conserved structural or sequence motifs that can be associated with substrate binding properties, chemical mechanisms, and molecular functions. We have assessed the functional and structural constraints imposed by cofactors on the evolution of new functions in a superfamily of flavoproteins characterized by two-dinucleotide binding domains, the "two dinucleotide binding domains" flavoproteins (tDBDF) superfamily. Although these enzymes catalyze many different types of oxidation/reduction reactions, each is initiated by a stereospecific hydride transfer reaction between two cofactors, a pyridine nucleotide and flavin adenine dinucleotide (FAD). Sequence and structural analysis of more than 1,600 members of the superfamily reveals new members and identifies details of the evolutionary connections among them. Our analysis shows that in all of the highly divergent families within the superfamily, these cofactors adopt a conserved configuration optimal for stereospecific hydride transfer that is stabilized by specific interactions with amino acids from several motifs distributed among both dinucleotide binding domains. The conservation of cofactor configuration in the active site restricts the pyridine nucleotide to interact with FAD from the re-side, limiting the flow of electrons from the re-side to the si-side. This directionality of electron flow constrains interactions with the different partner proteins of different families to occur on the same face of the cofactor binding domains. As a result, superimposing the structures of tDBDFs aligns not only these interacting proteins, but also their constituent electron acceptors, including heme and iron-sulfur clusters. Thus, not only are specific aspects of the cofactor-directed chemical mechanism conserved across the superfamily, the constraints they impose are manifested in the mode of protein-protein interactions. Overlaid on this foundation of conserved interactions, nature has conscripted different protein partners to serve as electron acceptors, thereby generating diversification of function across the superfamily. (+info)
Association of nucleophosmin negatively regulates CXCR4-mediated G protein activation and chemotaxis. (6/3048)CXCR4, the primary receptor for CXCL12, plays a critical role in the development of hematopoietic, vascular, central nervous, and immune systems by mediating directional migration of precursor cells. This mechanism promotes homing of tumor cells to metastatic sites that secrete CXCL12, and CXCR4 expression is a negative prognostic factor in acute myelogenous leukemia (AML). To elucidate mechanisms that regulate CXCR4 signaling, we used a proteomic approach to identify proteins physically associated with CXCR4. Analysis of CXCR4 immune complexes identified nucleophosmin (NPM), which was confirmed by reciprocal coimmunoprecipitation for NPM. Constitutively active CXCR4 variants bound higher levels of NPM than the wild-type receptor, which was reversed by T140, an inverse agonist. NPM binding to CXCR4 localized interactions to the C terminus and cytoplasmic loop (CL)-3, but not CL-1 or CL-2. Alanine scanning mutagenesis demonstrated that positively charged amino acids in CL-3 were critical for NPM binding. Recombinant NPM decreased GTP binding in membrane fractions after activation of CXCR4 by CXCL12. Suppression of NPM expression enhanced chemotactic responses to CXCL12, and, conversely, overexpression of a cytosolic NPM mutant reduced chemotaxis induced by CXCL12. This study provides evidence for a novel role for NPM as a negative regulator of CXCR4 signaling induced by CXCL12 that may be relevant to the biology of AML. (+info)
WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY motif of Spt23p and Mga2p. (7/3048)Rsp5p of Saccharomyces cerevisiae is a member of the C2-WW-HECT family of ubiquitin ligases and it interacts with targets via its WW domains. Spt23p and Mga2p are Rsp5p substrates and Rsp5p activates the OLE1 inducing functions of these membrane-localized transcription factors by ubiquitination. Although it is known that Rsp5p binds Mga2p and Spt23p via an imperfect WW domain-binding site (LPKY) that is located within the carboxy-terminal domain of the proteins, it remains unclear which WW domains mediate binding. We show that Rsp5p mutants harboring mutations in single WW domains are Spt23p/Mga2p binding and ubiquitination proficient. This is also the case for WW domains 1/2 and WW domains 1/3 mutants. However, disrupting WW domains 2 and 3 abrogates a physical and functional interaction with substrates in vitro and in cells. We also show that abrogation of WW domains 2 and 3 eliminates the activity of an Rsp5p dominant-negative mutant and an rsp5 WW domain 2/3 mutant is unable to rescue the proliferative defects of rsp5 Delta cells. Interestingly, while rsp5 Delta cells are able to grow on oleic acid containing YPD media, they as well as those transformed with the WW domain 2/3 mutant are unable to proliferate on oleic acid containing synthetic drop-out media. We conclude from these studies that WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY site on Spt23p and Mga2p. Also, we propose that WW domains 2 and 3 perform yet to be defined essential function(s) outside of the OLE1 pathway when cells are grown in nutrient restrictive media. (+info)
Critical role of helix 4 of HIV-1 capsid C-terminal domain in interactions with human lysyl-tRNA synthetase. (8/3048)Human tRNALys3 is used as the primer for human immunodeficiency virus type 1 (HIV-1) reverse transcription. HIV-1 Gag and GagPol, as well as host cell factor lysyl-tRNA synthetase (LysRS), are required for specific packaging of tRNALys into virions. Gag alone is sufficient for packaging of LysRS, and these two proteins have been shown to interact in vitro with an equilibrium binding constant of approximately 310 nM. The capsid (CA) domain of Gag binds to LysRS with a similar affinity as full-length Gag. In this work, we report further characterization of the interaction between HIV-1 CA and human LysRS using truncation constructs and point mutations in the putative interaction helices. Fluorescence anisotropy binding measurements reveal that a LysRS variant lacking the N-terminal 219 residues still displays high affinity binding to CA. The CA C-terminal domain (CTD) is also sufficient for binding to LysRS. Nuclear magnetic resonance spectroscopy studies using 15N-labeled CA-CTD reveal chemical shift perturbations of residues in and proximal to helix 4 of CA-CTD upon LysRS binding. A synthetic peptide that includes helix 4 binds to LysRS with high affinity, whereas peptides derived from the other three helical domains of CA-CTD do not. Alanine-scanning mutagenesis studies targeting residues in the helix 4 region support a direct interaction between this domain of CA-CTD and LysRS. The high resolution mapping studies reported here will facilitate future work aimed at disrupting the Gag-LysRS interaction, which represents a novel anti-viral strategy. (+info)
There are many different types of diseases, ranging from acute and short-term conditions such as the common cold or flu, to chronic and long-term conditions such as diabetes, heart disease, or cancer. Some diseases are infectious, meaning they can be transmitted from one person to another through contact with a contaminated surface or exchange of bodily fluids. Other diseases are non-infectious, meaning they are not transmitted from person to person and are typically caused by genetic mutations or environmental factors.
