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32 results for “glycocode”
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Do you know the mammalian monosaccharides? Most people who know their #aminoacids and #nucleotides answer no to this quesion... Want to learn? Download our new #glycogang #glycotime poster today! http://glyco-alberta.ca/educational-resources/ (in the for educators tab). Learn more about #glycosylation #education #biochemistry
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Do you know the mammalian monosaccharides? Most people who know their #aminoacids and #nucleotides answer no to this quesion... Want to learn? Download our new #glycogang #glycotime poster today! http://glyco-alberta.ca/educational-resources/ (in the for educators tab). Learn more about #glycosylation #education #biochemistry
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Do you know the mammalian monosaccharides? Most people who know their #aminoacids and #nucleotides answer no to this quesion... Want to learn? Download our new #glycogang #glycotime poster today! http://glyco-alberta.ca/educational-resources/ (in the for educators tab). Learn more about #glycosylation #education #biochemistry
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Do you know the mammalian monosaccharides? Most people who know their #aminoacids and #nucleotides answer no to this quesion... Want to learn? Download our new #glycogang #glycotime poster today! http://glyco-alberta.ca/educational-resources/ (in the for educators tab). Learn more about #glycosylation #education #biochemistry
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Do you know the mammalian monosaccharides? Most people who know their #aminoacids and #nucleotides answer no to this quesion... Want to learn? Download our new #glycogang #glycotime poster today! http://glyco-alberta.ca/educational-resources/ (in the for educators tab). Learn more about #glycosylation #education #biochemistry
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Intro: CERC in Glycomics, Professor of #Chemistry at University of Alberta, Director of a #Glycomics Institute (www.glyco-alberta.ca). I ❤️ #glycotime, studying glycans in #cancer #virology #hostresponse #vaccine response #microbiome etc using our #lectinmicroarray technology and #systemsbio approaches. Also, I study #miRNA #microRNA regulation of glycans and now upregulatory miRNA. #RNA. Am a #momademic #momademia and into #EDI #inclusion #womeninsteam #womeninstem #chembio #chemiverse
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Intro: CERC in Glycomics, Professor of #Chemistry at University of Alberta, Director of a #Glycomics Institute (www.glyco-alberta.ca). I ❤️ #glycotime, studying glycans in #cancer #virology #hostresponse #vaccine response #microbiome etc using our #lectinmicroarray technology and #systemsbio approaches. Also, I study #miRNA #microRNA regulation of glycans and now upregulatory miRNA. #RNA. Am a #momademic #momademia and into #EDI #inclusion #womeninsteam #womeninstem #chembio #chemiverse
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Intro: CERC in Glycomics, Professor of #Chemistry at University of Alberta, Director of a #Glycomics Institute (www.glyco-alberta.ca). I ❤️ #glycotime, studying glycans in #cancer #virology #hostresponse #vaccine response #microbiome etc using our #lectinmicroarray technology and #systemsbio approaches. Also, I study #miRNA #microRNA regulation of glycans and now upregulatory miRNA. #RNA. Am a #momademic #momademia and into #EDI #inclusion #womeninsteam #womeninstem #chembio #chemiverse
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Intro: CERC in Glycomics, Professor of #Chemistry at University of Alberta, Director of a #Glycomics Institute (www.glyco-alberta.ca). I ❤️ #glycotime, studying glycans in #cancer #virology #hostresponse #vaccine response #microbiome etc using our #lectinmicroarray technology and #systemsbio approaches. Also, I study #miRNA #microRNA regulation of glycans and now upregulatory miRNA. #RNA. Am a #momademic #momademia and into #EDI #inclusion #womeninsteam #womeninstem #chembio #chemiverse
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Intro: CERC in Glycomics, Professor of #Chemistry at University of Alberta, Director of a #Glycomics Institute (www.glyco-alberta.ca). I ❤️ #glycotime, studying glycans in #cancer #virology #hostresponse #vaccine response #microbiome etc using our #lectinmicroarray technology and #systemsbio approaches. Also, I study #miRNA #microRNA regulation of glycans and now upregulatory miRNA. #RNA. Am a #momademic #momademia and into #EDI #inclusion #womeninsteam #womeninstem #chembio #chemiverse
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A more recent example, our work on #COVID__19 , in which we found a #glycotime signature of severity in plasma and tissue.
