cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.1279394.v294
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While <i>O</i>-linked GalNAc-glycosylated structures do not occur in plants, the germline encoding of an anti-A-reactive immunoglobulin M (IgM) molecule that is complementary to mammalian <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, was experimentally documented in C57BL/10 mice. This anti-A antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, appears serologically identical to the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc-glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity.
DOI: 10.6084/m9.figshare.1265143.v1
title: CMG webpage figures

description: Figures from my computational modelling group page relating to MHC class I antigen processing.
DOI: 10.6084/m9.figshare.1265127.v1
title: UFSRATPaperDUDEAnalysis

description: Raw data from running USR, UFSRAT and ECFP4 on the DUD-E dataset
DOI: 10.6084/m9.figshare.1265143.v3
title: CMG webpage figures

description: Figures from my computational modelling group page relating to MHC class I antigen processing.
DOI: 10.6084/m9.figshare.1265143.v2
title: CMG webpage figures

description: Figures from my computational modelling group page relating to MHC class I antigen processing.
DOI: 10.6084/m9.figshare.1279394.v295
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While <i>O</i>-linked GalNAc glycans neither do occur in higher order plants nor in bacteria, the <i>O</i>-GalNAc glycan-bearing, ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to their non-immune anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, appears serologically identical to the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity.
DOI: 10.6084/m9.figshare.1279394.v296
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While <i>O</i>-linked GalNAc glycans do not occur in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to their non-immune anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, appears serologically identical to the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity.
DOI: 10.6084/m9.figshare.1279394.v297
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: <br> While <i>O</i>-linked GalNAc glycans are not found in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, appears serologically identical to the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity.
DOI: 10.6084/m9.figshare.1279394.v298
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While blood group A- or A-like specificities are not found in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, appears serologically identical to the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity. <br>
DOI: 10.6084/m9.figshare.1279394.v299
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While native GalNAc-determined blood group A- or A-like specificities are not found in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, appears serologically identical to the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity. <br>
DOI: 10.6084/m9.figshare.1265060
title: Open field phenotypes and genotypes (R/qtl csv format)

description: Open field data as well as SNP genotypes from the F8 Red Junglefowl x White Leghorn intercross. Behavioural variables are residuals after adjusting for sex, batch and body weight at 42 days.
DOI: 10.6084/m9.figshare.1265056
title: Data Archive: Social integration confers thermal benefits in a gregarious primate. Journal of Animal Ecology.

description: Data Archive: Social integration confers thermal benefits in a gregarious primate. Journal of Animal Ecology.
DOI: 10.6084/m9.figshare.1265060.v1
title: Open field phenotypes and genotypes (R/qtl csv format)

description: Open field data as well as SNP genotypes from the F8 Red Junglefowl x White Leghorn intercross. Behavioural variables are residuals after adjusting for sex, batch and body weight at 42 days.
DOI: 10.6084/m9.figshare.1279394.v300
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While native GalNAc-determined blood group A- or A-like specificities are not found in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A "auto" antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, serologically reacts like the human innate anti-A isoagglutinin. The target of this antibody is a trans-species developmental antigen that signifies malignancy when accumulating in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity. <br>
DOI: 10.6084/m9.figshare.1265056.v1
title: Data Archive: Social integration confers thermal benefits in a gregarious primate. Journal of Animal Ecology.

description: Data Archive: Social integration confers thermal benefits in a gregarious primate. Journal of Animal Ecology.
DOI: 10.6084/m9.figshare.1265054
title: PRIMED and GRS

description: GRS: python code PRIMED: database of primers for S. pombe and S. cerevisiae
DOI: 10.6084/m9.figshare.1265054.v2
title: PRIMED and GRS

description: GRS: python code PRIMED: database of primers for S. pombe and S. cerevisiae
DOI: 10.6084/m9.figshare.1279394.v301
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While native GalNAc-determined blood group A- or A-like specificities are not found in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A “auto” antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, serologically reacts like the human innate anti-A isoagglutinin because the target is a common trans-species developmental antigen that signifies malignancy when accumulated in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity.
DOI: 10.6084/m9.figshare.1265047
title: Clinical data on the effect of L-arginine supplementation on cardiovascular risk factors in healthy men

description: Data were collected from 52 healthy male sports club members (aged 18-35) at the Isfahan University Medical Sciences, Ishfan Iran. This was a double blind randomized controlled study where the intervention group were given 2000 mg L-arginine per day and the placebo group were given 2000mg maltodextrin per day over 45 days (November-December 2013). Please see associated article for more detailed methods.
DOI: 10.6084/m9.figshare.1265054.v1
title: PRIMED and GRS

description: GRS: python code PRIMED: database of primers for S. pombe and S. cerevisiae
DOI: 10.6084/m9.figshare.1265024
title: Genome SC Y55

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265023
title: Genome SC W303

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265024.v1
title: Genome SC Y55

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265022
title: Genome SC SK1

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265047.v1
title: Clinical data on the effect of L-arginine supplementation on cardiovascular risk factors in healthy men

description: Data were collected from 52 healthy male sports club members (aged 18-35) at the Isfahan University Medical Sciences, Ishfan Iran. This was a double blind randomized controlled study where the intervention group were given 2000 mg L-arginine per day and the placebo group were given 2000mg maltodextrin per day over 45 days (November-December 2013). Please see associated article for more detailed methods.
DOI: 10.6084/m9.figshare.1279394.v302
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While mucin-type <i>O</i>-GalNAc glycosylations and native blood A-like specificities are not known to occur in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids that were discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM). This anti-A “auto” antibody, which does not appear in animals subjected to an ovariectomy prior to the onset of puberty, serologically reacts like the human innate anti-A isoagglutinin because the target is a common trans-species developmental antigen that signifies malignancy when accumulated in non-developmental tissues. In mouse and man, this antibody molecule most likely gets its complementary footprints from the early growth-dependent, trans-species <i>O</i>-GalNAc glycosylation of proteins and subsequent GalNAc transferase depletion that completes the cell differentiation processes and results in release of complementary protein(s) involving the secretory IgM, which might establish this mechanism through expression of germline-specific serine residues and reveals the structure of the volatilely expressed, “lost” glycan. These early or first <i>O</i>-GalNAc glycosylations of proteins appear metabolically related to those of the mucin-type, “aberrant” monosaccharide GalNAcα1-<i>O</i>-Ser/Thr-R or Tn antigen and explain the anti-Tn cross-reactivity of anti-A-specific immunoglobulins and pronounced occurrence of cross-reactive anti-Tn antibody in the plasma of human histo (blood) group O. In fact, in the human blood group O, an A-allelic, phenotype-specific GalNAc glycosylation of plasma proteins does not occur and affect the levels of the anti-Tn antibody, which may function as a growth regulator that depending on its levels, initiates the process of growth inhibition through enzyme-substrate competition with subsequent trans-species <i>O</i>-GalNAc-glycosylations and mediates autologous cellular cytotoxicity.
DOI: 10.6084/m9.figshare.1265021
title: Genome SC S288C

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265020
title: Genome SC RM11_1A

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265018
title: PRIMED: S. cerevisiae RM11

description: Table S3
DOI: 10.6084/m9.figshare.1265019
title: Genome S. pombe

description: Sequence and annotation
DOI: 10.6084/m9.figshare.1265020.v1
title: Genome SC RM11_1A

description: Sequence and annotation