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Books on the topic 'Metalloproteasi'

Author: Grafiati

Published: 9 March 2023

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1

Galea, Charles A., ed. Matrix Metalloproteases. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6863-3.

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2

M, Hooper N., ed. Zinc metalloproteases in health and disease. London: Taylor & Francis, 1996.

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3

Bambai, Bijan. Purification, cloning, and expression of Cobrin: A C3-cleaving metalloprotease from venom of cobra (Naja naja kaouthia). Hamburg: Ad fontes Verlag, 1998.

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4

Webster, Ellis Lorenzo. Analysis of tissue inhibitor of metalloproteases (TIMP) as the unifying entity in the etiology of abdominal aortic aneurysms. [S.l: s.n.], 1991.

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5

Vincent, Lagente, and Boichot Elisabeth, eds. Matrix metalloproteinases in tissue remodelling and inflammation. Basel: Birkhäuser, 2008.

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6

Astrid, Sigel, and Sigel Helmut, eds. Probing of proteins by metal ions and their low-molecular-weight complexes. New York: Marcel Dekker, 2001.

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7

O, Hill H. A., Sadler P. J, Thomson A. J, and Auld D. S, eds. Metal sites in proteins and models. Berlin: Springer, 1997.

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8

1943-, Greenwald Robert A., Golub Lorne M, and New York Academy of Sciences., eds. Inhibition of matrix metalloproteinases: Therapeutic potential. New York, N.Y: New York Academy of Sciences, 1994.

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9

F, Riordan James, and Vallee Bert L, eds. Metallobiochemistry. San Diego: Academic Press, 1988.

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10

O, Hill H. A., Sadler P. J, and Thompson A. J, eds. Metal sites in proteins and models: Redox centres. Berlin: Springer, 1998.

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11

Hooper. Zinc Metalloproteasea Heal Dis. Taylor & Francis Books Ltd, 1995.

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12

Galea, Charles A. Matrix Metalloproteases: Methods and Protocols. Springer New York, 2018.

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13

Vacca, Joseph P., Gerd Folkers, Raimund Mannhold, and Hugo Kubinyi. Proteases as Drug Targets: Metalloproteases. Wiley & Sons, Incorporated, John, 2010.

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14

Galea, Charles A. Matrix Metalloproteases: Methods and Protocols. Springer New York, 2017.

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15

Zinc Metalloproteases In Health And Disease. Routledge, 2002. http://dx.doi.org/10.4324/9780203483138.

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16

Hooper, NM. Zinc Metalloproteases In Health And Disease. CRC, 1996.

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17

Hooper, N. M. Zinc Metalloproteases in Health and Disease. Taylor & Francis Group, 1996.

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18

Hooper, N. M. Zinc Metalloproteases in Health and Disease. Taylor & Francis Group, 1996.

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19

Hooper, N. M. Zinc Metalloproteases in Health and Disease. Taylor & Francis Group, 1996.

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20

Fry, Jessica Lynn. ADAM9 metalloproteases and breast cancer cell migration. 2010.

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21

(Editor), Astrid Sigel, and Helmut Sigel (Editor), eds. Metal Ions in Biological Systems Volume 38 (Metal Ions in Biological Systems). CRC, 2001.

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22

Noris, Marina, and Tim Goodship. The patient with haemolytic uraemic syndrome/thrombotic thrombocytopenic purpura. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0174.

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Abstract:

The patient who presents with microangiopathic haemolytic anaemia, thrombocytopenia, and evidence of acute kidney injury presents a diagnostic and management challenge. Haemolytic uraemic syndrome (HUS) and thrombotic thrombocytopenic purpura (TTP) are two of the conditions that frequently present with this triad. They are characterized by low platelet count with normal or near-normal coagulation tests, anaemia, and signs of intravascular red cell fragmentation on blood films, and high LDH levels.HUS associated with shiga-like toxins produced usually by E.coli (typically O157 strains) may occur in outbreaks or sporadically, with geographical variations in incidence. It is predominantly a disease of young children in which painful blood diarrhoea in a minority of infected patients is succeeded by microangiopathy and acute kidney injury. Management is supportive and recovery is usual, although permanent renal damage may lead to later deterioration. Older patients may be affected and tend to have worse outcomes. Neuraminidase-producing Streptococcus pneumoniae infections (usually pneumonia) very rarely cause a similar HUS.Atypical HUS occurs sporadically and is increasingly associated with defects in the regulation of the complement pathway, either genetic or autoimmune-caused. It may respond to plasma exchange for fresh frozen plasma. Recurrences are common, including after transplantation.TTP is associated with more neurological disease and less renal involvement, but HUS and TTP overlap substantially in their manifestations. The underlying problem is in von Willebrand factor (vWF) cleavage. The plasma metalloprotease ADAMTS13 is responsible for cleaving vWF multimers, a process that is important to prevent thrombosis in the microvasculature. Autoantibodies or rarely genetic deficiency may impair this process. Plasma exchange may remove antibodies and replenish the protease.

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23

Metallobiochemistry, Part A, Volume 158: Volume 158: Metabiochemistry Part A (Methods in Enzymology). Academic Press, 1988.

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24

(Editor), Robert A. Greenwald, New York Academy of Sciences (Corporate Author), and Lorne M. Golub (Editor), eds. Inhibition of Matrix Metalloproteinases: Therapeutic Potential (Annals of the New York Academy of Sciences, Vol 732). New York Academy of Sciences, 1994.

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25

(Editor), Robert A. Greenwald, New York Academy of Sciences (Corporate Author), and Lorne M. Golub (Editor), eds. Inhibition of Matrix Metalloproteinases: Therapeutic Potential (Annals of the New York Academy of Sciences). New York Academy of Sciences, 1994.

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26

(Editor), John N. Abelson, Melvin I. Simon (Editor), James F. Riordan (Editor), and Bert L. Vallee (Editor), eds. Metallobiochemistry, Part A, Volume 158: Volume 158: Metabiochemistry Part A (Methods in Enzymology). Academic Press, 1988.

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