https://pubs.acs.org/doi/10.1021/acsinfecdis.2c00421?ref=PDF
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A more recent example, our work on #COVID__19 , in which we found a #glycotime signature of severity in plasma and tissue.
https://pubs.acs.org/doi/10.1021/acsinfecdis.2c00421?ref=PDF
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Serious diseases—ranging from emphysema and cystic fibrosis to Alzheimer's disease—can result when the 🔹cellular oversight of protein folding goes awry🔹.
Identifying the glyco-code responsible for high-fidelity folding and quality control could be a promising way for drug therapies to target many diseases.
Scientists once thought that the single code governing life was #DNA, and that everything was governed by how DNA's four building blocks—A, C, G and T—combined and recombined.
But in recent decades, it has become clear that there are other codes at work, and especially in building the intricately folded, secreted proteins that are created in 🔸the human cell's protein factory, the "endoplasmic reticulum" (ER)🔸, a membrane-enclosed compartment where protein folding begins.
Approximately 7,000 different proteins—one-third of all the proteins in the human body—mature in the ER.
The secreted proteins—collectively known as the "#secretome"—are responsible for everything from our body's enzymes to its immune and digestive systems and must be formed correctly for the human body to function normally.Special molecules called "#chaperones," help fold the protein into its final shape.
They also help to identify proteins that haven't folded quite correctly, lending them additional help in refolding, or, if they're hopelessly misfolded, targeting them for destruction before they cause damage.
However, the chaperone system itself, which comprises a part of the cell's quality control department, sometimes fails, and when it does, the results can be catastrophic for our health.
The discovery of the carbohydrate-based chaperone system in the ER was due to the pioneering work that 👉Daniel Hebert, professor of biochemistry and molecular biology at UMass Amherst and one of the paper's senior authors, initiated as a postdoctoral fellow in the 1990s.
"The tools we have now, including glycoproteomics and mass spectrometry at UMass Amherst's Institute for Applied Life Sciences, are allowing us to answer questions that have remained open for over 25 years," says Hebert. "The lead author of this new paper, 👉Kevin Guay, is doing things I could only dream of when I first started."
Among the most pressing of these unanswered questions is: ♦️how do chaperones know when 7,000 different origami-like proteins are correctly folded?♦️
We know now that the answer involves an "ER gatekeeper" enzyme known as #UGGT, and a host of carbohydrate tags, called "N-glycans", which are linked to specific sites in the protein's amino acid sequence.Guay, who is completing his Ph.D. in the molecular cellular biology program at UMass Amherst, focused on two specific mammalian proteins, known as "alpha-1 antitrypsin" and "antithrombin".
⭐️Using CRISPR-edited cells, he and his co-authors modified the ER chaperone network to determine how the presence and location of N-glycans affected protein folding.
They watched as the disease variants were recognized by the ER gatekeeper UGGT and, in order to peer more closely, developed a number of innovative glycoproteomics techniques using mass spectrometry to understand what happens to the glycans that stud the surface of the proteins.
What they discovered is that ⚠️the enzyme UGGT "tags" misfolded proteins with sugars placed in specific positions. ⚠️
It's a sort of code that the chaperones can then read to determine exactly where the folding process went wrong and how to fix it.
"This is the first time that we've been able to see where UGGT puts sugars on proteins made in human cells for quality control," says Guay.
"We now have a platform for extending our understanding of how sugar tags can send proteins for further quality control steps and our work suggests that UGGT is a promising avenue for targeted drug therapy research."
"What's so exciting about this research," says👉 Lila Gierasch, distinguished professor of biochemistry and molecular biology at UMass Amherst and one of the paper's co-authors, "is the discovery that glycans act as a code for protein folding in the ER.
The discovery of the role that UGGT plays opens the door to future advancement in understanding and eventually treating the hundreds of diseases that result from misfolded proteins."
https://phys.org/news/2023-12-cellular-code-protein-therapeutic-avenues.html
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Serious diseases—ranging from emphysema and cystic fibrosis to Alzheimer's disease—can result when the 🔹cellular oversight of protein folding goes awry🔹.
Identifying the glyco-code responsible for high-fidelity folding and quality control could be a promising way for drug therapies to target many diseases.
Scientists once thought that the single code governing life was #DNA, and that everything was governed by how DNA's four building blocks—A, C, G and T—combined and recombined.
But in recent decades, it has become clear that there are other codes at work, and especially in building the intricately folded, secreted proteins that are created in 🔸the human cell's protein factory, the "endoplasmic reticulum" (ER)🔸, a membrane-enclosed compartment where protein folding begins.
Approximately 7,000 different proteins—one-third of all the proteins in the human body—mature in the ER.
The secreted proteins—collectively known as the "#secretome"—are responsible for everything from our body's enzymes to its immune and digestive systems and must be formed correctly for the human body to function normally.Special molecules called "#chaperones," help fold the protein into its final shape.
They also help to identify proteins that haven't folded quite correctly, lending them additional help in refolding, or, if they're hopelessly misfolded, targeting them for destruction before they cause damage.
However, the chaperone system itself, which comprises a part of the cell's quality control department, sometimes fails, and when it does, the results can be catastrophic for our health.
The discovery of the carbohydrate-based chaperone system in the ER was due to the pioneering work that 👉Daniel Hebert, professor of biochemistry and molecular biology at UMass Amherst and one of the paper's senior authors, initiated as a postdoctoral fellow in the 1990s.
"The tools we have now, including glycoproteomics and mass spectrometry at UMass Amherst's Institute for Applied Life Sciences, are allowing us to answer questions that have remained open for over 25 years," says Hebert. "The lead author of this new paper, 👉Kevin Guay, is doing things I could only dream of when I first started."
Among the most pressing of these unanswered questions is: ♦️how do chaperones know when 7,000 different origami-like proteins are correctly folded?♦️
We know now that the answer involves an "ER gatekeeper" enzyme known as #UGGT, and a host of carbohydrate tags, called "N-glycans", which are linked to specific sites in the protein's amino acid sequence.Guay, who is completing his Ph.D. in the molecular cellular biology program at UMass Amherst, focused on two specific mammalian proteins, known as "alpha-1 antitrypsin" and "antithrombin".
⭐️Using CRISPR-edited cells, he and his co-authors modified the ER chaperone network to determine how the presence and location of N-glycans affected protein folding.
They watched as the disease variants were recognized by the ER gatekeeper UGGT and, in order to peer more closely, developed a number of innovative glycoproteomics techniques using mass spectrometry to understand what happens to the glycans that stud the surface of the proteins.
What they discovered is that ⚠️the enzyme UGGT "tags" misfolded proteins with sugars placed in specific positions. ⚠️
It's a sort of code that the chaperones can then read to determine exactly where the folding process went wrong and how to fix it.
"This is the first time that we've been able to see where UGGT puts sugars on proteins made in human cells for quality control," says Guay.
"We now have a platform for extending our understanding of how sugar tags can send proteins for further quality control steps and our work suggests that UGGT is a promising avenue for targeted drug therapy research."
"What's so exciting about this research," says👉 Lila Gierasch, distinguished professor of biochemistry and molecular biology at UMass Amherst and one of the paper's co-authors, "is the discovery that glycans act as a code for protein folding in the ER.
The discovery of the role that UGGT plays opens the door to future advancement in understanding and eventually treating the hundreds of diseases that result from misfolded proteins."
https://phys.org/news/2023-12-cellular-code-protein-therapeutic-avenues.html
-
Serious diseases—ranging from emphysema and cystic fibrosis to Alzheimer's disease—can result when the 🔹cellular oversight of protein folding goes awry🔹.
Identifying the glyco-code responsible for high-fidelity folding and quality control could be a promising way for drug therapies to target many diseases.
Scientists once thought that the single code governing life was #DNA, and that everything was governed by how DNA's four building blocks—A, C, G and T—combined and recombined.
But in recent decades, it has become clear that there are other codes at work, and especially in building the intricately folded, secreted proteins that are created in 🔸the human cell's protein factory, the "endoplasmic reticulum" (ER)🔸, a membrane-enclosed compartment where protein folding begins.
Approximately 7,000 different proteins—one-third of all the proteins in the human body—mature in the ER.
The secreted proteins—collectively known as the "#secretome"—are responsible for everything from our body's enzymes to its immune and digestive systems and must be formed correctly for the human body to function normally.Special molecules called "#chaperones," help fold the protein into its final shape.
They also help to identify proteins that haven't folded quite correctly, lending them additional help in refolding, or, if they're hopelessly misfolded, targeting them for destruction before they cause damage.
However, the chaperone system itself, which comprises a part of the cell's quality control department, sometimes fails, and when it does, the results can be catastrophic for our health.
The discovery of the carbohydrate-based chaperone system in the ER was due to the pioneering work that 👉Daniel Hebert, professor of biochemistry and molecular biology at UMass Amherst and one of the paper's senior authors, initiated as a postdoctoral fellow in the 1990s.
"The tools we have now, including glycoproteomics and mass spectrometry at UMass Amherst's Institute for Applied Life Sciences, are allowing us to answer questions that have remained open for over 25 years," says Hebert. "The lead author of this new paper, 👉Kevin Guay, is doing things I could only dream of when I first started."
Among the most pressing of these unanswered questions is: ♦️how do chaperones know when 7,000 different origami-like proteins are correctly folded?♦️
We know now that the answer involves an "ER gatekeeper" enzyme known as #UGGT, and a host of carbohydrate tags, called "N-glycans", which are linked to specific sites in the protein's amino acid sequence.Guay, who is completing his Ph.D. in the molecular cellular biology program at UMass Amherst, focused on two specific mammalian proteins, known as "alpha-1 antitrypsin" and "antithrombin".
⭐️Using CRISPR-edited cells, he and his co-authors modified the ER chaperone network to determine how the presence and location of N-glycans affected protein folding.
They watched as the disease variants were recognized by the ER gatekeeper UGGT and, in order to peer more closely, developed a number of innovative glycoproteomics techniques using mass spectrometry to understand what happens to the glycans that stud the surface of the proteins.
What they discovered is that ⚠️the enzyme UGGT "tags" misfolded proteins with sugars placed in specific positions. ⚠️
It's a sort of code that the chaperones can then read to determine exactly where the folding process went wrong and how to fix it.
"This is the first time that we've been able to see where UGGT puts sugars on proteins made in human cells for quality control," says Guay.
"We now have a platform for extending our understanding of how sugar tags can send proteins for further quality control steps and our work suggests that UGGT is a promising avenue for targeted drug therapy research."
"What's so exciting about this research," says👉 Lila Gierasch, distinguished professor of biochemistry and molecular biology at UMass Amherst and one of the paper's co-authors, "is the discovery that glycans act as a code for protein folding in the ER.
The discovery of the role that UGGT plays opens the door to future advancement in understanding and eventually treating the hundreds of diseases that result from misfolded proteins."
https://phys.org/news/2023-12-cellular-code-protein-therapeutic-avenues.html
-
Serious diseases—ranging from emphysema and cystic fibrosis to Alzheimer's disease—can result when the 🔹cellular oversight of protein folding goes awry🔹.
Identifying the glyco-code responsible for high-fidelity folding and quality control could be a promising way for drug therapies to target many diseases.
