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Journal Article
by Bellomo, Rinaldo and McEvoy, Suzanne and Kai Lo, Sing and Myburgh, John and Neal, Bruce and Norton, Robyn and French, Julie and Finfer, Simon and Doig, Gordon and Hayek, Mary and O'Donnell, Sheridan and Bell, Anthony and Boyce, Neil and Blythe, David and Cade, John and Chapman, Marianne and Cole, Louise and Cooper, James and Davies, Andrew and French, Craig and Joyce, Christopher and McArthur, Colin and MacMahon, Stephen and Presneill, Jeffrey and Saul, Peter and Seppelt, Ian and Stephens, Dianne and Turner, Andrew and Williams, Anthony and Woolfe, Clive and Sandercock, Peter and Sprung, Charles and Duncan Young, J and Sivarajasingham, Siva and Francis, Lesley and Woodward, Mark and Charlton, Julie and Harry, Catherine and Higgins, Lisa and Moulden, Katherine and Vallance, Shirley and Chadderton, Janine and Newby, Lynette and Bates, Samantha and Goldsmith, Donna and Voss, Alison and Palermo, Annamaria and Jayne, Kathy and Merai, Mamta and Pandey, Sameer and Schmidt, Manuela and Carroll, Rosemary and McFadyen, Brett and Clarke, Jane and Powell, Juliet and Tai, Judi and Hynesova, Iveta and Weisbrodt, Leonie and Bradley, Lisa and Kelly, Theresa and Limpus, Anthony and Moore, Robyn and Creed, Stephanie and Kaplan, Sandra and Rivett, Justine and Thomas, Jane and Marsden, Kathy and Boyce, Catherine and Howe, Belinda and Robertson, Megan and O'Connor, Anne and Potter, Julie and Ramakrishnan, Naresh and Rajbhandari, Dorrilyn and Girling, Kathryn and Hodgetts, Marie and Jovanovska, Alina and Little, Lorraine and unav and Saline Versus Albumin and SAFE Study Investigators
BMJ, ISSN 0959-8138, 11/2006, Volume 333, Issue 7577, pp. 1044 - 1046
Journal Article
Molecular aspects of medicine, ISSN 0098-2997, 2012, Volume 33, Issue 3, pp. 209 - 290
Human serum albumin (HSA), the most abundant protein in plasma, is a monomeric multi-domain macromolecule, representing the main determinant of plasma oncotic pressure and the main modulator of fluid distribution between body compartments... 
Ligand binding properties | Human serum albumin | Human serum heme–albumin | Biotechnological applications | Biomedical aspects | Allostery | (Pseudo-)enzymatic properties | Genetic variants | Structure | Recombinant human serum albumin | Chemical modifications | Human serum heme-albumin | FAMILIAL DYSALBUMINEMIC HYPERTHYROXINEMIA | MEDICINE, RESEARCH & EXPERIMENTAL | ESTERASE-LIKE ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTALLOGRAPHIC ANALYSIS REVEALS | AMINO-ACID SUBSTITUTIONS | HIGH-AFFINITY BINDING | ISCHEMIA-MODIFIED ALBUMIN | PLASMA-PROTEIN-BINDING | PERFORMANCE LIQUID-CHROMATOGRAPHY | HIGH-LEVEL SECRETION | ALPHA-FETOPROTEIN GENES | Recombinant Proteins - metabolism | Recombinant Proteins - therapeutic use | Serum Albumin - therapeutic use | Humans | Serum Albumin - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Serum Albumin - chemistry | Serum Albumin - metabolism | Myoglobin | Atomic force microscopy | RNA | Prosthesis | Low density lipoproteins | Phthalocyanins | Postmenopausal women | Thioredoxin | Proteins | Iron compounds | Messenger RNA | Vitamin D | Heme | Thyroxine | Hemoglobin | Blood lipids | Thyroid hormones | Alfacalcidol | Chromosomes | Protein binding | Antigens | Enzymes | Biological products | Liver diseases | Albumin | Calcifediol | Fatty acids | Rheumatoid factor | Implants, Artificial | Rheumatoid arthritis | Ferroalloys | CEA (Oncology)
Journal Article
Angewandte Chemie (International ed.), ISSN 1433-7851, 2019, Volume 58, Issue 8, pp. 2350 - 2354
Journal Article