The diagnosis and treatment of disease is the focus of the medical field, and doctors and other healthcare professionals use a variety of tools and techniques to identify and manage diseases. These may include physical exams, laboratory tests, imaging studies, and medications. In some cases, surgery or other procedures may be necessary to treat a disease.
Some common examples of diseases include:
1. Heart disease: A condition that affects the heart and blood vessels, often caused by high blood pressure, high cholesterol, or smoking.
2. Diabetes: A condition in which the body is unable to properly regulate blood sugar levels, often caused by genetics or obesity.
3. Cancer: A condition in which abnormal cells grow and multiply, often causing damage to surrounding tissues.
4. Inflammatory diseases: Conditions such as arthritis, where the body's immune system causes inflammation and pain in the joints.
5. Neurological diseases: Conditions that affect the brain and nervous system, such as Alzheimer's disease, Parkinson's disease, or multiple sclerosis.
6. Infectious diseases: Conditions caused by the presence of pathogens such as bacteria, viruses, or fungi, including the common cold, flu, and tuberculosis.
7. Genetic diseases: Conditions that are caused by changes in DNA, such as sickle cell anemia or cystic fibrosis.
8. Autoimmune diseases: Conditions where the body's immune system attacks healthy cells and tissues, such as rheumatoid arthritis or lupus.
9. Pulmonary diseases: Conditions that affect the lungs, such as asthma, chronic obstructive pulmonary disease (COPD), or lung cancer.
10. Gastrointestinal diseases: Conditions that affect the digestive system, such as inflammatory bowel disease (IBD) or irritable bowel syndrome (IBS).
These are just a few examples of the many different types of diseases that exist. Diseases can be caused by a wide range of factors, including genetics, lifestyle choices, and environmental factors. Understanding the causes and symptoms of different diseases is important for developing effective treatments and improving patient outcomes.
The signs and symptoms of Liddle syndrome usually become apparent during infancy or early childhood and may include:
* Seizures: Seizures are the most common symptom of Liddle syndrome and can range from mild to severe. They can occur at any time, but are often triggered by fever, stress, or other infections.
* Poor muscle tone: Children with Liddle syndrome may have low muscle tone, which can make it difficult for them to sit up, walk, or perform other physical activities.
* Learning difficulties: Children with Liddle syndrome may experience learning difficulties, such as difficulty with speech, language, and cognitive skills.
* Developmental delays: Children with Liddle syndrome may experience developmental delays, such as delayed sitting, standing, or walking.
* Vision problems: Some children with Liddle syndrome may experience vision problems, such as blurred vision or difficulty seeing objects in the distance.
Liddle syndrome is usually diagnosed through a combination of clinical evaluation and genetic testing. Genetic testing can help identify mutations in the SCN1A gene that are associated with the condition. Imaging studies, such as electroencephalograms (EEGs) or magnetic resonance imaging (MRI), may also be used to rule out other conditions and confirm the diagnosis.
There is no cure for Liddle syndrome, but various treatments can help manage the symptoms. Anticonvulsant medications, such as sodium channel blockers, can help reduce the frequency and severity of seizures. Physical therapy and occupational therapy can help improve muscle tone and motor skills. Speech and language therapy may be helpful for children with learning difficulties or speech problems. In some cases, surgery may be necessary to treat related conditions, such as scoliosis or other spinal deformities.
The prognosis for children with Liddle syndrome varies depending on the severity of the condition and the presence of other health issues. With proper management, many children with Liddle syndrome can lead active, productive lives. However, some individuals may experience ongoing seizures or other health problems that can impact their quality of life. Regular follow-up appointments with a healthcare provider are important to monitor the condition and adjust treatment as needed.
In conclusion, Liddle syndrome is a rare genetic disorder that affects the nervous system and can cause a range of symptoms, including seizures, developmental delays, and vision problems. While there is no cure for the condition, various treatments can help manage the symptoms and improve the prognosis. Early diagnosis and ongoing medical care are essential to ensure the best possible outcome for individuals with Liddle syndrome.