Scientists once thought that the single code governing life was #DNA, and that everything was governed by how DNA's four building blocks—A, C, G and T—combined and recombined.
But in recent decades, it has become clear that there are other codes at work, and especially in building the intricately folded, secreted proteins that are created in 🔸the human cell's protein factory, the "endoplasmic reticulum" (ER)🔸, a membrane-enclosed compartment where protein folding begins.
Approximately 7,000 different proteins—one-third of all the proteins in the human body—mature in the ER.
The secreted proteins—collectively known as the "#secretome"—are responsible for everything from our body's enzymes to its immune and digestive systems and must be formed correctly for the human body to function normally.Special molecules called "#chaperones," help fold the protein into its final shape.
They also help to identify proteins that haven't folded quite correctly, lending them additional help in refolding, or, if they're hopelessly misfolded, targeting them for destruction before they cause damage.
However, the chaperone system itself, which comprises a part of the cell's quality control department, sometimes fails, and when it does, the results can be catastrophic for our health.
The discovery of the carbohydrate-based chaperone system in the ER was due to the pioneering work that 👉Daniel Hebert, professor of biochemistry and molecular biology at UMass Amherst and one of the paper's senior authors, initiated as a postdoctoral fellow in the 1990s.
"The tools we have now, including glycoproteomics and mass spectrometry at UMass Amherst's Institute for Applied Life Sciences, are allowing us to answer questions that have remained open for over 25 years," says Hebert. "The lead author of this new paper, 👉Kevin Guay, is doing things I could only dream of when I first started."
Among the most pressing of these unanswered questions is: ♦️how do chaperones know when 7,000 different origami-like proteins are correctly folded?♦️
We know now that the answer involves an "ER gatekeeper" enzyme known as #UGGT, and a host of carbohydrate tags, called "N-glycans", which are linked to specific sites in the protein's amino acid sequence.Guay, who is completing his Ph.D. in the molecular cellular biology program at UMass Amherst, focused on two specific mammalian proteins, known as "alpha-1 antitrypsin" and "antithrombin".
⭐️Using CRISPR-edited cells, he and his co-authors modified the ER chaperone network to determine how the presence and location of N-glycans affected protein folding.
They watched as the disease variants were recognized by the ER gatekeeper UGGT and, in order to peer more closely, developed a number of innovative glycoproteomics techniques using mass spectrometry to understand what happens to the glycans that stud the surface of the proteins.
What they discovered is that ⚠️the enzyme UGGT "tags" misfolded proteins with sugars placed in specific positions. ⚠️
It's a sort of code that the chaperones can then read to determine exactly where the folding process went wrong and how to fix it.
"This is the first time that we've been able to see where UGGT puts sugars on proteins made in human cells for quality control," says Guay.
"We now have a platform for extending our understanding of how sugar tags can send proteins for further quality control steps and our work suggests that UGGT is a promising avenue for targeted drug therapy research."
"What's so exciting about this research," says👉 Lila Gierasch, distinguished professor of biochemistry and molecular biology at UMass Amherst and one of the paper's co-authors, "is the discovery that glycans act as a code for protein folding in the ER.
The discovery of the role that UGGT plays opens the door to future advancement in understanding and eventually treating the hundreds of diseases that result from misfolded proteins."
https://phys.org/news/2023-12-cellular-code-protein-therapeutic-avenues.html
-
Serious diseases—ranging from emphysema and cystic fibrosis to Alzheimer's disease—can result when the 🔹cellular oversight of protein folding goes awry🔹.
Identifying the glyco-code responsible for high-fidelity folding and quality control could be a promising way for drug therapies to target many diseases.
Scientists once thought that the single code governing life was #DNA, and that everything was governed by how DNA's four building blocks—A, C, G and T—combined and recombined.
But in recent decades, it has become clear that there are other codes at work, and especially in building the intricately folded, secreted proteins that are created in 🔸the human cell's protein factory, the "endoplasmic reticulum" (ER)🔸, a membrane-enclosed compartment where protein folding begins.
