Welcome to the CFG Paradigm Pages - Revision history

Anna Crie at 12:25, 23 July 2011

2011-07-23T12:25:27Z

Anna Crie: moved Main Page to Welcome to the CFG Paradigm Pages

2011-07-23T12:20:34Z

moved Main Page to Welcome to the CFG Paradigm Pages

Kurt Drickamer: /* C-type Lectins */

2011-03-18T09:42:16Z

C-type Lectins

Carole Weaver at 18:01, 13 August 2010

2010-08-13T18:01:29Z

Carole Weaver at 17:53, 13 August 2010

2010-08-13T17:53:39Z

Carole Weaver at 17:53, 13 August 2010

2010-08-13T17:53:15Z

Carole Weaver: /* Bacterial Adhesins and Lectins */

2010-08-06T17:42:36Z

Bacterial Adhesins and Lectins

Anna Crie: /* GBPs Mediating Intracellular Trafficking & Other Mammalian GBPs */

2010-07-29T14:07:56Z

GBPs Mediating Intracellular Trafficking & Other Mammalian GBPs

Anna Crie: /* Galectins */

2010-05-13T21:51:17Z

Galectins

Anna Crie: /* Galectins */

2010-05-13T17:10:22Z

Galectins

@@ Line 1: / Line 1: @@
-'''Welcome to the CFG Paradigm Pages!'''<br>
 The Paradigm Pages were created by the Consortium for Functional Glycomics (CFG) to offer detailed information about 30 exemplary “Paradigm” glycan binding proteins (GBPs) that together encompass nine GBP families studied by the CFG. Each Paradigm GBP is representative of many other GBPs in its family and has clear biological functions that have become better understood through the use of CFG resources. The wiki-based Paradigm Pages are designed to track the progress of the CFG towards our goal to “define paradigms by which protein-carbohydrate interactions mediate cell communication.” CFG investigators are invited to upload and edit information about known progress in understanding each of these Paradigms, with a specific focus on how CFG resources have contributed to progress. To visit the Paradigm Page for each of the selected GBPs, follow the links below.
 <br><br>

@@ Line 6: / Line 6: @@
 <br>
 == C-type Lectins ==
-[[Image:Ctype.jpg|left|alt text]]
+[[Image:C-type lectin.jpg|left|alt text]]
 The C-type lectin family consists of proteins with diverse overall organization that contain structurally related carbohydrate-recognition domains. Although they generally share a common mechanism for interacting with sugars through a bound calcium ion, the spectrum of ligands bound by different members of the family is diverse and can include both endogenous mammalian oligosaccharides as well a sugar-containing structures on pathogenic micro-organisms. The biological functions of the C-type lectins are correspondingly diverse, but many of the best understood examples are membrane receptors found on the surface of cells of the immune system, which mediate interactions of these cells with each other and with viruses, bacteria, fungi and parasites, while other members of the family are soluble mediators of innate immunity. Outside the immune system, members of this group participate in clearance of circulating glycoproteins.

@@ Line 1: / Line 1: @@
 '''Welcome to the CFG Paradigm Pages!'''<br>
-The Paradigm Pages were created by the Consortium for Functional Glycomics (CFG) to offer detailed information about 30 exemplary “Paradigm” glycan binding proteins (GBPs) that together encompass nine GBP families studied by the CFG. Each Paradigm GBP is representative of many other GBPs in its family and has clear biological functions that have become better understood through the use of CFG resources. The Paradigm Pages are designed to track the progress of the CFG towards our goal to “define paradigms by which protein-carbohydrate interactions mediate cell communication.” Follow the links below to visit the Paradigm Page for each of the selected GBPs. CFG investigators are invited to upload and edit information about known progress in understanding each of these Paradigms, with a specific focus on how CFG resources have contributed to progress.
+The Paradigm Pages were created by the Consortium for Functional Glycomics (CFG) to offer detailed information about 30 exemplary “Paradigm” glycan binding proteins (GBPs) that together encompass nine GBP families studied by the CFG. Each Paradigm GBP is representative of many other GBPs in its family and has clear biological functions that have become better understood through the use of CFG resources. The wiki-based Paradigm Pages are designed to track the progress of the CFG towards our goal to “define paradigms by which protein-carbohydrate interactions mediate cell communication.” CFG investigators are invited to upload and edit information about known progress in understanding each of these Paradigms, with a specific focus on how CFG resources have contributed to progress. To visit the Paradigm Page for each of the selected GBPs, follow the links below.
 <br><br>
-Before you begin, please read these [http://www.functionalglycomics.org/static/consortium/CFGParadigm.shtml instructions].
+To contribute, please read these [http://www.functionalglycomics.org/static/consortium/CFGParadigm.shtml instructions].
 <br>
 <br>

@@ Line 1: / Line 1: @@
-'''Welcome to the Paradigm Pages!'''<br>
+'''Welcome to the CFG Paradigm Pages!'''<br>
 The Paradigm Pages were created by the Consortium for Functional Glycomics (CFG) to offer detailed information about 30 exemplary “Paradigm” glycan binding proteins (GBPs) that together encompass nine GBP families studied by the CFG. Each Paradigm GBP is representative of many other GBPs in its family and has clear biological functions that have become better understood through the use of CFG resources. The Paradigm Pages are designed to track the progress of the CFG towards our goal to “define paradigms by which protein-carbohydrate interactions mediate cell communication.” Follow the links below to visit the Paradigm Page for each of the selected GBPs. CFG investigators are invited to upload and edit information about known progress in understanding each of these Paradigms, with a specific focus on how CFG resources have contributed to progress.
 <br><br>
 Before you begin, please read these [http://www.functionalglycomics.org/static/consortium/CFGParadigm.shtml instructions].

