CRISPR-mediated knockout plasmids containing guide RNAs targeting BAX, BAK1, NCKAP1, ACSL4, SLC7A11, CYFIP1, WAVE-2, Abi2, HSPC300 were generated in lentiCRISPR v2 (Addgene, #52961) according to the standard protocol. The SLC7A11 cDNA–containing expression construct was described in previous publications25 , 26 . The lentiviral construct expressing membrane-bound green fluorescent protein (mGFP) (#22479) and Rac1-Q61L cDNA-containing construct (#84605) were obtained from Addgene. NCKAP1 cDNA and shRNA constructs targeting RPN1, N-WASP, WHAMM were obtained from the Functional Genomics Core Facility of The University of Texas MD Anderson Cancer Center. NCKAP1 and Rac1-Q61L cDNA were subsequently cloned into the vector pLX302 with a C-terminal V5 tag (Addgene, #25896). WAVE-2 constructs were provided by Dr. Daniel D. Billadeau. All constructs were confirmed by DNA sequencing. The sequences of gRNAs and shRNA used in this study are listed in Supplementary Table 4 . Necroptosis inhibitor Nec-1s (#2263) was from BioVision, and necrosis inhibitor Necrox-2 (#ALX-430-166-M001) was from Enzo. Ferroptosis inducer (1S,3R)-RSL3 (#19288) and apoptosis inducer staurosporine (#81590) were from Cayman Chemical. L-[1, 2, 1', 2'-14C]-cystine (#NEC854010UC) was from PerkinElmer. KL-11743 was from Kadmon. The following reagents were obtained from Sigma-Aldrich: 2-deoxy-D-glucose (#D8375-1G), Trolox (#238813), 4-Hydroxy-TEMPO (Tempol) (#176141), beta-mercaptoethanol (2ME) (#M6250), deferoxamine mesylate salt (DFO) (#D9533), ferrostatin-1 (#SML0583), chloroquine (#C6628), diamide (#D3648), diethyl-maleate (#D97703, BAY-876 (#SML1774), and L-Cystine (#C7602). All reagents were dissolved according to manufacturers’ instructions.
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Amino Acid
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Cystine
Cystine
Cystine is a disulfide-containing amino acid that plays a crucial role in protein structure and function.
It is formed by the oxidation of two cysteine residues, resulting in a stable, cyclic molecule.
Cystine is an important component of many proteins, contributing to their stability and three-dimensional structure.
It is also involved in various biological processes, including redox reactions, disulfide bond formation, and the regulation of cellular functions.
Cystine research is vital for understanding protien folding, protein-protein interacions, and the underlying mechanisms of diseases associated with cystine metbaolism.
Accurate and reproducible research in this area can lead to advancements in our understanding of cystine's role in health and disease.
It is formed by the oxidation of two cysteine residues, resulting in a stable, cyclic molecule.
Cystine is an important component of many proteins, contributing to their stability and three-dimensional structure.
It is also involved in various biological processes, including redox reactions, disulfide bond formation, and the regulation of cellular functions.
Cystine research is vital for understanding protien folding, protein-protein interacions, and the underlying mechanisms of diseases associated with cystine metbaolism.
Accurate and reproducible research in this area can lead to advancements in our understanding of cystine's role in health and disease.
Most cited protocols related to «Cystine»
2-Mercaptoethanol
ABI2 protein, human
Apoptosis
BAK1 protein, human
BAY-876
Caimans
Chloroquine
Cloning Vectors
Clustered Regularly Interspaced Short Palindromic Repeats
Cystine
Diamide
diethyl maleate
DNA, Complementary
Ferroptosis
ferrostatin-1
Glucose
Malignant Neoplasms
Membrane Proteins
Mesylate, Deferoxamine
NCKAP1 protein, human
Necroptosis
Necrosis
oxytocin, 1-desamino-(O-Et-Tyr)(2)-
Plasmids
RNA
Salts
Short Hairpin RNA
Staurosporine
tempol
TEMPOL-H
Trolox C
WASL protein, human
2-nitro-5-mercaptobenzoic acid
Acids
Alkylation
Amines
Biological Assay
Chromatography
Cystine
dansyl chloride
derivatives
Dinitrofluorobenzene
Disulfides
Dithionitrobenzoic Acid
Enzyme Assays
Fluorescence
Fluorometry
Glutathione Disulfide
Glutathione Reductase
High-Performance Liquid Chromatographies
Hypersensitivity
Iodoacetic Acid
NADP
Nitrobenzoic Acids
Plasma
Population Group
Sulfhydryl Compounds
Theoretical peptide isoelectric points are calculated using the bisection method described by Kozlowski [17 –19 (link)]. The net charge of the peptide can be found using the Henderson–Hasselbalch equation, taking into account contributions from negatively and positively charged groups (first and second terms in Eq. (1 ) respectively, where Ka is the acid dissociation constant of the amino acid).