Approximately 7,000 different proteins—one-third of all the proteins in the human body—mature in the ER.
The secreted proteins—collectively known as the "#secretome"—are responsible for everything from our body's enzymes to its immune and digestive systems and must be formed correctly for the human body to function normally.Special molecules called "#chaperones," help fold the protein into its final shape.
They also help to identify proteins that haven't folded quite correctly, lending them additional help in refolding, or, if they're hopelessly misfolded, targeting them for destruction before they cause damage.
However, the chaperone system itself, which comprises a part of the cell's quality control department, sometimes fails, and when it does, the results can be catastrophic for our health.
The discovery of the carbohydrate-based chaperone system in the ER was due to the pioneering work that 👉Daniel Hebert, professor of biochemistry and molecular biology at UMass Amherst and one of the paper's senior authors, initiated as a postdoctoral fellow in the 1990s.
"The tools we have now, including glycoproteomics and mass spectrometry at UMass Amherst's Institute for Applied Life Sciences, are allowing us to answer questions that have remained open for over 25 years," says Hebert. "The lead author of this new paper, 👉Kevin Guay, is doing things I could only dream of when I first started."
Among the most pressing of these unanswered questions is: ♦️how do chaperones know when 7,000 different origami-like proteins are correctly folded?♦️
We know now that the answer involves an "ER gatekeeper" enzyme known as #UGGT, and a host of carbohydrate tags, called "N-glycans", which are linked to specific sites in the protein's amino acid sequence.Guay, who is completing his Ph.D. in the molecular cellular biology program at UMass Amherst, focused on two specific mammalian proteins, known as "alpha-1 antitrypsin" and "antithrombin".
⭐️Using CRISPR-edited cells, he and his co-authors modified the ER chaperone network to determine how the presence and location of N-glycans affected protein folding.
They watched as the disease variants were recognized by the ER gatekeeper UGGT and, in order to peer more closely, developed a number of innovative glycoproteomics techniques using mass spectrometry to understand what happens to the glycans that stud the surface of the proteins.
What they discovered is that ⚠️the enzyme UGGT "tags" misfolded proteins with sugars placed in specific positions. ⚠️
It's a sort of code that the chaperones can then read to determine exactly where the folding process went wrong and how to fix it.
"This is the first time that we've been able to see where UGGT puts sugars on proteins made in human cells for quality control," says Guay.
"We now have a platform for extending our understanding of how sugar tags can send proteins for further quality control steps and our work suggests that UGGT is a promising avenue for targeted drug therapy research."
"What's so exciting about this research," says👉 Lila Gierasch, distinguished professor of biochemistry and molecular biology at UMass Amherst and one of the paper's co-authors, "is the discovery that glycans act as a code for protein folding in the ER.
The discovery of the role that UGGT plays opens the door to future advancement in understanding and eventually treating the hundreds of diseases that result from misfolded proteins."
https://phys.org/news/2023-12-cellular-code-protein-therapeutic-avenues.html
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New Section Editor @glycojones comments on the involvement of undergraduate students in a recent @ActaCrystF paper and encourages submissions from young researchers @iucr #StructuralGenomics #InorganicPyrophosphatases #Legionella https://doi.org/10.1107/S2053230X2300883X
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Apple seeds contain a cyanogenic glycoside called amygdalin, which breaks down into cyanide.
However a person weighing 60kgs would need to eat 25 whole apples including seeds in one sitting to feel any toxic effects.
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Apple seeds contain a cyanogenic glycoside called amygdalin, which breaks down into cyanide.
However a person weighing 60kgs would need to eat 25 whole apples including seeds in one sitting to feel any toxic effects.
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We explored the question, from which different areas of chemistry, including glycochemistry, peptide chemistry, materials chemistry and synthetic method development new electrophiles for covalent inhibitors can originate in order to keep expanding the druggable space. (2/2)
#Chemistry #ChemBio #ChemicalProteomics #ChemPro #ProteoProbes #DrugDiscovery #Glycotime #Peptides #Materials #Synthesis #Undruggable #CovalentInhibitors
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We explored the question, from which different areas of chemistry, including glycochemistry, peptide chemistry, materials chemistry and synthetic method development new electrophiles for covalent inhibitors can originate in order to keep expanding the druggable space. (2/2)
#Chemistry #ChemBio #ChemicalProteomics #ChemPro #ProteoProbes #DrugDiscovery #Glycotime #Peptides #Materials #Synthesis #Undruggable #CovalentInhibitors
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We explored the question, from which different areas of chemistry, including glycochemistry, peptide chemistry, materials chemistry and synthetic method development new electrophiles for covalent inhibitors can originate in order to keep expanding the druggable space. (2/2)
#Chemistry #ChemBio #ChemicalProteomics #ChemPro #ProteoProbes #DrugDiscovery #Glycotime #Peptides #Materials #Synthesis #Undruggable #CovalentInhibitors
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We explored the question, from which different areas of chemistry, including glycochemistry, peptide chemistry, materials chemistry and synthetic method development new electrophiles for covalent inhibitors can originate in order to keep expanding the druggable space. (2/2)
#Chemistry #ChemBio #ChemicalProteomics #ChemPro #ProteoProbes #DrugDiscovery #Glycotime #Peptides #Materials #Synthesis #Undruggable #CovalentInhibitors
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Jeroen Codee speaks at the #Reedijk Symposium: "A new twist in the tale - stereoselective glycosylation reactions for bacterial glycan assembly". Exciting insights into the importance of advanced glycosylation chemistries to make complex glycosides to better understand (bacterial) biology.
#ChemBio #Chemistry #Glycotime -
Jeroen Codee speaks at the #Reedijk Symposium: "A new twist in the tale - stereoselective glycosylation reactions for bacterial glycan assembly". Exciting insights into the importance of advanced glycosylation chemistries to make complex glycosides to better understand (bacterial) biology.
#ChemBio #Chemistry #Glycotime -
Jeroen Codee speaks at the #Reedijk Symposium: "A new twist in the tale - stereoselective glycosylation reactions for bacterial glycan assembly". Exciting insights into the importance of advanced glycosylation chemistries to make complex glycosides to better understand (bacterial) biology.
#ChemBio #Chemistry #Glycotime -
New fluorescence method lights up a better glycan-cleaving enzyme
Attached to many proteins are glycans—complex strings of sugars—that change how the whole unit functions. Removing them…
#NewsBeep #News #Science #CA #Canada #directedevolution #enzymes #glycomics #glycoproteins #glycosidehydrolase #MassSpectrometry #mucin-type #n-glycans #o-glycans #Proteomics #sialylT-antigen #structuralbiology #Tools
https://www.newsbeep.com/ca/164551/ -
#Fukushima #TEPCO
#汚染水の海洋放出に反対します
#日本政府は汚染水放出を中止せよ
#StopFukushimaWaterReleaseNow
#StopReleasingTEPCOWater
#fukushimanuclearwastewater
#FukushimaWater
【 The serious findings on the decomposition glycosides bonds of chitin & chitosan by ionizing radiation proves the ocean is not right place for discharge of #Fukushima radionuclides, as it can irreversibly destroy marine food chain & kill animals, fishes, whales, including humans. 】
↑
https://x.com/duabusan/status/1702141762100187619?s=12 -
#Fukushima #TEPCO
#汚染水の海洋放出に反対します
#日本政府は汚染水放出を中止せよ
#StopFukushimaWaterReleaseNow
#StopReleasingTEPCOWater
#fukushimanuclearwastewater
#FukushimaWater
【 The serious findings on the decomposition glycosides bonds of chitin & chitosan by ionizing radiation proves the ocean is not right place for discharge of #Fukushima radionuclides, as it can irreversibly destroy marine food chain & kill animals, fishes, whales, including humans. 】
↑
https://x.com/duabusan/status/1702141762100187619?s=12