Lista de obras - Lawrence A. Tabak - Dominio Público Uruguay

A molecular switch orchestrates enzyme specificity and secretory granule morphology

scientific article published in Nature Communications

All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

artículo científico publicado en 2002

An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues

artículo científico publicado en 2004

An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues

article published in 2008

Basic science: Bedrock of progress

artículo científico publicado en 2016

Biomedical research: strength from diversity

artículo científico publicado en 2013

Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos.

artículo científico publicado en 2017

Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling

artículo científico publicado en 2004

Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences

scientific article published on 15 July 2020

Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2

artículo científico publicado en 2006

Emerging Paradigms for the Initiation of Mucin-type Protein O-Glycosylation by the Polypeptide GalNAc Transferase Family of Glycosyltransferases ⬇️

artículo científico publicado el 24 de febrero de 2011

Erratum: UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases: completion of the family tree

artículo científico publicado en 2015

Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family

artículo científico publicado en 2003

Galnt1 is required for normal heart valve development and cardiac function

artículo científico publicado en 2015

Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding

artículo científico publicado en 2019

Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2

artículo científico publicado en 2009

Improved online LC-MS/MS identification of O-glycosites by EThcD fragmentation, chemoenzymatic reaction, and SPE enrichment

artículo científico publicado en 2020

Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1.

artículo científico publicado en 2009

Members of the GalNAc-T family of enzymes utilize distinct Golgi localization mechanisms

scientific article published on 01 November 2018

Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.

artículo científico publicado en 2015

NIH Roadmap interdisciplinary research initiatives

artículo científico publicado en 2005

Opinion: The Next Generation Researchers Initiative at NIH.

artículo científico publicado en 2017

Precision Health: Bringing Oral Health into the Context of Overall Health

artículo científico publicado en 2019

Research funding. A framework for decisions about research with HPAI H5N1 viruses

artículo científico publicado en 2013

Response

Response to: "Rescuing the NIH before it is too late".

artículo científico publicado en 2006

Small molecule inhibitors of mucin-type O-linked glycosylation from a uridine-based library

artículo científico publicado en 2004

Sociology. Weaving a richer tapestry in biomedical science

artículo científico publicado en 2011

The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation.

artículo científico publicado en 2017

The Partnership for Accelerating Cancer Therapies

The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection

artículo científico publicado en 2008

The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation

artículo científico publicado en 2013

UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree

artículo científico publicado en 2011

Lista de obras de Lawrence A. Tabak

A molecular switch orchestrates enzyme specificity and secretory granule morphology

All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues

An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues

Basic science: Bedrock of progress

Biomedical research: strength from diversity

Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos.

Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling

Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences

Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2

Emerging Paradigms for the Initiation of Mucin-type Protein O-Glycosylation by the Polypeptide GalNAc Transferase Family of Glycosyltransferases ⬇️

Erratum: UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases: completion of the family tree

Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family

Galnt1 is required for normal heart valve development and cardiac function

Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding

Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2

Improved online LC-MS/MS identification of O-glycosites by EThcD fragmentation, chemoenzymatic reaction, and SPE enrichment

Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1.

Members of the GalNAc-T family of enzymes utilize distinct Golgi localization mechanisms

Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.

NIH Roadmap interdisciplinary research initiatives

Opinion: The Next Generation Researchers Initiative at NIH.

Precision Health: Bringing Oral Health into the Context of Overall Health

Research funding. A framework for decisions about research with HPAI H5N1 viruses

Response

Response to: "Rescuing the NIH before it is too late".

Small molecule inhibitors of mucin-type O-linked glycosylation from a uridine-based library

Sociology. Weaving a richer tapestry in biomedical science

The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation.

The Partnership for Accelerating Cancer Therapies

The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection

The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation

UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree