cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.1279394.v303
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While the mucin-type <i>O</i>-GalNAc glycosylation and a native blood A-like specificity have not been discovered in any bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, 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 common target is a 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.1265017
title: PRIMED: S. cerevisiae S288C

description: Table S2
DOI: 10.6084/m9.figshare.1279394.v304
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While the mucin-type <i>O</i>-GalNAc glycosylation and a native blood A-like specificity have not yet been identified in bacteria, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, 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, shows the same serological reaction pattern as the human innate or non-immune anti-A isoagglutinin. 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.1265018.v2
title: PRIMED: S. cerevisiae RM11

description: Table S3
DOI: 10.6084/m9.figshare.1265016
title: PRIMED: S. cerevisiae SK1

description: Table S4
DOI: 10.6084/m9.figshare.1265018.v1
title: PRIMED: S. cerevisiae RM11

description: Table S4
DOI: 10.6084/m9.figshare.1265016.v2
title: PRIMED: S. cerevisiae SK1

description: Table S4
DOI: 10.6084/m9.figshare.1279394.v305
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While a native n-acetyl-d-galactosamine (D-GalNAc) - dermined blood group A-like specificity has not yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This anti-A “auto” antibody shows the same serological reaction pattern as the human innate or non-immune anti-A isoagglutinin. 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.1265015
title: PRIMED: S. cerevisiae W303

description: Table S5
DOI: 10.6084/m9.figshare.1265016.v1
title: PRIMED: S. cerevisiae SK1

description: Table S5
DOI: 10.6084/m9.figshare.1265014
title: PRIMES: S. cerevisiae Y55

description: Table S6
DOI: 10.6084/m9.figshare.1265017.v1
title: PRIMED: S. cerevisiae S288C

description: Table S2
DOI: 10.6084/m9.figshare.1265017.v3
title: PRIMED: S. cerevisiae S288C

description: Table S2
DOI: 10.6084/m9.figshare.1279394.v306
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While neither <i>O</i>-linked nor <i>N</i>-linked Acetyl-D-galactosamine (D-GalNAc)-determined, native blood group A-like specificities have yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This anti-A “auto” antibody shows the same serological reaction pattern as the human innate or non-immune anti-A isoagglutinin. 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.1265015.v1
title: PRIMED: S. cerevisiae W303

description: Table S3
DOI: 10.6084/m9.figshare.1265017.v2
title: PRIMED: S. cerevisiae S288C

description: Table S2
DOI: 10.6084/m9.figshare.1265013
title: PRIMED: S. pombe

description: Table S1
DOI: 10.6084/m9.figshare.1279394.v307
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While neither <i>O</i>-linked nor <i>N</i>-linked Acetyl-D-galactosamine (D-GalNAc)-determined, native blood group A-like specificities have yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This anti-A “auto” antibody shows the same serological reaction pattern as the human innate or non-immune anti-A isoagglutinin. 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.1265014.v1
title: PRIMES: S. cerevisiae Y55

description: Table S6
DOI: 10.6084/m9.figshare.1265009
title: Contact forces in several TKA designs during squatting: A numerical sensitivity analysis

description: Maximum contact tibio-femoral contact forces for different TKA designs under mal-alignment configurations under a squat task.
DOI: 10.6084/m9.figshare.1265013.v1
title: PRIMED: S. pombe

description: Table S1
DOI: 10.6084/m9.figshare.1265009.v1
title: Contact forces in several TKA designs during squatting: A numerical sensitivity analysis

description: Maximum contact tibio-femoral contact forces for different TKA designs under mal-alignment configurations under a squat task.
DOI: 10.6084/m9.figshare.1265014.v2
title: PRIMES: S. cerevisiae Y55

description: Table S6
DOI: 10.6084/m9.figshare.1279394.v308
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While <i>N</i>-Acetyl-D-galactosamine (D-GalNAc)-determined, native blood group A-like specificities have not yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This murine anti-A “auto” antibody and the human innate or non-immune anti-A isoagglutinin show identical serological reaction patterns. 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.1265013.v3
title: PRIMED: S. pombe

description: Table S1
DOI: 10.6084/m9.figshare.1265006
title: Bladed simulations and harmonic solution for OC3-Hywind turbine with harmonic wind and wave loading

description: Bladed simulations and harmonic linearised solutions of a floating wind turbine with harmonic wind and waves (no control). OC3-Hywind model.
DOI: 10.6084/m9.figshare.1265008
title: Contact forces in several TKA designs during squatting: A numerical sensitivity analysis