Rubulavirus infections are a type of viral infection caused by the rubulavirus, which is a member of the Paramyxoviridae family. The virus primarily affects the respiratory and gastrointestinal tracts and can cause a range of symptoms, including fever, cough, sore throat, runny nose, and diarrhea.
Rubulavirus infections are most commonly seen in young children and can be severe in some cases, particularly in those with underlying medical conditions such as asthma or heart disease. In rare cases, the virus can also cause more serious complications such as pneumonia or encephalitis.
There is no specific treatment for rubulavirus infections, and treatment is primarily focused on managing symptoms and supporting the body's immune system. Over-the-counter medications such as acetaminophen or ibuprofen may be used to help manage fever and pain, while antiviral medications may be prescribed in severe cases.
Prevention is key to managing rubulavirus infections, and this includes practicing good hygiene, avoiding close contact with people who are sick, and getting vaccinated against the virus. Vaccination is particularly important for children and individuals who work with young children, as they are at higher risk of contracting the virus.
In conclusion, rubulavirus infections can cause a range of symptoms and can be severe in some cases, particularly in young children and those with underlying medical conditions. Prevention and good hygiene practices are key to managing these infections, and treatment is focused on supporting the body's immune system and managing symptoms.
Neoplasm refers to an abnormal growth of cells that can be benign (non-cancerous) or malignant (cancerous). Neoplasms can occur in any part of the body and can affect various organs and tissues. The term "neoplasm" is often used interchangeably with "tumor," but while all tumors are neoplasms, not all neoplasms are tumors.
Types of Neoplasms
There are many different types of neoplasms, including:
1. Carcinomas: These are malignant tumors that arise in the epithelial cells lining organs and glands. Examples include breast cancer, lung cancer, and colon cancer.
2. Sarcomas: These are malignant tumors that arise in connective tissue, such as bone, cartilage, and fat. Examples include osteosarcoma (bone cancer) and soft tissue sarcoma.
3. Lymphomas: These are cancers of the immune system, specifically affecting the lymph nodes and other lymphoid tissues. Examples include Hodgkin lymphoma and non-Hodgkin lymphoma.
4. Leukemias: These are cancers of the blood and bone marrow that affect the white blood cells. Examples include acute myeloid leukemia (AML) and chronic lymphocytic leukemia (CLL).
5. Melanomas: These are malignant tumors that arise in the pigment-producing cells called melanocytes. Examples include skin melanoma and eye melanoma.
Causes and Risk Factors of Neoplasms
The exact causes of neoplasms are not fully understood, but there are several known risk factors that can increase the likelihood of developing a neoplasm. These include:
1. Genetic predisposition: Some people may be born with genetic mutations that increase their risk of developing certain types of neoplasms.
2. Environmental factors: Exposure to certain environmental toxins, such as radiation and certain chemicals, can increase the risk of developing a neoplasm.
3. Infection: Some neoplasms are caused by viruses or bacteria. For example, human papillomavirus (HPV) is a common cause of cervical cancer.
4. Lifestyle factors: Factors such as smoking, excessive alcohol consumption, and a poor diet can increase the risk of developing certain types of neoplasms.
5. Family history: A person's risk of developing a neoplasm may be higher if they have a family history of the condition.
Signs and Symptoms of Neoplasms
The signs and symptoms of neoplasms can vary depending on the type of cancer and where it is located in the body. Some common signs and symptoms include:
1. Unusual lumps or swelling
4. Weight loss
5. Change in bowel or bladder habits
6. Unexplained bleeding
7. Coughing up blood
8. Hoarseness or a persistent cough
9. Changes in appetite or digestion
10. Skin changes, such as a new mole or a change in the size or color of an existing mole.
Diagnosis and Treatment of Neoplasms
The diagnosis of a neoplasm usually involves a combination of physical examination, imaging tests (such as X-rays, CT scans, or MRI scans), and biopsy. A biopsy involves removing a small sample of tissue from the suspected tumor and examining it under a microscope for cancer cells.
The treatment of neoplasms depends on the type, size, location, and stage of the cancer, as well as the patient's overall health. Some common treatments include:
1. Surgery: Removing the tumor and surrounding tissue can be an effective way to treat many types of cancer.
2. Chemotherapy: Using drugs to kill cancer cells can be effective for some types of cancer, especially if the cancer has spread to other parts of the body.
3. Radiation therapy: Using high-energy radiation to kill cancer cells can be effective for some types of cancer, especially if the cancer is located in a specific area of the body.
4. Immunotherapy: Boosting the body's immune system to fight cancer can be an effective treatment for some types of cancer.
5. Targeted therapy: Using drugs or other substances to target specific molecules on cancer cells can be an effective treatment for some types of cancer.
Prevention of Neoplasms
While it is not always possible to prevent neoplasms, there are several steps that can reduce the risk of developing cancer. These include:
1. Avoiding exposure to known carcinogens (such as tobacco smoke and radiation)
2. Maintaining a healthy diet and lifestyle
3. Getting regular exercise
4. Not smoking or using tobacco products
5. Limiting alcohol consumption
6. Getting vaccinated against certain viruses that are associated with cancer (such as human papillomavirus, or HPV)
7. Participating in screening programs for early detection of cancer (such as mammograms for breast cancer and colonoscopies for colon cancer)
8. Avoiding excessive exposure to sunlight and using protective measures such as sunscreen and hats to prevent skin cancer.