As the isoelectric point (pI) represents the pH at which the net charge of the peptide equals zero, finding the root of this equation (in this case numerically, using the bisection method) gives the pI (or pH at zero charge).
Peptide Calculator takes into account side chain charge contributions from Arg, Asp, Cys, Glu, His, Lys and Tyr residues, in addition to the N-terminal amine and C-terminal carboxyl groups (only if the terminus types are set to ‘Unmodified’ and ‘Acid’ respectively). Other residue side chains are not taken into account for pI estimation, and are designated ‘Other’ in the charge summary pie chart.
Molar extinction coefficients are estimated using Eq. (2 ), described by Pace et al. [20 (link)]. The formula takes into account numbers of Trp and Tyr residues in the peptide ( and respectively), in addition to the number of cystine residues ( ) formed via disulfide bond formation between pairs of cysteine side chains (reduced cysteine residues do not contribute significantly to the absorbance above 275 nm [20 (link)]).
Peptide Calculator outputs two values for , calculating the theoretical molar extinction coefficient based on either formation of the maximum number of disulfide bonds possible ( equal to the number of cysteine residue pairs), or complete reduction resulting in the absence of disulfides ( ).
As the isoelectric point (pI) represents the pH at which the net charge of the peptide equals zero, finding the root of this equation (in this case numerically, using the bisection method) gives the pI (or pH at zero charge).
Peptide Calculator takes into account side chain charge contributions from Arg, Asp, Cys, Glu, His, Lys and Tyr residues, in addition to the N-terminal amine and C-terminal carboxyl groups (only if the terminus types are set to ‘Unmodified’ and ‘Acid’ respectively). Other residue side chains are not taken into account for pI estimation, and are designated ‘Other’ in the charge summary pie chart.
Molar extinction coefficients are estimated using Eq. (
Peptide Calculator outputs two values for , calculating the theoretical molar extinction coefficient based on either formation of the maximum number of disulfide bonds possible ( equal to the number of cysteine residue pairs), or complete reduction resulting in the absence of disulfides ( ).
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Acids
Amines
Amino Acids, Acidic
Cysteine
Cystine
Disulfides
Extinction, Psychological
Molar
Peptides
Plant Roots
Control isolates used for assay design and optimization are defined in Table
S1 .
626 cell lysates were used to determine the sensitivity of the
sodC assay (Table 1 and Table S2 ), including lysates prepared from a
temporally and geographically dispersed convenience sample of isolates from the
CDC Meningitis Laboratory strain collection (received 1993–2008,
n = 106) and all isolates from a US carriage study
(n = 520) [20] , [21] (link) known to be Nm by SASG [1] , [2] , rt-PCR serogrouping [5] (link), NH
strips (bioMérieux® sa), and Cystine Trypticase Agar (CTA) sugars
(Remel) [1] ,
[2] . To
further confirm identification, multilocus sequence typing (MLST) was performed
on all U.S. carriage study and ctrA-negative NG isolates.
The specificity of the sodC assay for detecting only
meningococci was determined using cell lysates from a total of 244 non-Nm
isolates (Table 2 ).
S1
626 cell lysates were used to determine the sensitivity of the
sodC assay (
temporally and geographically dispersed convenience sample of isolates from the
CDC Meningitis Laboratory strain collection (received 1993–2008,
n = 106) and all isolates from a US carriage study
(n = 520) [20] , [21] (link) known to be Nm by SASG [1] , [2] , rt-PCR serogrouping [5] (link), NH
strips (bioMérieux® sa), and Cystine Trypticase Agar (CTA) sugars
(Remel) [1] ,
[2] . To
further confirm identification, multilocus sequence typing (MLST) was performed
on all U.S. carriage study and ctrA-negative NG isolates.
The specificity of the sodC assay for detecting only
meningococci was determined using cell lysates from a total of 244 non-Nm
isolates (
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Agar
Biological Assay
Cells
Cystine
Hypersensitivity
Meningitis
Reverse Transcriptase Polymerase Chain Reaction
Strains
Sugars
trypticase
Ventilatory parameters were recorded in freely moving rats by whole body plethysmography (PLY3223; Data Sciences International, St. Paul, MN) as described previously23 (link)–27 (link). The rats were placed in individual chambers and given 60 min to acclimatize to allow true resting ventilatory parameters to be established. Study 1—see Supplemental Table S1 : Two groups of rats received a bolus injection of morphine (10 mg/kg, IV) and after 15 min, one group received an injection of vehicle (saline) whereas the other received an injection of d -cystine diEE (500 μmol/kg, IV) and ventilatory parameters were recorded for a further 75 min. Study 2—see Supplemental Table S3 : Two groups of rats received a bolus injection of morphine (10 mg/kg, IV) and after 15 min, one group received an injection of vehicle (saline) whereas the other received an injection of d -cystine (500 μmol/kg, IV) and ventilatory parameters were recorded for a further 75 min. Study 3—see Supplemental Table S4 : Since Trivedi and Deth7 (link) proposed that administration of N-acetyl- l -cysteine (l -NAC) may help reverse the redox-based epigenetic status of opioid addiction, we thought it appropriate to also determine whether the thiolester, l -N-acetylcysteine methyl ester (l -NACme), which is a highly cell penetrable reducing agent21 (link), would reverse the negative effects of morphine on breathing. Two groups of rats received a bolus injection of morphine (10 mg/kg, IV) and after 15 min, one group received an injection of vehicle (saline) whereas the other received an injection l -NACme (500 μmol/kg, IV)21 (link). The rats received another injection of vehicle or l -NACme (500 μmol/kg, IV) 15 min later and ventilatory parameters were recorded for a further 60 min.
Due to the closeness of the body weights of all of the groups of rats, ventilatory data are shown without any corrections for body weight. The provided software (Fine Pointe, BUXCO) constantly corrected digitized values for changes in chamber temperature and humidity. Pressure changes associated with the respiratory waveforms were then converted to volumes (i.e., TV, PIF and PEF) using the algorithm of Epstein and colleagues28 (link)–30 (link). Specifically, factoring in chamber temperature and humidity, the cycle analyzers filtered the acquired signals, and BUXCO algorithms (Fine Pointe) generated an array of box flow data that identified a waveform segment as an acceptable breath. From that data vector, the minimum and maximum values were determined. Flows at this point were considered to be “box flow” signals. From this array, the minimum and maximum box flow values were determined and multiplied by a compensation factor provided by the selected algorithm50 (link),51 (link), thus producing TV, PIF and PEF values that were used to determine accepted and rejected waveforms, with rejected waveforms remaining below 5% throughout all phases of the protocols except for a transient rise in rejection of breaths to 15–20% for 1–2 min after injection of morphine (data not shown).
Due to the closeness of the body weights of all of the groups of rats, ventilatory data are shown without any corrections for body weight. The provided software (Fine Pointe, BUXCO) constantly corrected digitized values for changes in chamber temperature and humidity. Pressure changes associated with the respiratory waveforms were then converted to volumes (i.e., TV, PIF and PEF) using the algorithm of Epstein and colleagues28 (link)–30 (link). Specifically, factoring in chamber temperature and humidity, the cycle analyzers filtered the acquired signals, and BUXCO algorithms (Fine Pointe) generated an array of box flow data that identified a waveform segment as an acceptable breath. From that data vector, the minimum and maximum values were determined. Flows at this point were considered to be “box flow” signals. From this array, the minimum and maximum box flow values were determined and multiplied by a compensation factor provided by the selected algorithm50 (link),51 (link), thus producing TV, PIF and PEF values that were used to determine accepted and rejected waveforms, with rejected waveforms remaining below 5% throughout all phases of the protocols except for a transient rise in rejection of breaths to 15–20% for 1–2 min after injection of morphine (data not shown).