description: Maximum contact patellofemoral contact forces for different TKA designs under mal-alignment configurations under a squat task.
DOI: 10.6084/m9.figshare.1279394.v309
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While <i>N</i>-Acetyl-D-galactosamine (D-GalNAc)-determined, native blood group A-like specificities have not yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This murine anti-A “auto” antibody and the human innate or non-immune anti-A isoagglutinin show identical serological reaction patterns. 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.1265008.v1
title: Contact forces in several TKA designs during squatting: A numerical sensitivity analysis

description: Maximum contact patellofemoral contact forces for different TKA designs under mal-alignment configurations under a squat task.
DOI: 10.6084/m9.figshare.1265013.v2
title: PRIMED: S. pombe

description: Table S1
DOI: 10.6084/m9.figshare.1264995
title: Increasing diversity in emerging non-religious communities (data)

description: These four supplementary tables relate to the publication "Hassall, C and Bushfield, I 2014 Increasing Diversity in Emerging Non-religious Communities. Secularism and Nonreligion".
DOI: 10.6084/m9.figshare.1279394.v310
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While as a source of the human anti-A/B isoagglutinin production neither <i>N</i>- nor <i>O</i>-linked <i>N</i>-acetyl-D-galactosamine (D-GalNAc)-determined, native blood group A-like specificities have yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This murine anti-A “auto” antibody and the human innate or non-immune anti-A isoagglutinin show identical serological reaction patterns. 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.1264993
title: Linearised response with harmonic wind and waves (no control)

description: Linearised response of a floating wind turbine with harmonic wind and waves (no control). OC3-Hywind model.
DOI: 10.6084/m9.figshare.1264994
title: Bladed simulations with harmonic wind and waves (no control)

description: Bladed simulations of a floating wind turbine with harmonic wind and waves (no control). OC3-Hywind model.
DOI: 10.6084/m9.figshare.1264995.v1
title: Increasing diversity in emerging non-religious communities (data)

description: These four supplementary tables relate to the publication "Hassall, C and Bushfield, I 2014 Increasing Diversity in Emerging Non-religious Communities. Secularism and Nonreligion".
DOI: 10.6084/m9.figshare.1264951
title: Tables for Social context of the Old Kingdom copper model tools

description: Supplemental tables for an article in the journal World Archaeology "Social context of the Old Kingdom copper model tools"
DOI: 10.6084/m9.figshare.1264994.v1
title: Bladed simulations with harmonic wind and waves (no control)

description: Bladed simulations of a floating wind turbine with harmonic wind and waves (no control). OC3-Hywind model.
DOI: 10.6084/m9.figshare.1264930
title: Sub3_EEG_raw_set4_data.mat

description: This is a subset data for instructed truth-telling condition in the WE(with prior-experience) task.
DOI: 10.6084/m9.figshare.1264951.v1
title: Tables for Social context of the Old Kingdom copper model tools

description: Supplemental tables for an article in the journal World Archaeology "Social context of the Old Kingdom copper model tools"
DOI: 10.6084/m9.figshare.1264919
title: Temperature response curves of photosynthesis (and underlying biochemistry) over 3 seasons in Eucalyptus globulus grown in a factorial design of elevated CO2 and warming.

description: Gas exchange data from Crous et al. 2013 in Global Change Biology including CO2 response curves at 5 temperature and quantification of Rlight using the Laisk method at 4 different temperatures.<br>There are 3 files including in this dataset, 1 raw data file<br>(name: WTC_Temp&CO2_CM_GX-AciTemp_20101202-20110908_R)<br>and 2 processed files including fits to the classic photosynthesis model and, Rlight and gamma* data.<br>Names:<br>(WTC_Temp&CO2_CM_GX-AciFits_20101202-20110908_L2 and WTC_Temp&CO2_CM_GX-Rlight_20110311-20110318_L2).
DOI: 10.6084/m9.figshare.1264930.v1
title: Sub3_EEG_raw_set4_data.mat

description: This is a subset data for instructed truth-telling condition in the WE(with prior-experience) task.
DOI: 10.6084/m9.figshare.1279394.v311
title: Germline encoded anti-A-reactive IgM arising from growth-dependent and aberrant O-GalNAc glycosylations.*

description: While as a source of the human anti-A/B isoagglutinin production neither <i>N</i>- nor <i>O</i>-linked <i>N</i>-acetyl-D-galactosamine (D-GalNAc)-determined, native blood group A-like specificities have yet been demonstrated in prokaryotic microorganisms, the <i>O</i>-GalNAc glycan-bearing ovarian glycolipids, discovered in C57BL/10 mice, are complementary to the syngeneic anti-A-reactive, secretory immunoglobulin M (IgM), which does not appear in animals subjected to an ovariectomy prior to the onset of puberty. This murine anti-A “auto” antibody and the human innate or non-immune anti-A isoagglutinin show identical serological reaction patterns. 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.