It's important to note that not all cancers can be prevented, and some may be caused by factors that are not yet understood or cannot be controlled. However, by taking these steps, individuals can reduce their risk of developing cancer and improve their overall health and well-being.
Myogenic regulatory factors
Zinc finger protein 208
Short linear motif
Epstein-Barr virus latent membrane protein 2
WRKY protein domain
Coronavirus nucleocapsid protein
Bacillus virus phi29
Voltage-gated ion channel
Tetratricopeptide repeat protein 39B
Short interspersed nuclear element
60S ribosomal protein L7
Adapter molecule crk
The POZ domain: A conserved protein-protein interaction motif<...
Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral...
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Intramolecular interactions control Vms1 translocation to damaged mitochondria
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RCSB PDB - 1L2Z: CD2BP2-GYF domain in complex with proline-rich CD2 tail segment peptide
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ELM - Detail for LIG WW 1
British Library EThOS: Interactions in the dystrophin-associated protein complex (DAPC) regulated by phosphorylation
Evolutionary conservation of domain-domain interactions | Genome Biology | Full Text
Publications | Max Planck Institute of Biochemistry
Frontiers | Regulation of Dynamic Protein S-Acylation
Structure of the neuronal protein calexcitin suggests a mode of interaction in signalling pathways of learning and memory -...
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NOT-OD-21-148: Request for Information (RFI): Transporters of Nutrients, Dietary Components, Metabolites, and Drugs
ER resident protein 44 promotes malignant phenotype in nasopharyngeal carcinoma through the interaction with ATP citrate lyase ...
Caveolin-1 scaffolding domain peptides enhance anti-inflammatory effect of heme oxygenase-1 through interrupting its interact...
Adenoviruses in Fecal Samples from Asymptomatic Rhesus Macaques, United States - Volume 18, Number 7-July 2012 - Emerging...
PTPN12 Antibody (NB100-60666): Novus Biologicals
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Mittag Lab | St. Jude Research
NIH VideoCast - Molecular mechanisms regulating excitatory synapses
- 38. Physiological levels of calcitonin regulate the mouse osteoclast calcitonin receptor by a protein kinase Alpha-mediated mechanism. (nih.gov)
- 39. Tight junction protein ZO-1 controls organic cation/carnitine transporter OCTN2 (SLC22A5) in a protein kinase C-dependent way. (nih.gov)
- NMR analysis shows that the Fyn but not the Lck tyrosine kinase SH3 domain competes with CD2BP2 GYF-domain binding to the same CD2 proline-rich sequence in vitro. (rcsb.org)
- However it is noted that the kinases inhibitors may not selectively differentiate kinases since a large number of protein kinase enzymes share a common cofactor and similar three-dimensional structure of the catalytic site. (iscb.org)
- LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. (nih.gov)
- 11/05/2007) TOTAL 2008 NEW DESCRIPTORS = 456 MH - A Kinase Anchor Proteins UI - D054758 MN - D12.644.360.24.65 MN - D12.776.157.57.01 MN - D12.776.476.24.69 MS - A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A subtypes to distinct subcellular sites. (nih.gov)
- They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. (nih.gov)
- Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. (nih.gov)
- Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation. (nih.gov)
- Inhibition of DNA binding by the phosphorylation of poly ADP-ribose polymerase protein catalysed by protein kinase C. Biochem Biophys Res Commun 187 , 730-736. (nih.gov)
- Single-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase. (nih.gov)
- The first intracellular domain modulates ligand binding and signal transduction. (nih.gov)
- Intracellular protein interaction domains are essential for eukaryotic signaling. (rcsb.org)
- This PTP contains a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may be related to protein intracellular half-life. (novusbio.com)
- SLC proteins transport the widest variety of molecules across the plasma membrane and intracellular membranes by facilitated diffusion (e.g. (nih.gov)
- Nedd8, a ubiquitin-like protein that regulates RING-domain E3 ubiquitin ligases, promoted Î´ENaC ubiquitination, decreased both the intracellular and cell surface Î´ENaC populations, and decreased Î´ßÎ³ENaC amiloride-sensitive short circuit current (Isc -amiloride) in a mammalian epithelium. (bvsalud.org)
- Protein palmitoylation is catalyzed by members of the DHHC family of eukaryotic integral membrane enzymes so called because of the catalytic Asp-His-His-Cys motif in a cysteine rich domain (CRD) that resides in an intracellular loop. (nih.gov)
- We previously demonstrated that VCP/Cdc48-associated mitochondrial stress responsive 1 (Vms1) is a component of a mitochondrial surveillance system that mediates the stress-responsive degradation of mitochondrial proteins by the proteasome. (nih.gov)
- We further identified positively charged surface residues by KS mutagenesis, which mediates key interactions with the negatively charged ACP surface. (nih.gov)
- Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. (nih.gov)
- RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1. (nih.gov)
- The CUE domain was first described as a region of homology between the yeast Cue1 (coupling of ubiquitin to ER degradation) and human Tollip proteins. (cellsignal.com)
- The domain is approximately 40 amino acids in length and is found in proteins that have a variety of functions, including the degradation of misfolded proteins in the endoplasmic reticulum and protein sorting. (cellsignal.com)
- Although physico-chemically it amounts to attachment of a mere "hydrophobic stick", protein lipidation can modulate protein function by altering structure, folding, interaction with other proteins, degradation and importantly, attachment to membranes. (nih.gov)
