scholarly journals In vivo acetylation identified at lysine 70 of human lens αA-crystallin

1998 ◽  
Vol 7 (6) ◽  
pp. 1451-1457 ◽  
Author(s):  
Peiping P. Lin ◽  
Richard C. Barry ◽  
David L. Smith ◽  
Jean B. Smith
Keyword(s):  
Human Lens

scholarly journals In vivo carbamylation and acetylation of water-soluble human lens αB-crystallin lysine 92

2001 ◽  
Vol 10 (6) ◽  
pp. 1130-1136 ◽  
Author(s):  
Veniamin N. Lapko ◽  
David L. Smith ◽  
Jean B. Smith
Keyword(s):  
Water Soluble ◽  
Human Lens ◽  
Αb Crystallin

Assigning in vivo carbamylation and acetylation in human lens proteins using tandem mass spectrometry and database searching

2007 ◽  
Vol 259 (1-3) ◽  
pp. 161-173 ◽  
Author(s):  
Zee-Yong Park ◽  
Rovshan Sadygov ◽  
Judy M. Clark ◽  
John I. Clark ◽  
John R. Yates
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Human Lens ◽  
Database Searching ◽  
Tandem Mass ◽  
Lens Proteins

In Vivo Measurements On Human Lens Using Quasielastic Light Scattering

1987 ◽  
Author(s):  
Peter C. Magnante ◽  
Leo T. Chylack ◽  
George B. Benedek ◽  
Teodosio Libondi ◽  
Stephen N. Joffe ◽  
...  
Keyword(s):  
Light Scattering ◽  
Human Lens ◽  
Quasielastic Light Scattering ◽  
In Vivo Measurements

scholarly journals In Vivo Quasi-Elastic Light Scattering Eye Scanner Detects Molecular Aging in Humans

2020 ◽  
Vol 75 (9) ◽  
pp. e53-e62
Author(s):  
Olga Minaeva ◽  
Srikant Sarangi ◽  
Danielle M Ledoux ◽  
Juliet A Moncaster ◽  
Douglas S Parsons ◽  
...  
Keyword(s):  
Light Scattering ◽  
Human Lens ◽  
Fetal Life ◽  
Healthy Human ◽  
Elastic Light Scattering ◽  
Lens Proteins ◽  
Age Dependent ◽  
Molecular Aging

Abstract The absence of clinical tools to evaluate individual variation in the pace of aging represents a major impediment to understanding aging and maximizing health throughout life. The human lens is an ideal tissue for quantitative assessment of molecular aging in vivo. Long-lived proteins in lens fiber cells are expressed during fetal life, do not undergo turnover, accumulate molecular alterations throughout life, and are optically accessible in vivo. We used quasi-elastic light scattering (QLS) to measure age-dependent signals in lenses of healthy human subjects. Age-dependent QLS signal changes detected in vivo recapitulated time-dependent changes in hydrodynamic radius, protein polydispersity, and supramolecular order of human lens proteins during long-term incubation (~1 year) and in response to sustained oxidation (~2.5 months) in vitro. Our findings demonstrate that QLS analysis of human lens proteins provides a practical technique for noninvasive assessment of molecular aging in vivo.

Age-Related Changes of Human Lens Epithelial Cells in vivo

2001 ◽  
Vol 33 (6) ◽  
pp. 363-366 ◽  
Author(s):  
Hideaki Oharazawa ◽  
Nobuhiro Ibaraki ◽  
Hironori Matsui ◽  
Kunitoshi Ohara
Keyword(s):  
Epithelial Cells ◽  
Human Lens ◽  
Lens Epithelial Cells ◽  
Human Lens Epithelial Cells ◽  
Age Related ◽  
Age Related Changes

In Vivo Modification of the C-Terminal Lysine of Human Lens αB-Crystallin

1997 ◽  
Vol 65 (5) ◽  
pp. 673-680 ◽  
Author(s):  
PEIPING LIN ◽  
DAVID L SMITH ◽  
JEAN B SMITH
Keyword(s):  
Human Lens ◽  
Αb Crystallin

scholarly journals An estimate of the size and shape of the human lens fibre in vivo.

1987 ◽  
Vol 71 (12) ◽  
pp. 916-922 ◽  
Author(s):  
N A Brown ◽  
A J Bron ◽  
J M Sparrow
Keyword(s):  
Human Lens ◽  
Size And Shape ◽  
Lens Fibre
Sign in / Sign up

Export Citation Format

Share Document