Any process that stops, prevents or reduces the frequency, rate or extent of forward locomotion.

Any process that modulates the speed, mechanical force, or rhythm of the anterior movement of an organism.

Any process that activates or increases the frequency, rate or extent of forward locomotion.

Any process that modulates the frequency, rate or extent of heparan sulfate binding.

Any process that stops, prevents or reduces the frequency, rate or extent of heparan sulfate binding.

Any process that stops, prevents or reduces the frequency, rate or extent of backward locomotion.

Any process that modulates the speed, mechanical force, or rhythm of the posterior movement of an organism.

Any process that activates or increases the frequency, rate or extent of backward locomotion.

Any process that activates or increases the frequency, rate or extent of pentose-phosphate shunt.

Any process that modulates the frequency, rate or extent of the pentose-phosphate shunt, the process in which glucose is oxidized, coupled to NADPH synthesis.

Any process that modulates the frequency, rate or extent of heparan sulfate proteoglycan binding.

Any process that activates or increases the frequency, rate or extent of heparan sulfate binding.

Any process that stops, prevents or reduces the frequency, rate or extent of pentose-phosphate shunt.

Any process that stops, prevents or reduces the frequency, rate or extent of heparan sulfate proteoglycan binding.

Any process that activates or increases the frequency, rate or extent of heparan sulfate proteoglycan binding.

The aggregation, arrangement and bonding together of a set of components to form an intranuclear rod.

The development of the portion of the ureteric bud tube that contributes to the morphogenesis of the metanephros.

The development of the portion of the ureteric bud that contributes to the morphogenesis of the ureter. The ureter ureteric bud is the initial structure that forms the ureter.

Binding to a MH2 (MAD homology 2) protein domain. The MH2 domain is found at the carboxy-terminus of MAD related proteins such as Smads. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers.

Binding to a MH1 (MAD homology 1) protein domain. The MH1 domain is found at the amino terminus of MAD related proteins such as Smads and can mediate DNA binding in some proteins. Smads also use the MH1 domain to interact with some transcription factors.