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Acetylcysteine
Body Weight
Cells
Cloning Vectors
Cystine
Esters
factor A
Humidity
Morphine
N-acetylcysteine lysinate
Opiate Addiction
Oxidation-Reduction
Plethysmography, Whole Body
Pressure
Rattus norvegicus
Respiratory Rate
Saline Solution
Transients
Most recents protocols related to «Cystine»
Example 14
Cystinuria is a genetic disorder of amino acid import in the kidney characterized by excessive excretion of cystine, and dibasic amino acids (ornitihine, lysine, and arginine) in the urine, and cystine stone formation in the urinary tract.
The potential of a methionine consuming strain described herein to treat, prevent, or reduce cystinuria was evaluated by analyzing the effect of a methionine restricted diet in a Slc3a1 knockout (KO) mouse model for cystinuria. Slc3a1 KO mice were subjected to a reduction in the methionine content of diet from the standard 0.62% to 0.12% for eight weeks, and cysteine as well as cystine levels in urine and plasma, and stone formation in the bladder were evaluated according to a scheme shown in
Cystine stone formation was not observed in any of the twelve mice on the low-methionine diet. In contrast, bladder stones were observed in nine out of twelve mice (75%) on the 0.62% diet. Time of stone formation ranged from 2-8 weeks following diet treatment.
These data suggest that a treatment resulting in a reduction in plasma or urinary methionine, e.g., administration of a methionine-consuming strain described herein, is a promising approach for the treatment of cystinuria.
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Amino Acid Metabolism, Inborn Errors
Amino Acids, Diamino
Arginine
Calculi
Calculus, Bladder
Cysteine
Cystine
Cystinuria
Diet
Dietary Restriction
Genes, vif
Kidney
Lysine
Methionine
Mice, Knockout
Mus
Plasma
Strains
Urinary Calculi
Urine
Analysis of carbon, hydrogen, nitrogen, sulfur and oxygen content was performed by elemental analysis (EA) with a Flash Smart EA CHNS/O with MV (Thermo Scientific, USA). Each sample was measured twice. BBOT (2,5-(bis(5-tert-butyl- 2-benzo-oxazol-2-yl) thiophene) was used as standard for the CHNS analysis and a cystine standard was used for the oxygen analysis.
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Carbon
Cystine
Hydrogen
Nitrogen
Oxygen
Sulfur
TERT protein, human
Thiophene
293T cells were transfected with plasmids in 12-well culture plates as described above, 15 h p.t. cells were starved in DMEM lacking L-methionine and L-cysteine (Gibco) for 30 min, and subsequently incubated with 44 μCi EasyTag EXPRESS 35S protein labeling mix (PerkinElmer) for 30 min. Total protein samples were analyzed by SDS PAGE as described above. 35S-labeled proteins were detected by drying the gels and exposing them to a Storage Phosphor screen, which was scanned 3 days later with a Storm 820 scanner (GE Healthcare).
Vero E6 cells in 12-well culture plates with coverslips were transfected with 0.5 ug plasmid DNA and 3 ul Lipofectamine2000/ml in DMEM containing 8% FCS without antibiotics. At 18 h p.t. cells were starved in DMEM lacking L-methionine and L-cystine (Gibco) to which 250 μM L-cystine was added for 30 min, and subsequently incubated with 25 μM Click-IT AHA (L-Azidohomoalanine) (Invitrogen) for 1h. Cells were washed twice with warm PBS and fixed for 15 min in 3% PFA in PBS. Cells were permeabilized in 0.2% Triton X-100 in PBS for 15 min and washed with 3% FCS in PBS. Cells were incubated with 15 uM Click-iT DIBO-Alexa Fluor 555 (Invitrogen) in 1% FCS in PBS for 1h at RT in the dark. Cells were washed twice with 1% FCS in PBS and twice with PBS-Glycine for a total of >15 min. Cells were incubated with a rabbit antiserum against CHIKV nsP2 helicase (kind gift from prof. Andres Merits, University of Tartu, Estonia) diluted 1:1000 in 5% FCS in PBS for 1h at 37°C in the dark. Cells were washed 3 times with PBS-Glycine for 10 min. The secondary antibody goat-a-rabbit-Alexa488 (Invitrogen) was diluted 1:300 in 5% FCS in PBS and cells were incubated for 1h at 37°C in the dark. Cells were washed 3 times in PBS for 10 min. Coverslips were mounted with Prolong Glass and analyzed using a Leica DM6B Fluorescence Microscope and LASX software (Leica).
Vero E6 cells in 12-well culture plates with coverslips were transfected with 0.5 ug plasmid DNA and 3 ul Lipofectamine2000/ml in DMEM containing 8% FCS without antibiotics. At 18 h p.t. cells were starved in DMEM lacking L-methionine and L-cystine (Gibco) to which 250 μM L-cystine was added for 30 min, and subsequently incubated with 25 μM Click-IT AHA (L-Azidohomoalanine) (Invitrogen) for 1h. Cells were washed twice with warm PBS and fixed for 15 min in 3% PFA in PBS. Cells were permeabilized in 0.2% Triton X-100 in PBS for 15 min and washed with 3% FCS in PBS. Cells were incubated with 15 uM Click-iT DIBO-Alexa Fluor 555 (Invitrogen) in 1% FCS in PBS for 1h at RT in the dark. Cells were washed twice with 1% FCS in PBS and twice with PBS-Glycine for a total of >15 min. Cells were incubated with a rabbit antiserum against CHIKV nsP2 helicase (kind gift from prof. Andres Merits, University of Tartu, Estonia) diluted 1:1000 in 5% FCS in PBS for 1h at 37°C in the dark. Cells were washed 3 times with PBS-Glycine for 10 min. The secondary antibody goat-a-rabbit-Alexa488 (Invitrogen) was diluted 1:300 in 5% FCS in PBS and cells were incubated for 1h at 37°C in the dark. Cells were washed 3 times in PBS for 10 min. Coverslips were mounted with Prolong Glass and analyzed using a Leica DM6B Fluorescence Microscope and LASX software (Leica).
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Alexa Fluor 555
Antibiotics
azidohomoalanine
Cell Culture Techniques
Cells
Cysteine
Cystine
DNA Helicases
Gels
Glycine
Goat
HEK293 Cells
Immune Sera
Immunoglobulins
Methionine
Microscopy, Fluorescence
Phosphorus
Plasmids
Proteins
Rabbits
SDS-PAGE
T-Lymphocyte
Triton X-100
Protocol full text hidden due to copyright restrictions
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Acetylation
Alkylation
Cystine
Cytokinesis
Digestion
Immune Tolerance
Ions
Lysine
Methionine
Mice, House
Peptide Library
Peptides
Proteins
Student
Trypsin
All SILAC/MS data were processed using the MaxQuant software (Max Planck Institute of Biochemistry; v.1.5.3.30). The default values were used for the first search tolerance and main search tolerance—20 ppm and 6 ppm, respectively. Labels were set to Arg10 and Lys8. MaxQuant was set up to search the reference mouse proteome database downloaded from UniProt on 9 January 2020. MaxQuant performed the search assuming trypsin digestion with up to two missed cleavages. Peptide, site and protein false-discovery rate (FDR) were all set to 1% with a minimum of one peptide needed for identification but two peptides needed to calculate a protein level ratio. The following modifications were used as variable modifications for identifications and included for protein quantification: oxidation of methionine, acetylation of the protein N terminus, ubiquitination of lysine, phosphorylation of serine, threonine and tyrosine residues, and carbamidomethyl on cystine. Intensity values measured in all replicates were log2-transformed (Supplementary Table 4 ), P values were computed using Fisher’s tests and corrected using Benjamini–Hochberg FDR correction. All raw MS data files have been deposited to the ProteomeXchange Consortium (and PXD039176). The Gene Ontology term enrichment analysis was performed using Enrichr online tool (https://maayanlab.cloud/Enrichr/ ), STRING (https://string-db.org ) and clusterProfiler57 (link).
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Acetylation
Cystine
Cytokinesis
Digestion
Immune Tolerance
Lysine
Methionine
Mice, Laboratory
nucleoprotein, Measles virus
Peptides
Phosphorylation
Proteins
Proteome
Serine
Staphylococcal Protein A
Threonine
Trypsin
Tyrosine
Ubiquitination
Top products related to «Cystine»
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L-cystine is a naturally occurring amino acid that can be used as a laboratory reagent. It is a white, crystalline solid that is soluble in water and dilute acids or bases. L-cystine serves as a source of sulfur in various biochemical applications.
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Cystine is a laboratory equipment product manufactured by Merck Group. It is a naturally occurring amino acid that is used in various biological and chemical applications. Cystine serves as a core component in the production and analysis of cellular and molecular structures.
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L-methionine is an essential amino acid that is used in various laboratory applications. It serves as a building block for proteins and plays a role in cellular metabolism. L-methionine is commonly utilized in cell culture media, biochemical assays, and research studying protein synthesis and amino acid metabolism.
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Cysteine is a non-essential amino acid used as a laboratory reagent. It is a white crystalline solid that is soluble in water and organic solvents. Cysteine plays a role in the formation of disulfide bonds in proteins and serves as a precursor to other sulfur-containing compounds.
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DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.
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Methionine is an essential amino acid used in laboratory settings. It is a colorless, crystalline compound that serves as a building block for proteins and other biomolecules. Methionine is a key component in various biochemical processes and is utilized in experimental procedures within the scientific community.
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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[14C] cystine is a radioactive isotope of the amino acid cystine. It is used as a labeling agent in various research applications, such as studying protein synthesis and metabolism.
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Sulfasalazine is a laboratory compound used as a chemical reagent. It is a yellow, crystalline powder that is commonly utilized in various analytical and research applications. The core function of Sulfasalazine is to serve as a chemical standard or reference material in laboratory settings.
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L-glutamine is a laboratory-grade amino acid that serves as a key component in cell culture media. It provides a source of nitrogen and energy for cellular metabolism, supporting the growth and proliferation of cells in vitro.
More about "Cystine"
Cystine, a disulfide-containing amino acid, plays a vital role in protein structure and function.
Formed by the oxidation of two cysteine residues, this cyclic molecule is an important component of many proteins, contributing to their stability and three-dimensional conformation.
Cystine research is crucial for understanding protein folding, protein-protein interactions, and the underlying mechanisms of diseases associated with cystine metabolism, such as cystinosis.
Cystine, also known as L-cystine, is closely related to other sulfur-containing amino acids like L-methionine and cysteine.
These compounds are essential for various biological processes, including redox reactions, disulfide bond formation, and the regulation of cellular functions.
The culture medium DMEM, which contains L-glutamine and fetal bovine serum (FBS), is commonly used in cystine research to provide the necessary nutrients for cell growth and development.
Accurate and reproducible research on cystine is vital for advancing our understanding of its role in health and disease.
Scientists often utilize radioactive [14C] cystine to study its metabolism and distribution within cells and organisms.
Compounds like sulfasalazine, which can interfere with cystine transport, are also important tools in cystine research, as they help elucidate the regulatory mechanisms involved in cystine homeostasis.
By leveraging the insights gained from the MeSH term description and the metadescription, researchers can enhance the reproducibility and accuracy of their cystine studies.
PubCompare.ai's AI-driven protocols can assist in locating the best research approaches from literature, preprints, and patents, enabling researchers to identify the most effective methods and streamline their investigative processes.
With these resources, scientists can achieve more reliable results and deepen our understanding of cystine's critical functions in protein structure, cellular processes, and disease pathogenesis.
Formed by the oxidation of two cysteine residues, this cyclic molecule is an important component of many proteins, contributing to their stability and three-dimensional conformation.
Cystine research is crucial for understanding protein folding, protein-protein interactions, and the underlying mechanisms of diseases associated with cystine metabolism, such as cystinosis.
Cystine, also known as L-cystine, is closely related to other sulfur-containing amino acids like L-methionine and cysteine.
These compounds are essential for various biological processes, including redox reactions, disulfide bond formation, and the regulation of cellular functions.
The culture medium DMEM, which contains L-glutamine and fetal bovine serum (FBS), is commonly used in cystine research to provide the necessary nutrients for cell growth and development.
Accurate and reproducible research on cystine is vital for advancing our understanding of its role in health and disease.
Scientists often utilize radioactive [14C] cystine to study its metabolism and distribution within cells and organisms.
Compounds like sulfasalazine, which can interfere with cystine transport, are also important tools in cystine research, as they help elucidate the regulatory mechanisms involved in cystine homeostasis.
By leveraging the insights gained from the MeSH term description and the metadescription, researchers can enhance the reproducibility and accuracy of their cystine studies.
PubCompare.ai's AI-driven protocols can assist in locating the best research approaches from literature, preprints, and patents, enabling researchers to identify the most effective methods and streamline their investigative processes.
With these resources, scientists can achieve more reliable results and deepen our understanding of cystine's critical functions in protein structure, cellular processes, and disease pathogenesis.