نتایج جستجو برای: carbamylation

تعداد نتایج: 238  

Journal: :The Yale Journal of Biology and Medicine 1974
O. Castro J. Orlin S. C. Finch

The in vitro incubation of human sickle cell erythrocytes (SS RBCs) with sodium cyanate results in significant prolongation of their 'Cr intravascular survival (1, 2). This effect appears to be mediated through carbamylation of the amino terminal valine residue in the hemoglobin S molecule which results in inhibition of erythrocyte sickling (3). Initial clinical studies have shown that the oral...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
Boguslaw Stec

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in carbon fixation and the most abundant protein on earth. It has been studied extensively by biochemical and structural methods; however, the most essential activation step has not yet been described. Here, we describe the mechanistic details of Lys carbamylation that leads to RuBisCO activation by atmospheric CO(2)....

Journal: :Journal of experimental botany 2008
Robert L Houtz Roberta Magnani Nihar R Nayak Lynnette M A Dirk

Both the large (LS) and small (SS) subunits of Rubisco are subject to a plethora of co- and post-translational modifications. With the exceptions of LS carbamylation and SS transit sequence processing, the remaining modifications, including deformylation, acetylation, methylation, and N-terminal proteolytic processing of the LS, are still biochemically and/or functionally undefined although the...

Journal: :Current opinion in rheumatology 2014
Lars Klareskog Khaled Amara Vivianne Malmström

PURPOSE OF REVIEW To describe recent progress concerning rheumatoid arthritis (RA)-associated autoantibodies, in particular antibodies to citrullinated proteins antigens. RECENT FINDINGS An increasingly diverse and RA-associated repertoire of antibodies has been defined over the last few years. These antibodies are preferentially, but not exclusively, reactive with posttranslationally modifie...

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