@@ Line 1: / Line 1: @@
-'''The CFG Paradigms'''
+'''Welcome to the Paradigm Pages!'''<br>
+The Paradigm Pages were created by the Consortium for Functional Glycomics (CFG) to offer detailed information about 30 exemplary “Paradigm” glycan binding proteins (GBPs) that together encompass nine GBP families studied by the CFG. Each Paradigm GBP is representative of many other GBPs in its family and has clear biological functions that have become better understood through the use of CFG resources. The Paradigm Pages are designed to track the progress of the CFG towards our goal to “define paradigms by which protein-carbohydrate interactions mediate cell communication.” Follow the links below to visit the Paradigm Page for each of the selected GBPs. CFG investigators are invited to upload and edit information about known progress in understanding each of these Paradigms, with a specific focus on how CFG resources have contributed to progress.
-The purpose of this section of the CFG database is to document the success of the CFG in achieving its overall goal to 'define paradigms by which protein-carbohydrate interactions mediate cell communication.' Below are the paradigms chosen by the CFG steering committee, subgroup leaders, and other participating investigators to represent each of the major classes of glycan-binding proteins (GBPs). Follow the links to each paradigm for more information and to contribute to a Wiki page describing how the CFG and its PIs have contributed to the understanding of that GBP.
+<br><br>
 Before you begin, please read these [http://www.functionalglycomics.org/static/consortium/CFGParadigm.shtml instructions].
 <br>

← Older revision	Revision as of 12:20, 23 July 2011
(No difference)

@@ Line 51: / Line 51: @@
 [[Image:AdhesinsBacterial.jpg|left|alt text]]
-Infection by bacteria is generally initiated by the specific recognition of host epithelial surfaces by adhesins and lectins. The GBP are therefore virulent factors that play a role in the first step of adhesion and invasion. The GBP are called adhesins when they are part of organelles, such as fimbriae and flagella. They are referred to as lectins when they are soluble, and lectin-domain when attached to other proteins, that are often hydrolytic enzymes also involved in the infection process. The human targets for bacterial adhesins and lectins are mostly fucosylated human histo-blood group and/or sialylated epitopes. Defining the biological role of bacterial adhesins and lectins together with their structure and specificity is a prerequisite for the development of strategies for inhibiting their binding to human tissues.
+Infection by bacteria is generally initiated by the specific recognition of host epithelial surfaces by adhesins and lectins. These GBPs are therefore virulence factors that play a role in the first step of adhesion and invasion. The GBPs are called adhesins when they are part of organelles, such as fimbriae and flagella. They are referred to as lectins when they are soluble, and lectin-domain when attached to other proteins, which are often hydrolytic enzymes also involved in the infection process. The human targets for bacterial adhesins and lectins are mostly fucosylated human histo-blood group and/or sialylated epitopes. Defining the biological role of bacterial adhesins and lectins together with their structure and specificity is a prerequisite for the development of strategies for inhibiting their binding to human tissues.
 <li>Paradigm 1: [[PA-IIL]]
 <li>Paradigm 2: [[CBM47]]

@@ Line 41: / Line 41: @@
 == GBPs Mediating Intracellular Trafficking & Other Mammalian GBPs ==
 [[Image:CIMPR.jpg|left|alt text]]
-<br>
 Both calreticulin and the cation-dependent mannose-6-phosphate receptor are glycan-binding proteins recognizing discrete and specific carbohydrates involved in intracellular trafficking of membrane and secretory glycoproteins. In the case of calreticulin, glycan binding is associated with the quality control apparatus ensuring that only properly folded proteins will exit the endoplasmic reticulum. In the case of the cation-dependent mannose-6-phosphate receptor, phosphorylated mannose residues are recognized, allowing lysosomal proteins to be properly targeted. These paradigms are important for understanding diseases of protein misfolding and many lysosomal storage disorders. The ficolins are a class of glycan-binding proteins with affinity for N-acetyl residues that have distinct fold from other known lectins yet mediate pathogen recognition. Polymorphisms in ficoloin genes may also have pathophysiological implications.
 <li>Paradigm 1: [[Cation-dependent Mannose-6-phosphate receptor]]

@@ Line 27: / Line 27: @@
 <li>Paradigm 3: [[Galectin-9]]
 <br><br>
 == Siglecs ==