beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis (Q24597379)

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O Oda

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R Inagi

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Y Iida

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N Araki

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N Yamada

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S Horiuchi

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N Taniguchi

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K Maeda

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T Kinoshita

Journal of Clinical Investigation

10

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language of work or name

English

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publication date

September 1993

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published in

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volume

92

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page(s)

1243-52

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issue

3

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cites work

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Advanced glycosylation end products in patients with diabetic nephropathy

30 May 2018

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Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging.

30 May 2018

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Detection of novel beta 2-microglobulin in the serum of hemodialysis patients and its amyloidogenic predisposition

30 May 2018

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12 December 2020

Purification and complete amino acid sequence of novel beta 2-microglobulin

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12 December 2020

Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure

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12 December 2020

Hemoglobin-AGE: a circulating marker of advanced glycosylation

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12 December 2020

Partial characterization of circulating macromolecular beta 2-microglobulin complexes by density gradient ultracentrifugation and page-blotting

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12 December 2020

A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin

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12 December 2020

Histochemical and immunohistochemical characterization of amyloid associated with chronic hemodialysis as beta 2-microglobulin

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12 December 2020

Tumour necrosis factor α stimulates resorption and inhibits synthesis of proteoglycan in cartilage

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12 December 2020

Beta 2-microglobulin: a new form of amyloid protein associated with chronic hemodialysis

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12 December 2020

Detection of D-glucose-derived pyrrole compounds during Maillard reaction under physiological conditions

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12 December 2020

Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling

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12 December 2020