- Protein lipidation is the co-translational or post-translational covalent addition of a variety of lipids to target proteins. (frontiersin.org)
- Our current view of cell membranes is far from the historical view of a being floating mixture of lipids and proteins mixed uniformly in the form of bilayers. (intechopen.com)
- Covalent attachment of lipids is one of the most prevalent forms of post translational protein modification. (nih.gov)
- Rev has been reported to interact with many host proteins including importin-ß, histone chaperons (Nap1 and B23), and tubulin through its ARM domain. (nih.gov)
- Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. (nih.gov)
- Retinoblastoma protein recruits histone deacetylase to repress transcription. (nih.gov)
- 24. The LIM domain protein FHL1C interacts with tight junction protein ZO-1 contributing to the epithelial-mesenchymal transition (EMT) of a breast adenocarcinoma cell line. (nih.gov)
- 25. TAZ interacts with zonula occludens-1 and -2 proteins in a PDZ-1 dependent manner. (nih.gov)
- 26. SARS-CoV-2 Envelope (E) protein interacts with PDZ-domain-2 of host tight junction protein ZO1. (nih.gov)
- Furthermore we identified a novel motif on DEPS-1, PBS, which interacts directly with the Piwi domain of PRG-1. (biorxiv.org)
- This protein interacts strongly with caspase 2 and weakly with caspase 9. (nih.gov)
- Rev interacts with Crm1 through a leucine-rich nuclear export signal located in its C-terminus, and with RRE through an Arginine rich motif (ARM) located in the N-terminal region. (nih.gov)
- Impact of Escherichia coli K12 and O18:K1 on human platelets: Differential effects on platelet activation, RNAs and proteins. (nih.gov)
- mRNAs are targeted for silencing by small RNAs based on Watson-Crick base-pair complementarity in complex with members of the Argnonaute (Ago) protein family ( Meister, 2013 ). (biorxiv.org)
- Building upon this understanding, we are now exploring how the architecture of the RNA-binding domains - as well as the specific composition and sequence patterns of the LCD - may promote dynamic compartmentalization of hnRNPA1, other RNA-binding proteins, and RNAs into RNP granules. (stjude.org)
- Bioinformation related to transporter genes, messenger RNAs and their protein products are annotations often found in gene/protein databases such as genecards.org and NCBI . (nih.gov)
- The proteins of interest for this RFI are largely the product the products of two large gene families, the Solute Carrier (SLC) and ATP-Binding Cassette (ABC) family of genes. (nih.gov)
- Most new protein-coding genes originate from old genes by duplication and domain shuffling. (iscb.org)
- Yet de novo protein-coding genes - derived from intergenic DNA - were recently found in multiple species. (iscb.org)
- These genes are of particular interest as they alone can invent novel protein structures. (iscb.org)
- We asked how often de novo genes appear, how many exist in any genome and what proteins they make. (iscb.org)
- The name MADS-box is derived from the four first letters of MCM1 from Saccharomyces cerevisiae , AGAMOUS from Arabidopsis , DEFICIENS from snapdragon and SRF4 from humans, and the proteins encoded by these genes contain a highly conserved region called the MADS-box that is approximately 60 amino acid residues in length ( Messenguy & Dubois, 2003 ). (peerj.com)
- Structurally, almost all MADS-box genes contain a conserved MADS domain consisting of 60 amino acid residues at the N- terminus, and this domain is responsible for binding the CArG-box (CC(A/T) 6 GG) in the regulatory region of target genes ( Messenguy & Dubois, 2003 ). (peerj.com)
- The main difference between plant type I and type II MADS-box genes is whether they contain a K domain. (peerj.com)
- Type I MADS-box genes contain only one highly conserved MADS domain with no or few introns, and their abundance is lower at the transcriptional level. (peerj.com)
- Type II MADS-box genes have a multi-intron structure with the exception of the highly conserved MADS domain. (peerj.com)
- This comprehensive network maps genetic interactions for essential gene pairs, highlighting essential genes as densely connected hubs. (thebiogrid.org)
- These novel composite genes were likely advantageous for their hosts, since they show significant residence times in haloarchaeal genomes-consistent with a long phylogenetic history involving vertical descent and lateral gene transfer-and encode proteins with optimized isoelectric points. (biomedcentral.com)
- There are a range of different mechanisms that can produce novel genes, including de novo genes, synthesized either partly or completely from non-coding DNA [ 12 ], from the divergence of an existing protein-coding sequence beyond the point at which it is recognizable as a homologue (e.g. following gene duplication events), or by fusion or fission of existing protein-coding sequences [ 13 ]. (biomedcentral.com)
- There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. (nih.gov)
- The POZ domain acts as a specific protein-protein interaction domain: The POZ domains of ZID and Ttk can interact with themselves but not with each other, POZ domains from ZF5, or the viral protein SalF17R. (umn.edu)
- In the present work, we developed a single predictive model for building a host-viral interactome based on the identification of structural descriptors from motif-domain interactions of protein complexes deposited in the Protein Data Bank (PDB). (nih.gov)
- therefore, viral and human proteins sharing a descriptor were predicted as interacting proteins. (nih.gov)
- The analysis of the host-viral interactome allowed to identify a set of new interactions that further explain molecular mechanism associated with viral infections and showed that it was able to capture human proteins already associated to viral infections (human infectome) and non-infectious diseases (human diseasome). (nih.gov)
- The analysis of human proteins targeted by viral proteins in the context of a human interactome showed that their neighbors are enriched in proteins reported with differential expression under infection and disease conditions. (nih.gov)
- She currently studies the underlying mechanisms of viral pathogenesis, viral protein-host protein interactions, and the potential use of humanized scFvs and nanobodies for treatment. (nih.gov)
- The HIV-1 Rev protein is a key regulatory factor that is essential for both early and late phases of viral replication cycles, and therefore represents an important viral target for drug development. (nih.gov)
- Skp1 connects cell cycle regulation to the ubiquitin proteolysis machinery through a novel motif, the F-box. (nih.gov)
- However, the POZ domain of GAGA can interact efficiently with the POZ domain of Ttk. (umn.edu)
- Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association, thereby preventing heterotrimer formation. (embl.de)
- This, along with de novo proteins' propensity to interact, increases the chance that some will use their novel structures (and possibly novel functionalities) to integrate into existing genetic networks and survive for a long evolutionary time. (iscb.org)
- A conserved MFP motif in α−helix1 and an LL motif in α−helix 3 interact with the conserved hydrophobic patch of ubiquitin. (cellsignal.com)
- Unlike SH3 domains, which use two surface pockets to accommodate proline residues of ligands, the GYF domain employs phylogenetically conserved hydrophobic residues to create a single interaction surface. (rcsb.org)
- Protein S-acylation is the reversible addition of fatty acids to the cysteine residues of target proteins. (frontiersin.org)
- The removal of fatty acids from acylated cysteine residues is catalyzed by acyl protein thioesterases. (frontiersin.org)
- For the rest of this review, we specifically discuss S-acylation, the covalent linkage of various fatty acids (14-20 carbons) via a thioester bond to the cysteine residues of substrate proteins. (frontiersin.org)
- LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. (nih.gov)
- RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. (embl.de)
- RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state. (embl.de)
- This RGS domain is necessary for conferring upon RGS proteins the capacity to regulate negatively a variety of Galpha protein subunits. (embl.de)
- Previous work found that ENaC gating is regulated by proteases through cleavage of the extracellular domains of the α and Î³ subunits. (bvsalud.org)
- Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS . (nih.gov)
- Recognition modules in proteins that mediate interactions between specific proteins involved in SIGNAL TRANSDUCTION PATHWAYS . (nih.gov)
- These sub-organelle ultrastructures depend on the Piwi-interacting motif of DEPS-1 and mediate piRNA function. (biorxiv.org)
- We have made critical contributions to the conceptual understanding that biomolecular condensates are formed through phase separation and that multivalent interactions in disordered proteins and through domain-motif interactions mediate this process. (stjude.org)
- While the LCD of hnRNPA1 is sufficient to mediate phase separation, its folded RNA-binding domains also contribute to phase separation in the presence of RNA, giving rise to several mechanisms of assembly. (stjude.org)
- These studies define cellular and biochemical mechanisms by which Vms1 locali-zation to mitochondria is controlled to enable an efficient protein quality control system. (nih.gov)
- The tendency and ability of proteins to change shape dictates how cellular components cluster and how sequence and conformation drive function. (stjude.org)
- We have dissected the interaction between HIV-1 Gag and the host cellular ESCRT-associated protein, Alix. (nih.gov)
- This occurred through a decrease in ENaC protein at the cell surface and in the total cellular pool, an effect that did not require the catalytic activity of PCSK9. (bvsalud.org)
- A global genetic interaction network maps a wiring diagram of cellular function. (thebiogrid.org)
- In the cellular milieu, thioesters can be cleaved by thioesterases and thus protein S-acylation is unique in being the only reversible form of protein lipidation. (nih.gov)
- These components are then inserted into enzymes and other proteins for use in a wide range of crucial cellular activities like electron transport in respiratory chain complexes, regulatory sensing, photosynthesis, and DNA repair. (nih.gov)
- 27. Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: binding to PDZ-domain proteins and cell-cell adhesion regulate plasma membrane and nuclear localization of ARVCF. (nih.gov)
- Instead, evidence accumulated in the last three decades has revealed that membrane constituents can segregate to form discrete domains. (intechopen.com)
- Our research focuses on understanding the molecular interactions underlying the formation of membrane-less organelles or so-called biomolecular condensates and how they give rise to function and disease. (stjude.org)
- This study reports the demonstration that localization of Grk protein to the dorsal-anterior region of the oocyte depends on membrane trafficking, differing from the nonmembranous particle transport of its mRNA during this stage. (sdbonline.org)
- During her postdoctoral studies at the University of Massachusetts Medical School (UMASS), she focused on the structure and function of outer membrane proteins, mainly Occ-family of porins from P. aeruginosa , and their role in bacterial pathogenesis and antibiotic resistance. (nih.gov)
- Three members of the membrane bound O-acyltransferase (MBOAT) family, a distinct family of integral membrane enzymes, also catalyze protein lipidation. (nih.gov)
- Short AMINO ACID SEQUENCES which are the BINDING SITES on the LIGANDS of protein interaction domains. (nih.gov)
- Noncoding RNA sequences can regulate gene expression via interactions with epigenetic and other control mechanisms. (stanford.edu)
- This suggests that new structural information will come from understanding the structures of sequences from combined domains. (nih.gov)
- abstract = "We describe a novel zinc finger protein, ZID (zinc finger protein with interaction domain). (umn.edu)
- Our study reveals how specific protein-protein interactions drive the spatial organisation and function of small RNA pathways within membraneless organelles. (biorxiv.org)
- RGS (Regulator of G Protein Signalling) proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. (embl.de)
- Such disorders as hay fever, periodontitis, atherosclerosis, rheumatoid arthritis, and even cancer showed the involvement of similar pathways with a range of protein targets engaged in chronic inflammation development. (lifechemicals.com)
- This screening set was designed based on published data on protein interaction signaling pathways and the protein structural data availability (RCSB protein data bank) along with active protein inhibitors (ChEMBL DB). (lifechemicals.com)
- From NCBI Gene: This gene encodes a member of the Ced-4 family of apoptosis proteins. (nih.gov)
- My laboratory characterizes the molecular mechanisms underlying neurotransmitter receptor transport and localization at the synapse using several research strategies which include (1) defining sorting motifs present in neurotransmitter receptor cytosolic domains, (2) isolating neurotransmitter receptor-associated proteins, and (3) determining the role of protein-protein interactions in trafficking and specific synapse localization. (nih.gov)
- The localization of grk mRNA and its protein product in the oocyte is crucial for the establishment of both the AP and dorsal-ventral axes. (sdbonline.org)
- This finding is based on the study of a newly identified hypomorphic allele of Syx1A whose germ-line clones have defective dorsal follicle-cell specification and abnormal Grk protein localization after stage 7. (sdbonline.org)
- Although no defect was detected in Syx1A clones in Grk posterior localization and signaling to activate EGFR in the posterior follicle cells, it cannot be ruled out that that Syx1A has no role in the posterior localization of Grk protein. (sdbonline.org)
- Protein·protein interactions, which often involve interactions among an acyl carrier protein (ACP) and ACP partner enzymes, are important for coordinating polyketide biosynthesis. (nih.gov)
- What sets these three apart is that each of these three enzymes, Goat, Hhat and Porcupine, has a unique substrate, all secreted signaling proteins and each uses a distinct fatty acyl substrate. (nih.gov)
- They fold to form recognition pockets complementary to the short interaction sequence motifs on their LIGANDS . (nih.gov)
- Of the different forms of protein lipidation, the most pervasive form is attachment of a fatty acid to internal cysteines through a thioester. (nih.gov)
- HN - 2008 BX - Child Abuse, Adult Survivors MH - Agouti Signaling Protein UI - D054366 MN - D12.644.276.49 MN - D12.776.467.49 MN - D23.529.49 MS - A secreted protein of approximately 131 amino acids (depending on species) that regulates the synthesis of eumelanin (brown/black) pigments in MELANOCYTES. (nih.gov)
- HN - 2008 (1993) MH - Agouti-Related Protein UI - D054369 MN - D12.644.276.74 MN - D12.776.467.74 MN - D23.529.74 MS - A secreted protein of approximately 131 amino acids that is related to AGOUTI SIGNALING PROTEIN and is also an antagonist of MELANOCORTIN RECEPTOR activity. (nih.gov)
- Although they have conserved catalytic cores, DHHC enzymes vary in their protein substrate selection, lipid substrate preference, and regulatory mechanisms. (frontiersin.org)
- Of interest, MTD-mediated mitochondrial targeting of Vms1 is negatively regulated by a direct interaction with the Vms1 N-terminus. (nih.gov)
- We generated a global genetic interaction network for Saccharomyces cerevisiae, constructing more than 23 million double mutants, identifying about 550,000 negative and about 350,000 positive genetic interactions. (thebiogrid.org)
- Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. (embl.de)
- 28. Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins. (nih.gov)
- 34. Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins. (nih.gov)
- Identified structural elements suggest that the encoded protein resembles a receptor. (nih.gov)
- This entry represents a structural domain with a multi-helical fold consisting of a 4-helical bundle with a left-handed twist and an up-and-down topology. (embl.de)
- In 2015, she joined the Laboratory of Structural Biology Research and the Protein Expression Laboratory at the National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS). (nih.gov)
- Dr. Eren's research focuses on understanding the structural and mechanistic aspects of Rev-host protein interactions and finding target regions to inhibit Rev activity using antibodies, synthetic peptides, and aptamers. (nih.gov)
- Furthermore, Structural Genomics efforts have contributed 40% of known novel domains. (nih.gov)
- In general, prenylation is an enzymatically mediated multi-step process that adds hydrophobic prenyl moieties to the C-terminal cysteines of substrate proteins. (frontiersin.org)
- CUE domains have been shown to both bind mono and polyubiquitin and some CUE domain-containing proteins are themselves ubiquitinylated in a CUE domain-dependent manner. (cellsignal.com)
- Modeling tools have been used to characterize domain families that bind PI. (nih.gov)
- Proteins that bind PI typically have two motifs (or multiple motifs) which allow for temporal and spatial separation of binding events. (nih.gov)
- The immunogen recognized by this antibody maps to a region between residue 760 and 780 of human protein tyrosine phosphatase, non-receptor type 12 using the numbering given in entry NP_002826.2 (GeneID 5782). (novusbio.com)
- Our laboratory is studying these mechanisms, including SPOP's association with the death-domain-associated protein (DAXX) and the androgen receptor. (stjude.org)
- Using these cell biological approaches, we hope to elucidate the mechanisms of neurotransmitter receptor trafficking in neurons and the role of accessory proteins at central synapses. (nih.gov)
- To understand the complex role of auxilin in uncoating and clathrin assembly in more detail, we analyzed the molecular organization of its clathrin-binding domain (amino acids 547-813). (wikigenes.org)
- Protein Engineering Group and Molecular Modeling Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert-Rössle-Strasse 10, D-13125 Berlin, Germany. (rcsb.org)
- However, the molecular mechanisms of how RNA and proteins in these phase separated organelles assemble remain largely unexplored. (biorxiv.org)
- Ozdemir ES, Jang H, Gursoy A, Keskin O, Li Z , Sacks DB, Nussinov R. Unraveling the molecular mechanism of interactions of the Rho GTPases Cdc42 and Rac1 with the scaffolding protein IQGAP2. (nih.gov)
- We discuss the implications of multimerization for the function of POZ domain proteins. (umn.edu)
- RGS proteins can function as effector antagonists, and recent evidence suggests that RGS proteins can have positive effects on signaling as well. (embl.de)
- Therefore Î´- and α - ßÎ³ENaC channel function may be influenced by RING-domain E3 ubiquitin ligases. (bvsalud.org)
- These interactions were enhanced by Nedd4-2 and were dependent on the catalytic function of Nedd4-2 as well as its WW domains. (bvsalud.org)
- Tyrosine phosphorylation of the scaffold protein IQGAP1 in the MET pathway alters function. (nih.gov)
- No trend was observed between resistance and antibody interactions. (cdc.gov)
- 21. The PDZ motif peptide of ZO-1 attenuates Pseudomonas aeruginosa LPS-induced airway inflammation. (nih.gov)
- This inhibitory effect is not dependent on interactions with other proteins and does not appear dependent on specific interactions between the POZ domain and the finger region. (umn.edu)
- These studies reveal that the Syx1A dependent trafficking of Grk protein is required for efficient EGFR signaling during DV patterning (Tian, 2013). (sdbonline.org)
- Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner. (nih.gov)
- Zhang M, Li Z , Jang H, Hedman AC, Sacks DB, Nussinov R. Ca2+-dependent switch of calmodulin interaction mode with tandem IQ motifs in the scaffolding protein IQGAP1. (nih.gov)
- Protein interactions between a pathogen and its host are fundamental in the establishment of the pathogen and underline the infection mechanism. (nih.gov)
- Probing the selectivity and protein·protein interactions of a nonreducing fungal polyketide synthase using mechanism-based crosslinkers. (nih.gov)
- Here, we employ mechanism-based crosslinkers to successfully probe ACP and ketosynthase (KS) domain interactions in NR-PKSs. (nih.gov)
- We are further investigating the mechanism of the generation of insoluble protein deposits in persistent stress granules in neurodegenerative disease. (stjude.org)
- It is a redundant collection of different structures obtained for the same protein. (iscb.org)
- As in the past, topics of gene cloning, gene expression, protein purification and crystallization and rapid NMR structure determination were highlighted in the meeting program. (nih.gov)
- Mutation of ENaC PY motifs, responsible for inherited hypertension (Liddle syndrome), decreased Hrs binding to ENaC. (bvsalud.org)
- Proteomic analysis of the PIWI protein PRG-1 revealed an interaction with the constitutive P granule protein DEPS-1. (biorxiv.org)
- On the other hand, the prolonged assembly of stress granules can result in their maturation and protein aggregation, giving rise to the hallmarks of neurodegenerative diseases such as ALS. (stjude.org)
- We found that, compared to ancient proteins, de novo proteins are shorter, more disordered, promiscuous (interacting with more proteins and DNA), vulnerable to proteases, and less prone to aggregation. (iscb.org)
- While the majority of the lipid modifications to proteins are irreversible, S-acylation is reversible and can be highly dynamic. (frontiersin.org)
- Our laboratory has shown that a low-complexity domain (LCD) within the RNA-binding protein hnRNPA1 undergoes reversible phase separation into protein-rich droplets. (stjude.org)
- The presence of these additional modules within the RGS proteins provides for multiple novel regulatory interactions performed by these molecules. (embl.de)
- The protein encoded by this gene is phosphorylated and activated by ROCK, a downstream effector of Rho, and the encoded protein, in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. (nih.gov)
- At its amino terminus ZID contains a 120-amino-acid conserved motif present in a large family of proteins that includes both the otherwise unrelated zinc finger proteins, such as Ttk, GAGA, and ZF5, and a group of poxvirus proteins: We therefore refer to this domain as the POZ (poxvirus and zinc finger) domain. (umn.edu)
- 33. The carboxyl terminus of Neph family members binds to the PDZ domain protein zonula occludens-1. (nih.gov)
- LRCH proteins: a novel family of cytoskeletal regulators. (nih.gov)
- The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. (novusbio.com)
- Ced-family members contain a caspase recruitment domain (CARD) and are known to be key mediators of programmed cell death. (nih.gov)
- The HMG-1 box protein family. (nih.gov)
- The encoded protein contains a distinct N-terminal pyrin-like motif, which is possibly involved in protein-protein interactions. (nih.gov)
- Amino acid optimizations, which lowered the isoelectric point of haloarchaeal proteins, and abundant lateral gene transfers from bacteria have been invoked to explain this deep evolutionary transition. (biomedcentral.com)
- It functions as a subunit of a ubiquitin ligase and is important for maintaining appropriate protein levels of many proto-oncogenes. (stjude.org)